P R O T E I N S E Q U E N C E D A T A B A S E of PIR-International Release 70.03, November 09, 2001 262525 sequences, 89717977 residues Protein Information Resource (PIR)* National Biomedical Research Foundation 3900 Reservoir Road, N.W., Washington, DC 20007, USA Japan International Protein Munich Information Center for Information Database (JIPID) Protein Sequences (MIPS) Amakubo 1-16-1 GSF-Forschungszentrum f. Umwelt und Gesundheit Tsukuba 305-0005, Japan am Max-Planck-Instut f. Biochemie Am Klopferspitz 18, D-82152 Martinsried, FRG This database may be redistributed without prior consent, provided that this notice be given to each user and that the words "Derived from" shall precede this notice if the database has been altered by the redistributor. Copyright 2000, PIR-International. *PIR is a registered mark of NBRF.
CCHU A31764 A05676 I55192 A00001 24-Apr-1984 30-Sep-1991 28-Jul-2000
cytochrome c [validated] human man Homo sapiens Evans, M.J. Scarpulla, R.C. Proc. Natl. Acad. Sci. U.S.A. 8519889625-9629 The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution. MUID89071748 A31764 DNA 1-105 GBM22877 NIDg181241 PIDNAAA35732.1 PIDg181242 Matsubara, H. Smith, E.L. J. Biol. Chem. 23819632732-2753 Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, and the complete amino acid sequence. A05676 protein 2-28;29-46;47-100;101-105 Matsubara, H. Smith, E.L. J. Biol. Chem. 23719623575-3576 The amino acid sequence of human heart cytochrome c. annotation 66-Leu is found in 10% of the molecules in pooled protein Tanaka, Y. Ashikari, T. Shibano, Y. Amachi, T. Yoshizumi, H. Matsubara, H. J. Biochem. 1031988954-961 Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae. MUID89008207 I55192 translated from GB/EMBL/DDBJ mRNA 78-105 GBD00265 NIDg2897691 PIDNBAA00187.1 PIDg219557 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation polymorphism respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIW GEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCCZ A00002 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c chimpanzee chimpanzee Pan troglodytes Needleman, S.B. submitted to the Atlas October1968 A00002 protein 1-104 Needleman, S.B. Margoliash, E. unpublished results, 1966, cited by Margoliash, E., and Fitch, W.M., Ann. N.Y. Acad. Sci. 151, 359-381 1968 annotation compositions of chymotryptic peptides cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWG EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMQR A00003 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c rhesus macaque rhesus macaque Macaca mulatta Rothfus, J.A. Smith, E.L. J. Biol. Chem. 24019654277-4283 Amino acid sequence of rhesus monkey heart cytochrome c. MUID66045191 compositions of chymotryptic peptides sequences of residues 55-61 and 68-70 A00003 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGITWG EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMKP A00004 17-Dec-1982 17-Dec-1982 03-Mar-2000
cytochrome c spider monkey spider monkey Ateles sp. Margoliash, E. unpublished results, cited by Shelnutt, J.A., Rousseau, D.L., Dethmers, J.K., and Margoliash, E., Biochemistry 20, 6485-6497 1981 A00004 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVFKGKRIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQASGFTYTEANKNKGIIWG EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMS A23057 A04604 A00009 31-Dec-1990 30-Sep-1991 28-Jul-2000
cytochrome c [validated] mouse house mouse Mus musculus Limbach, K.J. Wu, R. Nucleic Acids Res. 131985617-630 Characterization of a mouse somatic cytochrome c gene and three cytochrome c pseudogenes. MUID85215501 A23057 DNA 1-105 EMBLX01756 NIDg50618 PIDNCAA25899.1 PIDg50619 strain BALB/c Carlson, S.S. Mross, G.A. Wilson, A.C. Mead, R.T. Wolin, L.D. Bowers, S.F. Foley, N.T. Muijsers, A.O. Margoliash, E. Biochemistry 1619771437-1442 Primary structure of mouse, rat, and guinea pig cytochrome c. MUID77134768 A04604 protein 2-105 strain BALB/c 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITW GEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCRT A04605 C28160 A00009 31-Dec-1990 30-Sep-1991 28-Jul-2000
cytochrome c [validated] rat Norway rat Rattus norvegicus Scarpulla, R.C. Agne, K.M. Wu, R. J. Biol. Chem. 25619816480-6486 Isolation and structure of a rat cytochrome c gene. MUID81215609 A04605 DNA 1-105 GBK00750 GBM28216 NIDg550511 PIDNAAA21711.1 PIDg203699 Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 26319886791-6796 Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants. MUID88198250 C28160 mRNA 1-105 GBM20622 NIDg203722 PIDNAAA41014.1 PIDg203723 Carlson, S.S. Mross, G.A. Wilson, A.C. Mead, R.T. Wolin, L.D. Bowers, S.F. Foley, N.T. Muijsers, A.O. Margoliash, E. Biochemistry 1619771437-1442 Primary structure of mouse, rat, and guinea pig cytochrome c. MUID77134768 annotation peptide mapping, compositional analysis, and partial sequencing indicate that rat cytochrome c is identical with that of mouse 57/1 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site blocked amino end (Gly) (in mature form) (probably acetylated) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITW GEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCRB A00009 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] rabbit domestic rabbit Oryctolagus cuniculus Needleman, S.B. Margoliash, E. J. Biol. Chem. 2411966853-863 Rabbit heart cytochrome c. MUID66093127 A00009 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKDERADLIAYLKKATNE
CCGW A04608 A00009 31-Dec-1990 31-Dec-1990 28-Jul-2000
cytochrome c [validated] guanaco guanaco Lama guanicoe Niece, R.L. Margoliash, E. Fitch, W.M. Biochemistry 16197768-72 Complete amino acid sequence of guanaco (Lama guanicoe) cytochrome c. MUID77087753 A04608 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCCM A04607 A00009 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c Arabian camel Arabian camel Camelus dromedarius Sokolovsky, M. Moldovan, M. Biochemistry 111972145-149 Primary structure of cytochrome c from the camel, Camelus dromedarius. MUID72096652 A04607 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCWHC A04606 A00009 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c California gray whale California gray whale Eschrichtius robustus, Eschrichtius gibbosus Goldstone, A. Smith, E.L. J. Biol. Chem. 24119664480-4486 Amino acid sequence of whale heart cytochrome c. MUID67041932 A04606 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCPG A00007 17-Mar-1987 17-Mar-1987 28-Jul-2000
cytochrome c [validated] pig domestic pig Sus scrofa domestica Stewart, J.W. Margoliash, E. Can. J. Biochem. 4319651187-1206 The primary structure of the cytochrome c from various organs of the hog. MUID66072936 A00007 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCBO A92022 A00007 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c bovine cattle Bos primigenius taurus Nakashima, T. Higa, H. Matsubara, H. Benson, A. Yasunobu, K.T. J. Biol. Chem. 24119661166-1177 The amino acid sequence of bovine heart cytochrome c. MUID66132521 A92022 protein 1-104 Tsunasawa, S. Narita, K. J. Biochem. 921982607-613 Micro-identification of amino-terminal acetylamino acids in proteins. MUID83056735 annotation acetylation cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCSH A91454 A00007 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c sheep domestic sheep Ovis orientalis aries, Ovis ammon aries Smith, E.L. Margoliash, E. Fed. Proc. 2319641243-1247 Evolution of cytochrome c. A91454 protein 1-104 amino acid compositions and mobilities of tryptic and chymotryptic peptides were determined cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCHOD A00006 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c donkey donkey Equus asinus Walasek, O.F. Margoliash, E. J. Biol. Chem. 2521977830-834 Transmission of the cytochrome c structural gene in horse-donkey crosses. MUID77118552 A00006 protein 1-104 compositions of chymotryptic peptides and the sequence of residues 47-48 were determined mules and hinnies are heterozygous, having equal amounts of horse and donkey cytochromes c cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
CCHOZ A91330 A00006 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c common zebra common zebra, plains zebra Equus burchelli, Equus quagga Guertler, L. Horstmann, H.J. FEBS Lett. 181971106-108 Zur Primaerstruktur des Cytochromes c des Steppenzebras (Equus quagga boehmi). A91330 protein 1-104 the amino acid composition and the sequence of residues 40-48 were determined cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
CCHO A00005 S59487 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] horse domestic horse Equus caballus Margoliash, E. Smith, E.L. Kreil, G. Tuppy, H. Nature 19219611125-1127 The complete amino-acid sequence. A00005 protein 1-104 Theodorakis, J.L. Armes, L.G. Margoliash, E. Biochim. Biophys. Acta 12521995114-125 beta-Thiopropionyl cytochromes c modified at lysyl residues: preparation and characterization of the monosubstituted horse cytochromes c. MUID96001358 S59487 preliminary protein 1-10;11-18;19-26;27-34;38-47;50-54;55-58;60-67;68-74;75-82;83-97;98-104 Luo, Y. Brayer, G.D. submitted to the Brookhaven Protein Data Bank August1994 PDB1HRC annotation X-ray crystallography, 1.9 angstroms, residues 1-104 Dickerson, R.E. Takano, T. Eisenberg, D. Kallai, O.B. Samson, L. Cooper, A. Margoliash, E. J. Biol. Chem. 24619711511-1533 Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. MUID71116428 annotation X-ray crystallography, 2.8 angstroms cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 experimental 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
CCHP A00008 19-Feb-1984 19-Feb-1984 03-Mar-2000
cytochrome c hippopotamus hippopotamus Hippopotamus amphibius Thompson, R.B. Borden, D. Tarr, G.E. Margoliash, E. J. Biol. Chem. 25319788957-8961 Heterogeneity of amino acid sequence in hippopotamus cytochrome c. MUID79067782 A00008 protein 1-104 3-Ile was also found cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQSPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKQATNE
CCDG A00010 13-Jul-1981 13-Jul-1981 31-Mar-2000
cytochrome c dog dog Canis lupus familiaris McDowall, M.A. Smith, E.L. J. Biol. Chem. 24019654635-4647 Amino acid sequence of dog heart cytochrome c. MUID66047448 A00010 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQK(C.A.Q.C.H.T.V.E)KGGKHKTGPNLHGLFGRKTGQAPGFSYTDA NKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKKATKE
CCSLE A04615 A00010 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c southern elephant seal southern elephant seal Mirounga leonina Augusteyn, R.C. McDowall, M.A. Webb, E.C. Zerner, B. Biochim. Biophys. Acta 2571972264-272 Primary structure of cytochrome c from the elephant seal, Mirounga leonina. MUID72170090 A04615 protein 1-104 peptides were positioned by homology cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKIATKE
CCBTS A04614 A00010 31-Dec-1990 31-Dec-1990 11-May-2000
cytochrome c Schreibers's long-fingered bat Schreibers's long-fingered bat Miniopterus schreibersi Strydom, D.J. van der Walt, S.J. Botes, D.P. Comp. Biochem. Physiol. B 43197221-24 The amino acid sequence of bat (Miniopteris schreibersi) cytochrome c. MUID73123526 A04614 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EATLMEYLENPKKYIPGTKMIFAGIKKSAERADLIAYLKKATKE
CCKGG A00011 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] eastern gray kangaroo eastern gray kangaroo Macropus giganteus Nolan, C. Margoliash, E. J. Biol. Chem. 24119661049-1059 Primary structure of the cytochrome c from the great grey kangaroo, Macropus canguru. MUID66132505 A00011 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLNGIFGRKTGQAPGFTYTDANKNKGIIWG EDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCMST B28160 A00012 I48313 24-Apr-1984 30-Sep-1991 28-Jul-2000
cytochrome c, testis-specific [validated] cytochrome c T mouse house mouse Mus musculus Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 26319886791-6796 Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants. MUID88198250 B28160 mRNA 1-105 GBM20625 NIDg192875 PIDNAAA37501.1 PIDg309203 Hennig, B. Eur. J. Biochem. 551975167-183 Change of cytochrome c structure during development of the mouse. MUID76022386 A00012 protein 2-57,'IV',60-61,'ZZ',64-66,'Z',68-69,'ZB',72-105 strain BALB/c Hake, L.E. Alcivar, A.A. Hecht, N.B. Development 1101990249-257 Changes in mRNA length accompany translational regulation of the somatic and testis-specific cytochrome c genes during spermatogenesis in the mouse. MUID91184013 I48313 translated from GB/EMBL/DDBJ mRNA 1-105 EMBLX55771 NIDg288155 PIDNCAA39293.1 PIDg288156 Mammalian testis contains two forms of cytochrome c, one identical with the form found in somatic tissues and another that is expressed in a stage-specific manner during spermatogenic differentiation. cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain sperm testis product cytochrome c, testis-specific 2-105 experimental domain cytochrome c homology 5-99 modified-site blocked amino end (Gly) (in mature form) (probably acetylated) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDAEAGKKIFVQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIW SEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIKYLKQATSS
CCRTT A28160 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c, testis-specific rat Norway rat Rattus norvegicus Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 26319886791-6796 Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants. MUID88198250 A28160 DNA mRNA 1-105 GBM20627 GBM20628 NIDg203727 PIDNAAA41015.1 PIDg203729 GBM20623 NIDg203730 PIDg203731 Mammalian testis contains two forms of cytochrome c, one identical to the form found in somatic tissues and another that is expressed in a stage-specific manner during spermatogenic differentiation. 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain sperm testis product cytochrome c, testis-specific 2-105 predicted domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 predicted binding-site heme (Cys) (covalent) 15,18 predicted binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDAEAGKKIFIQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIW TEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIQYLKEATSS
CCPY A00013 04-Dec-1986 04-Dec-1986 03-Mar-2000
cytochrome c pigeon domestic pigeon Columba livia Chan, S.K. Tulloss, I. Margoliash, E. unpublished results, cited by Wojciech, R., and Margoliash, E., in Handbook of Biochemistry, Sober, H.A., ed., pp.C158-C161, Chemical Rubber Co., Cleveland 1968 A00013 protein 1-104 compositions of tryptic peptides and sequences of residues 89-91, 92-99, and 100-104 were determined cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKAERADLIAYLKQATAK
CCCH A00014 A04611 24-Apr-1984 20-Aug-1994 28-Jul-2000
cytochrome c [validated] chicken chicken Gallus gallus Limbach, K.J. Wu, R. Nucleic Acids Res. 1119838931-8950 Isolation and characterization of two alleles of the chicken cytochrome c gene. MUID84169527 A00014 DNA 1-105 GBK02303 NIDg211708 PIDNAAA48741.1 PIDg211709 Chan, S.K. Margoliash, E. J. Biol. Chem. 2411966507-515 Amino acid sequence of chicken heart cytochrome. MUID66080352 A04611 protein 2-105 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITW GEDTLMEYLENPKKYIPGTKMIFAGIKKKSERVDLIAYLKDATSK
CCTK A04612 A00014 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c turkey common turkey Meleagris gallopavo Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas June1966 A04612 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERVDLIAYLKDATSK
CCDK A00015 04-Dec-1986 04-Dec-1986 03-Mar-2000
cytochrome c duck domestic duck Anas platyrhynchos Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas June1966 compositions of tryptic peptides sequences of residues 1-5, 92-99, and 100-104 A00015 protein 1-104 Pekin breed cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATAK
CCOS A00016 04-Dec-1986 04-Dec-1986 28-Jul-2000
cytochrome c [validated] ostrich ostrich Struthio camelus Howard, N.L. Joubert, F.J. Strydom, D.J. Comp. Biochem. Physiol. B 48197475-85 The amino acid sequence of ostrich (Struthio camelus) cytochrome C. MUID74175476 A00016 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLDGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
CCEU A00017 04-Dec-1986 04-Dec-1986 28-Jul-2000
cytochrome c [validated] emu emu Dromaius novaehollandiae Augusteyn, R.C. Biochim. Biophys. Acta 30319731-7 Primary structure of cytochrome c from the emu, Dromaeus novaehollandiae. MUID73171069 A00017 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLNGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
CCPN A00018 04-Dec-1986 04-Dec-1986 03-Mar-2000
cytochrome c king penguin king penguin Aptenodytes patagonicus Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas July1967 A00018 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGIFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
CCST A00019 24-Apr-1984 30-Sep-1988 31-Mar-2000
cytochrome c snapping turtle snapping turtle Chelydra serpentina Chan, S.K. Tulloss, I. Margoliash, E. Biochemistry 519662586-2597 Primary structure of the cytochrome c from the snapping turtle, Chelydra serpentina. MUID67172948 A00019 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEK.GKKIF.VQKCAQCHTVEKGGKH.KTGPNLNGL.IGRKTGQAEGF.SYTEANKN. KGITWG.EETLM.EY.LENPKKY.IPGTKM.IF.AGIKKKAERADL.IAY.LKDATSK
CCFG A00021 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c bullfrog bullfrog Rana catesbeiana Chan, S.K. Walasek, O.F. Barlow, G.H. Margoliash, E. submitted to the Atlas July1967 A00021 protein 1-104 The presence of Lys-104 is not certain. We have arranged the amino acids in positions 88-92 by homology with the other cytochrome c sequences. This arrangement is contrary to the authors'. cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted disulfide-bonds 20-102 experimental 104 complete tentative GDVEKGKKIF(V,Q.K.C.A.Q.C.H.T.C,E.K.G.G.K.H)KVGPNLYGLIGRKTGQA AGFSYTDANKNKGITW(G.E,D,T.L.M.E.Y)LENPKKYIPGTKMIFAGI(K.K.K.G. E.R.Q)DLIAY(L.K.S,A,C,S,K)
CCBN A00022 13-Jul-1981 10-Oct-1997 28-Jul-2000
cytochrome c [validated] skipjack tuna skipjack tuna Euthynnus pelamis, Katsuwonus pelamis Nakayama, T. Titani, K. Narita, K. J. Biochem. 701971311-326 The amino acid sequence of cytochrome c from bonito (Katsuwonus pelamis, Linnaeus). MUID72003272 A00022 protein 1-103 Tanaka, N. Yamane, T. Tsukihara, T. Ashida, T. Kakudo, M. submitted to the Brookhaven Protein Data Bank August1976 PDB1CYC annotation X-ray crystallography, 2.3 angstroms, residues 1-103 Tanaka, N. Yamane, T. Tsukihara, T. Ashida, T. Kakudo, M. J. Biochem. 771975147-162 The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function. MUID75170243 annotation X-ray crystallography, reduced form, 2.3 angstroms Matsuura, Y. Hata, Y. Yamaguchi, T. Tanaka, N. Kakudo, M. J. Biochem. 851979729-737 Structure of bonito heart ferricytochrome c and some remarks on molecular interaction in its crystalline state. MUID79150869 annotation X-ray crystallography, oxidized form, 2.8 angstroms Mandel, N. Mandel, G. Trus, B.L. Rosenburg, J. Carlson, G. Dickerson, R.E. J. Biol. Chem. 25219774619-4636 Tuna cytochrome c at 2.0 A resolution. III. Coordinate optimization and comparison of structures. MUID77207068 annotation commercial Scombridae, X-ray crystallography, oxidized and reduced forms, 2.0 angstroms this is the final paper in a series cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 experimental 103 complete GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKTGQAEGYSYTDANKSKGIVWN ENTLMEYLENPKKYIPGTKMIFAGIKKKGERQDLVAYLKSATS
CCCA A00023 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c common carp common carp Cyprinus carpio Guertler, L. Horstmann, H.J. Eur. J. Biochem. 12197048-57 Die Aminosaeure-sequenz vom Cytochrom c des Karpfens, Cyprinus carpio. MUID70137310 A00023 protein 1-103 the sequence of iso-2-cytochrome c differs from that shown in having 4-Asp the protein was obtained from food carp that consisted of two cross-bred strains, the European carp and the Amur carp the isocytochromes may be the result of strain differences The sequence shown is iso-1-cytochrome c. cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 103 complete tentative GDVEK.GKK.VFVQK.CAQCHTVZBGGK.HK.VGPNLWGLFGRK.TGQAPGFSYTBABK. SK.GIVWBZZTLMEYLZBPK.KYIPGTK.MIFAGIK.KKGER.ADLIAYLK.SATS
CCDF A00024 23-Oct-1981 23-Oct-1981 28-Jul-2000
cytochrome c [validated] Puget Sound dogfish Puget Sound dogfish Squalus sucklii Goldstone, A. Smith, E.L. J. Biol. Chem. 24219674702-4710 Amino acid sequence of the cytochrome c from the dogfish, Squalus sucklii. MUID68054790 A00024 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKVFVQKCAQCHTVENGGKHKTGPNLSGLFGRKTGQAQGFSYTDANKSKGITWQ QETLRIYLENPKKYIPGTKMIFAGLKKKSERQDLIAYLKKTAAS
CCLM A00025 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] Pacific lamprey Pacific lamprey Lampetra tridentata, Entosphenus tridentatus Nolan, C. Fitch, W.M. Uzzell, T. Weiss, L.J. Margoliash, E. Biochemistry 1219734052-4060 Amino acid sequence of a cytochrome c from the common Pacific lamprey, Entosphenus tridentatus. MUID74011773 A00025 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKVFVQKCSQCHTVEKAGKHKTGPNLSGLFGRKTGQAPGFSYTDANKSKGIVWN QETLFVYLENPKKYIPGTKMIFAGIKKEGERKDLIAYLKKSTSE
CCRS A94624 A92021 A00020 19-Feb-1984 19-Feb-1984 03-Mar-2000
cytochrome c eastern diamondback rattlesnake eastern diamondback rattlesnake Crotalus adamanteus Ambler, R. submitted to the Protein Sequence Database January1984 A94624 protein 1-104 Bahl, O.P. Smith, E.L. J. Biol. Chem. 24019653585-3593 Amino acid sequence of rattlesnake heart cytochrome c. MUID66019642 A92021 protein 1-85,'SK',88-92,'N',94-100,'K',102-103,'A' cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFSMKCGTCHTVEEGGKHKTGPNLHGLFGRKTGQAVGYSYTAANKNKGIIWG DDTLMEYLENPKKYIPGTKMVFTGLKSKKERTDLIAYLKEATAK
CCRSW S14358 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c western rattlesnake western rattlesnake Crotalus viridis Ambler, R.P. Daniel, M. Biochem. J. 2741991825-831 Rattlesnake cytochrome c. A re-appraisal of the reported amino acid sequence. MUID91190099 S14358 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFSMKCGTCHTVEEGGKHKTGPNLHGLFGRKTGQAVGYSYTAANKNKGIIWG DDTLMEYLENPKKYIPGTKMVFTGLKSKKERTDLIAYLKEATAK
CCSF A00026 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c starfish (Asterias rubens) common European starfish Asterias rubens Lyddiatt, A. Boulter, D. FEBS Lett. 671976331-334 The amino acid sequence of cytochrome c from Asterias rubens L. (common starfish). MUID77003681 A00026 protein 1-103 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 103 complete tentative GQVEKGKKIFVQRCAQCHTVEKAGKHK.TGPNLNGILGRKTGQAAGFSYTDANRNKGITW K.NETLFEYLENPKKYIPGTKMVFAGLK.KQKERQDLIAYLEAATK
T32611 T32611 S13048 03-Mar-2000 03-Mar-2000 28-Jul-2000
cytochrome c [validated] protein E04A4.7 Caenorhabditis elegans Caenorhabditis elegans Sammons, L. Wohldmann, P. Biewald, T. submitted to the EMBL Data Library December1997 The sequence of C. elegans cosmid E04A4. T32611 translated from GB/EMBL/DDBJ DNA 1-111 EMBLAF038611 PIDNAAB92035.1 GSPDBGN00022 CESPE04A4.7 strain Bristol N2; clone E04A4 Vanfleteren, J.R. Evers, E.A.I.M. van de Werken, G. van Beeumen, J.J. Biochem. J. 2711990613-620 The primary structure of cytochrome c from the nematode Caenorhabditis elegans. MUID91058490 S13048 protein 2-65,'K',67-111 CESPE04A4.7 4 60/3 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion domain cytochrome c homology 10-103 modified-site acetylated amino end (Ser) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 20,23 experimental binding-site heme iron (His, Met) (axial ligands) 24,85 predicted 111 complete MSDIPAGDYEKGKKVYKQRCLQCHVVDSTATKTGPTLHGVIGRTSGTVSGFDYSAANKNK GVVWTRETLFEYLLNPKKYIPGTKMVFAGLKKADERADLIKYIEVESAKSL
T27492 T27492 03-Nov-2000 03-Nov-2000 03-Nov-2000
cytochrome c ZC116.2 Caenorhabditis elegans Caenorhabditis elegans Smye, R. submitted to the EMBL Data Library June1996 T27492 translated from GB/EMBL/DDBJ DNA 1-123 EMBLZ74046 PIDNCAA98555.1 GSPDBGN00023 CESPZC116.2 clone ZC116 CESPZC116.2 5 24/3; 94/3 cytochrome c cytochrome c homology chromoprotein heme iron metalloprotein domain cytochrome c homology 20-113 binding-site heme (Cys) (covalent) 30,33 predicted binding-site heme iron (His, Met) (axial ligands) 34,95 predicted 123 complete MGKKKSDTASGGAIPEGDNEKGKKIFKQRCEQCHVVNSLQTKTGPTLNGVIGRQSGQVAG FDYSAANKNKGVVWDRQTLFDYLADPKKYIPGTKMVFAGLKKADERADLIKFIEVEAAKK PSA
CCWB A00027 24-Apr-1984 01-Feb-1985 03-Mar-2000
cytochrome c earthworm (Eisenia foetida) common brandling worm, common dung-worm Eisenia foetida Lyddiatt, A. Boulter, D. FEBS Lett. 62197685-88 The amino acid sequence of cytochrome c from Eisenia foetida (Savigny) (common brandling worm). MUID76118291 A00027 protein 1-108 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 9-103 binding-site heme (Cys) (covalent) 19,22 predicted binding-site heme iron (His, Met) (axial ligands) 23,85 predicted 108 complete GGIPAGDVEKGKTIFKQRCAQCHTVDKGGPHKTGPNLHGIFGRATGQAAGFAYTDANKSK GITWTKDTLYEYLENPKKYIPGTKMVFAGLKNEKQRANLIAYLEQETK
CCMM A00028 24-Apr-1984 24-Apr-1984 11-May-2000
cytochrome c monsoon river-prawn monsoon river-prawn Macrobrachium malcolmsonii Lyddiatt, A. Boulter, D. Comp. Biochem. Physiol. B 551976337-342 A comparison of cytochrome C from Macrobrachium malcomsonii with other invertebrate cytochromes C. MUID77024998 A00028 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQRCAQCHSAQANLKHKTGPNLNGLFGRQTGQASGYVYTDANKAKGITWQ ADTLDVYLENPKKYIPGTKMVFAGLKKANERADLIAYLKQATNL
CCHA A00029 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] brown garden snail brown garden snail Helix aspersa Brown, R.H. Richardson, M. Boulter, D. Ramshaw, J.A.M. Jefferies, R.P.S. Biochem. J. 1281972971-974 The amino acid sequence of cytochrome c from Helix aspersa Mueller (garden snail). MUID73054484 A00029 protein 1-104 the amidation states of residues 16, 21, 52, 70, and 90 were assigned by homology with other cytochromes c cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GZAZKGKKIFTQKCLQCHTVEAGGKHKTGPNLSGLFGRKQGQAPGFAYTDANKGKGITWK NQTLFEYLENPKKYIPGTKMVFAGLKBZTERVHLIAYLZZATKK
CCFFCM A00030 13-Jul-1981 30-Jun-1991 03-Mar-2000
cytochrome c Mediterranean fruit fly Mediterranean fruit fly Ceratitis capitata Fernandez-Sousa, J.M. Gavilanes, J.G. Municio, A.M. Paredes, J.A. Perez-Aranda, A. Rodriguez, R. Biochim. Biophys. Acta 3931975358-367 Primary structure of cytochrome c from the insect Ceratitis capitata. MUID75205681 A00030 protein 1-107 some peptides were positioned by homology cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete GVPAGDVEKGKKLFVQRCAQCHTVEAGGKHKVGPNLHGLIGRKTGQAAGFAYTDANKAKG ITWNEDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
CCFFDM A22945 A23058 A25506 A38039 A00030 30-Jun-1991 20-Aug-1994 03-Mar-2000
cytochrome c DC4 fruit fly (Drosophila melanogaster) Drosophila melanogaster Swanson, M.S. Zieminn, S.M. Miller, D.D. Garber, E.A.E. Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. 8219851964-1968 Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c. MUID85166253 A22945 DNA 1-108 GBM11381 NIDg157160 PIDNAAA28437.1 PIDg157161 Limbach, K.J. Wu, R. Nucleic Acids Res. 131985631-644 Characterization of two Drosophila melanogaster cytochrome c genes and their transcripts. MUID85215502 A23058 DNA 1-108 GBX01760 NIDg7782 PIDNCAA25900.1 PIDg7783 Inoue, S. Inoue, H. Hiroyoshi, T. Matsubara, H. Yamanaka, T. J. Biochem. 1001986955-965 Developmental variation and amino acid sequences of cytochromes c of the fruit fly Drosophila melanogaster and the flesh fly Boettcherisca peregrina. MUID87137362 A25506 protein 2-108 Nolan, C. Weiss, L.J. Adams, J.J. Margoliash, E. unpublished results, cited by Wojciech, R., and Margoliash, E., in Handbook of Biochemistry, Sober, H.A., ed., pp.C160-C161, Chemical Rubber Co., Cleveland 1968 A38039 protein 2-54,'N',56-64,'QD',67-108 some peptides were positioned by homology This protein is expressed at varying, but relatively high levels throughout development. DC4 FlyBaseFBgn0000409 2 36A 10-11 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c DC4 2-108 experimental domain cytochrome c homology 9-103 binding-site heme (Cys) (covalent) 19,22 predicted binding-site heme iron (His, Met) (axial ligands) 23,85 predicted 108 complete MGVPAGDVEKGKKLFVQRCAQCHTVEAGGKHKVGPNLHGLIGRKTGQAAGFAYTDANKAK GITWNEDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
CCFHHF A38040 A00030 30-Jun-1991 30-Jun-1991 03-Mar-2000
cytochrome c horn fly horn fly Haematobia irritans Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas July1967 A38040 protein 1-107 some peptides were positioned by homology cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete GVPAGDVEKGKKIFVQRCAQCHTVEAGGKHKVGPNLHGLFGRKTGQAAGFAYTNANKAKG ITWQDDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
CCHFGB A38041 A00030 30-Jun-1991 30-Jun-1991 03-Mar-2000
cytochrome c greenbottle fly (Lucilia cuprina) Lucilia cuprina Shaw, D.C. Williams, K.L. Smith, E. Birt, L.M. Biochim. Biophys. Acta 5321978179-184 The amino acid sequence of cytochrome c from the blowfly Lucilia cuprina. MUID78080930 A38041 protein 1-107 the compositions of the tryptic peptides and the sequence of residues 44-49 were determined cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete tentative GVPAGDVEKGKKIFVQRCAQCHTVEAGGKHKVGPNLHGLFGRKTGQAPGFAYTNANKAKG ITWQDDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
CCLQ A00033 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c desert locust desert locust Schistocerca gregaria Lyddiatt, A. Boulter, D. Biochem. J. 1631977333-338 The amino acid sequence of cytochrome c from the locust, Schistocerca gregaria Forskal. MUID77201499 A00033 protein 1-107 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete GVPQGDVEKGKKIFVQRCAQCHTVEAGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKSKG ITWDENTLFIYLENPKKYIPGTKMVFAGLKKPEERADLIAYLKESTK
CCMT A00032 13-Jul-1981 23-Oct-1981 28-Jul-2000
cytochrome c [validated] ailanthus silkmoth ailanthus silkmoth Samia cynthia Chan, S.K. Margoliash, E. J. Biol. Chem. 2411966335-348 Properties and primary structure of the cytochrome c from the flight muscles of the moth, Samia cynthia. MUID66080329 A00032 protein 1-107 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 experimental binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete GVPAGNAENGKKIFVQRCAQCHTVEAGGKHKVGPNLHGFYGRKTGQAPGFSYSNANKAKG ITWGDDTLFEYLENPKKYIPGTKMVFAGLKKANERADLIAYLKESTK
CCWOT A90578 B22945 A00032 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c tobacco hornworm tobacco hornworm Manduca sexta Chan, S.K. Biochim. Biophys. Acta 2211970497-501 Biochemical studies in the developing thoracic muscles of the tobacco horn worm. MUID71108407 A90578 protein 1-107 the compositions of chymotryptic peptides were determined and residues were ordered by homology with silkmoth cytochrome c Swanson, M.S. Zieminn, S.M. Miller, D.D. Garber, E.A.E. Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. 8219851964-1968 Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c. MUID85166253 B22945 mRNA 26-31,'I',33-53,'D',55-63,'NE',66-107 GBM11382 NIDg159496 PIDNAAA29308.1 PIDg159497 the authors translated the codon GAT for residue 29 as Asn, AAT for residue 39 as Gln, and GAG for residue 40 as Asp cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete tentative GVPAGNADNGKKIFVQRCAQCHTVEAGGKHKVGPNLHGFFGRKTGQAPGFSYSNANKAKG ITWQDDTLFEYLENPKKYIPGTKMVFAGLKKANERADLIAYLKQATK
B23058 B23058 29-Aug-1987 20-Aug-1994 03-Mar-2000
cytochrome c DC3 fruit fly (Drosophila melanogaster) Drosophila melanogaster Limbach, K.J. Wu, R. Nucleic Acids Res. 131985631-644 Characterization of two Drosophila melanogaster cytochrome c genes and their transcripts. MUID85215502 B23058 DNA 1-105 GBX01761 NIDg7780 PIDNCAA25901.1 PIDg7781 This protein is expressed at constant, but relatively low levels during development. DC3 FlyBaseFBgn0000408 2 36A 10-11 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c DC3 2-105 predicted domain cytochrome c homology 7-101 binding-site heme (Cys) (covalent) 17,20 predicted binding-site heme iron (His, Met) (axial ligands) 21,83 predicted 105 complete MGSGDAENGKKIFVQKCAQCHTYEVGGKHKVGPNLGGVVGRKCGTAAGYKYTDANIKKGV TWTEGNLDEYLKDPKKYIPGTKMVFAGLKKAEERADLIAFLKSNK
CCHB A00031 28-May-1986 28-May-1986 28-Jul-2000
cytochrome c [validated] honeybee honeybee Apis mellifera Inoue, S. Matsubara, H. Yamanaka, T. J. Biochem. 971985947-954 Complete amino acid sequence of cytochrome c from the honeybee, Apis mellifera, and evolutionary relationship of the honey bee to other insects on the basis of the amino acid sequence. MUID85261185 A00031 protein 1-107 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 experimental binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete GIPAGDPEKGKKIFVQKCAQCHTIESGGKHKVGPNLYGVYGRKTGQAPGYSYTDANKGKG ITWNKETLFEYLENPKKYIPGTKMVFAGLKKPQERADLIAYIEQASK
CCHQ A00035 23-Oct-1981 23-Oct-1981 31-Mar-2000
cytochrome c yeast (Pichia anomala) Pichia anomala, Candida pelliculosa Becam, A.M. Lederer, F. Eur. J. Biochem. 1181981295-302 Amino-acid sequence of the cytochrome c from the yeast Hansenula anomala. Identification of three methylated positions. MUID82027230 A00035 protein 1-109 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 10-104 binding-site heme (Cys) (covalent) 20,23 experimental binding-site heme iron (His, Met) (axial ligands) 24,86 predicted modified-site N6-methyllysine or N6,N6-dimethyllysine (Lys) 61 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 78,79 experimental 109 complete tentative PAPFKKGSEKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRQSGKAEGYSYTDANIK KAVEWSEQTM.SDYLENPKKYIPGTKM.AFGGLKKEKDRNDLVTYLANATK
CCDBK A00036 23-Oct-1981 23-Oct-1981 28-Jul-2000
cytochrome c [validated] yeast (Torulaspora hansenii) Torulaspora hansenii, Debaryomyces hansenii, Candida famata Sugeno, K. Narita, K. Titani, K. J. Biochem. 701971659-682 The amino acid sequence of cytochrome c from Debaryomyces kloeckeri. MUID72091989 A00036 protein 1-109 the source was designated as Debaryomyces kloeckeri cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 10-104 binding-site heme (Cys) (covalent) 20,23 experimental binding-site heme iron (His, Met) (axial ligands) 24,86 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 78 experimental 109 complete PAPYEKGSEKKGANLFKTRCLQCHTVEEGGPHKVGPNLHGVVGRTSGQAQGFSYTDANKK KGVEWTEQDLSDYLENPKKYIPGTKMAFGGLKKAKDRNDLITYLVKATK
CCCK A91919 A91202 A91401 A00034 23-Oct-1981 23-Oct-1981 28-Jul-2000
cytochrome c [validated] yeast (Issatchenkia orientalis) Issatchenkia orientalis, Candida krusei Narita, K. Titani, K. J. Biochem. 631968226-241 The amino acid sequence of cytochrome c from Candida krusei. MUID68368768 A91919 protein 1-21,'E',23-109 Lederer, F. Eur. J. Biochem. 311972144-147 Candida krusei cytochrome c: a correction to the sequence. Glutamine-16, an invariant residue in mitochondrial cytochrome c? MUID73060342 A91202 protein 1-38 Machleidt, W. Wachter, E. Scheulen, M. Otto, J. FEBS Lett. 371973217-220 Solid-phase edman degradation of a protein: N-terminal sequence of cytochrome c from Candida krusei. MUID74055069 A91401 protein 1-35 DeLange, R.J. Glazer, A.N. Smith, E.L. J. Biol. Chem. 24519703325-3327 Identification and location of epsilon-N-trimethyllysine in yeast cytochrome c. MUID70293148 annotation methylation cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 10-104 binding-site heme (Cys) (covalent) 20,23 experimental binding-site heme iron (His, Met) (axial ligands) 24,86 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 78 predicted 109 complete PAPFEQGSAKKGATLFKTRCAQCHTIEAGGPHKVGPNLHGIFSRHSGQAEGYSYTDANKR AGVEWAEPTMSDYLENPKKYIPGTKMAFGGLKKAKDRNDLVTYMLEASK
CCBY A00037 S46588 A91921 S22785 S57067 S63773 24-Apr-1984 30-Jun-1992 28-Jul-2000
cytochrome c 1 [validated] iso-1-cytochrome c protein GTA109 protein J1653 protein YJR048w yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Smith, M. Leung, D.W. Gillam, S. Astell, C.R. Montgomery, D.L. Hall, B.D. Cell 161979753-761 Sequence of the gene for iso-1-cytochrome c in Saccharomyces cerevisiae. MUID79211240 A00037 DNA 1-109 EMBLV01298 NIDg3626 PIDNCAA24605.1 PIDg3627 Huang, M.E. Manus, V. Chuat, J.C. Galibert, F. Yeast 101994811-818 Revised nucleotide sequence of the COR region of yeast Saccharomyces cerevisiae chromosome X. MUID95066383 S46588 translation not shown DNA 1-109 EMBLL26347 NIDg508621 PIDNAAA62856.1 PIDg695795 Narita, K. Titani, K. J. Biochem. 651969259-267 The complete amino acid sequence in baker's yeast cytochrome c. MUID69191928 A91921 protein 2-20,'EL',23-109 the final paper in a series the source is designated as S. oviformis McNeil, J.B. Smith, M. J. Mol. Biol. 1871986363-378 Transcription initiation of the Saccharomyces cerevisiae iso-1-cytochrome c gene. Multiple, independent T-A-T-A sequences. MUID86200219 S22785 DNA 1-22 EMBLX03472 NIDg3613 PIDNCAA27189.1 PIDg3614 DeLange, R.J. Glazer, A.N. Smith, E.L. J. Biol. Chem. 24519703325-3327 Identification and location of epsilon-N-trimethyllysine in yeast cytochrome c. MUID70293148 annotation location of trimethyllysine for isoform 1 Huang, M.E. Chuat, J.C. Galibert, F. submitted to the Protein Sequence Database September1995 S57067 DNA 1-109 EMBLZ49548 NIDg1015706 PIDNCAA89576.1 PIDg1015707 GSPDBGN00010 MIPSYJR048w Huang, M.E. Chuat, J.C. Galibert, F. Yeast 111995775-781 Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA genes and 14 new open reading frames including a gene most probably belonging to the family of ubiquitin-protein ligases. MUID95397595 S63773 nucleic acid sequence not shown translation not shown DNA 1-109 EMBLL36344 NIDg1197060 PIDNAAA88751.1 PIDg1197077 the nucleotide sequence was submitted to the EMBL Data Library, February 1996 SGDCYC1 MIPSYJR048w SGDS0003809 MIPSYJR048w 10R nuclear cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-109 experimental domain cytochrome c homology 10-104 binding-site heme (Cys) (covalent) 20,23 experimental binding-site heme iron (His, Met) (axial ligands) 24,86 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 78 experimental 109 complete MTEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGIFGRHSGQAEGYSYTDANIK KNVLWDENNMSEYLTNPKKYIPGTKMAFGGLKKEKDRNDLITYLKKACE
CCBYBC A00038 S30842 S50505 S18478 S18480 28-Feb-1981 13-Jul-1981 23-Mar-2001
cytochrome c2 iso-2-cytochrome c yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Montgomery, D.L. Leung, D.W. Smith, M. Shalit, P. Faye, G. Hall, B.D. Proc. Natl. Acad. Sci. U.S.A. 771980541-545 Isolation and sequence of the gene for iso-2-cytochrome c in Saccharomyces cerevisiae. MUID80145659 A00038 DNA 1-113 EMBLV01299 NIDg3628 PIDNCAA24606.1 PIDg3629 Mulligan, J.T. Dietrich, F.S. Hennessey, K.M. Sehl, P. Komp, C. Wei, Y. Taylor, P. Nakahara, K. Roberts, D. Davis, R.W. submitted to the EMBL Data Library February1993 S30842 DNA 1-113 GBU18779 EMBLL10830 NIDg603625 PIDNAAB65003.1 PIDg603640 Dietrich, F.S. submitted to the EMBL Data Library December1994 The sequence of S. cerevisiae cosmids 8199, 8334, and 9871. S50505 DNA 1-113 EMBLU18779 NIDg603625 PIDNAAB65003.1 PIDg603640 GSPDBGN00005 MIPSYEL039c Sokolik, C.W. Cohen, R.E. J. Biol. Chem. 26619919100-9107 The structures of ubiquitin conjugates of yeast iso-2-cytochrome c. MUID91225014 S18478 protein 2-113 the location of the trimethyllysine was determined for isoform 2 S18480 protein 2-24 the amino-terminal sequence of isoform 2 as synthesized and ubiquitinylated by an in vitro rabbit system was determined DeLange, R.J. Glazer, A.N. Smith, E.L. J. Biol. Chem. 24519703325-3327 Identification and location of epsilon-N-trimethyllysine in yeast cytochrome c. MUID70293148 annotation methylation SGDCYC7 SGDCYP3 MIPSYEL039c MIPSYEL039c SGDS0000765 5L nuclear cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 14-108 binding-site heme (Cys) (covalent) 24,27 predicted binding-site heme iron (His, Met) (axial ligands) 28,90 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 82 experimental 113 complete MAKESTGFKPGSAKKGATLFKTRCQQCHTIEEGGPNKVGPNLHGIFGRHSGQVKGYSYTD ANINKNVKWDEDSMSEYLTNPKKYIPGTKMAFAGLKKEKDRNDLITYMTKAAK
CCZP T41220 T42217 A00039 24-Apr-1984 28-Jul-2000 28-Jul-2000
cytochrome c fission yeast (Schizosaccharomyces pombe) Schizosaccharomyces pombe Lyne, M. Rajandream, M.A. Barrell, B.G. Volckaert, G. submitted to the EMBL Data Library March1998 T41220 translated from GB/EMBL/DDBJ DNA 1-109 EMBLAL049644 PIDNCAB41053.1 GSPDBGN00066 SPDBSPCC191.07 strain 972h-; cosmid c191 Russell, P.R. Hall, B.D. Mol. Cell. Biol. 21982106-116 Structure of the Schizosaccharomyces pombe cytochrome c gene. MUID82271854 T42217 preliminary translated from GB/EMBL/DDBJ DNA 1-109 EMBLJ01318 NIDg173376 PIDNAAA35300.1 PIDg173377 Simon-Becam, A.M. Claisse, M. Lederer, F. Eur. J. Biochem. 861978407-416 Cytochrome c from Schizosaccharomyces pombe. 2. Amino-acid sequence. MUID78190652 A00039 protein 2-57,'K',59,'R',61-64,'BZZ',68-109 SPDBSPCC191.07 1 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-109 experimental domain cytochrome c homology 9-103 binding-site heme (Cys) (covalent) 19,22 experimental binding-site heme iron (His, Met) (axial ligands) 23,85 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 77 experimental 109 complete MPYAPGDEKKGASLFKTRCAQCHTVEKGGANKVGPNLHGVFGRKTGQAEGFSYTEANRDK GITWDEETLFAYLENPKKYIPGTKMAFAGFKKPADRNNVITYLKKATSE
CCHL A92114 B90188 A00040 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c imperfect fungus (Thermomyces lanuginosus) Thermomyces lanuginosus, Humicola lanuginosa Morgan, W.T. Hensley Jr., C.P. Riehm, J.P. J. Biol. Chem. 24719726555-6565 Proteins of the thermophilic fungus Humicola lanuginosa. I. Isolation and amino acid sequence of a cytochrome c. MUID73015873 A92114 protein 1-10,'SA',13-23,'E',25-26,'GEGANVSQ',35-111 ATCC 16455 Lederer, F. Simon, A.M. Biochem. Biophys. Res. Commun. 561974317-323 Neurospora crassa and Humicola lanuginosa cytochromes C: more homology in the heme region. MUID74147482 B90188 protein 1-37 residues at positions 21, 22, 25, 26, 27, and 34 were not positively identified cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6-dimethyllysine (Lys) 80 experimental modified-site N6,N6,N6-trimethyllysine (Lys) (partial) 94 experimental 111 complete tentative AKGGSFEPGDASKGANLFKTRCAQCHSVEQGGANKIGPNLHGLFGRKTGSVEGYSYTDAN KQAGITW.NEDTLF.EY.LENPKKFIPGTKMAFGGLKKNKDRNDLITYLKEATK
CCNC S48221 A92024 A90188 A00041 24-Apr-1984 12-Apr-1996 28-Jul-2000
cytochrome c [validated] Neurospora crassa Neurospora crassa Bottorff, D.A. Parmaksizoglu, S. Lemire, E.G. Coffin, J.W. Bertrand, H. Nargang, F.E. Curr. Genet. 261994329-335 Mutations in the structural gene for cytochrome c result in deficiency of both cytochromes aa(3) and c in Neurospora crassa. MUID95188270 S48221 preliminary DNA 1-108 EMBLL19358 NIDg388929 PIDNAAA92156.1 PIDg388930 Heller, J. Smith, E.L. J. Biol. Chem. 24119663165-3180 Neurospora crassa cytochrome c. II. Chymotryptic peptides, tryptic peptides, cyanogen bromide peptides, and the complete amino acid sequence. MUID67002604 A92024 protein 2-20,'E',22-23,'GEGGNLTQ',32-108 Lederer, F. Simon, A.M. Biochem. Biophys. Res. Commun. 561974317-323 Neurospora crassa and Humicola lanuginosa cytochromes C: more homology in the heme region. MUID74147482 A90188 protein 2-44 residues at positions 19, 22, and 43 were not positively identified at positions 33, 37, and 40, Leu could not be distinguished from Ile DeLange, R.J. Glazer, A.N. Smith, E.L. J. Biol. Chem. 24419691385-1388 Presence and location of an unusual amino acid, epsilon-N-trimethyllysine, in cytochrome c of wheat germ and Neurospora. MUID69128197 annotation methylation 6/1; 101/2 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 9-103 binding-site heme (Cys) (covalent) 19,22 experimental binding-site heme iron (His, Met) (axial ligands) 23,85 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 77 experimental 108 complete MGFSAGDSKKGANLFKTRCAQCHTLEEGGGNKIGPALHGLFGRKTGSVDGYAYTDANKQK GITWDENTLFEYLENPKKYIPGTKMAFGGLKKDKDRNDIITFMKEATA
CCUS A00042 24-Apr-1984 30-Sep-1988 31-Mar-2000
cytochrome c smut fungus (Ustilago sphaerogena) Ustilago sphaerogena Bitar, K.G. Vinogradov, S.N. Nolan, C. Weiss, L.J. Margoliash, E. Biochem. J. 1291972561-569 The primary structure of cytochrome c from the rust fungus Ustilago sphaerogena. MUID73161218 A00042 protein 1-107 ATCC 12421 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 experimental binding-site heme iron (His, Met) (axial ligands) 22,84 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 76 absent 107 complete tentative GFEDGDAKKGARIFKTRCAQCHTLGAGEPNKVGPNLHGLFGRKSGTVEGF.SY.TDANKK AGQVW.EEETFL.EYLENPKKYIPGTKMAFGGLKKEKDRNDLVTYLREETK
CCRPBN A00043 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] rape rape Brassica napus Richardson, M. Ramshaw, J.A.M. Boulter, D. Biochim. Biophys. Acta 2511971331-333 The amino acid sequence of rape (Brassica napus L.) cytochrome c. A00043 protein 1-111 109-Ser was found in 40% of the molecules cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation polymorphism respiratory chain domain cytochrome c homology 12-106 modified-site blocked amino end (Ala) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFDEAPPGNSKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNKAVEWEEKTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKEATA
CCRPBO A04613 A00043 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c cauliflower cauliflower Brassica oleracea var. botrytis Thompson, E.W. Richardson, M. Boulter, D. Biochem. J. 1241971783-785 The amino acid sequence of cytochrome c of Fagopyrum esculentum Moench (buckwheat) and Brassica oleracea L. (cauliflower). MUID72074418 A04613 protein 1-111 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation polymorphism respiratory chain domain cytochrome c homology 12-106 modified-site blocked amino end (Ala) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFDEAPPGNSKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNKAVEWEEKTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKEATA
CCPU A00044 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c cucurbit cucurbit Cucurbita sp. Thompson, E.W. Richardson, M. Boulter, D. Biochem. J. 1241971779-781 The amino acid sequence of cytochrome c from Cucurbita maxima L. (pumpkin). MUID72074417 A00044 protein 1-111 47-Lys, 52-Ala, and 109-Ser were also found cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation polymorphism respiratory chain domain cytochrome c homology 12-106 modified-site blocked amino end (Ala) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFDEAPPGNSKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSAAN KNRAVIWEEKTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKEATA
CCMB A00045 C00047 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c mung bean mung bean Vigna radiata Thompson, E.W. Laycock, M.V. Ramshaw, J.A.M. Boulter, D. submitted to the Atlas August1970 A00045 protein 1-111 Thompson, E.W. Laycock, M.V. Ramshaw, J.A.M. Boulter, D. Biochem. J. 1171970183-192 The amino acid sequence of Phaseolus aureus L. (mung-bean) cytochrome c. MUID70207558 annotation sequence Thompson, E.W. Richardson, M. Boulter, D. Biochem. J. 1211971439-446 The amino acid sequence of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c. MUID72042446 C00047 protein 1-3,'BZ',6-9,'B',11-111 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 predicted binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 predicted 111 complete ASFDEAPPGNSKSGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSYSTAN KNMAVIWEEKTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKESTA
CCHECC A00046 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] hemp hemp, marijuana Cannabis sativa Wallace, D.G. Brown, R.H. Boulter, D. Phytochemistry 1219732617-2622 The amino acid sequence of Cannabis sativa cytochrome-c. A00046 protein 1-111 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site blocked amino end (Ala) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFBZAPPGBSKAGEKIFKTKCAECHTVGRGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNMAVTWZZKTLYDYLLNPKKYIPGTKMVFPGLKKPZBRADLIAYLKESTA
CCES A00047 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] oriental sesame oriental sesame Sesamum indicum Thompson, E.W. Richardson, M. Boulter, D. Biochem. J. 1211971439-446 The amino acid sequence of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c. MUID72042446 A00047 protein 1-111 the authors placed the amides at positions 24, 70, and 97 by homology with other cytochromes c 4-Ser was found in 30% of the molecules cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFBZAPPGBVKSGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSAAN KNMAVIWGENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLIAYLKEATA
CCRZ JS0709 A00048 T02065 31-Jul-1979 20-Aug-1994 28-Jul-2000
cytochrome c [validated] rice rice Oryza sativa Nishi, R. Uchimiya, H. Kato, A. submitted to JIPID July1992 JS0709 translation not shown mRNA 1-112 DDBJD12634 NIDg218248 PIDNBAA02159.1 PIDg218249 strain Yamahousi Mori, E. Morita, Y. J. Biochem. 871980249-266 Amino acid sequence of cytochrome c from rice. MUID80137364 A00048 protein 2-112 the amidation states of residues 25, 37, 40, 42, 48, 69, 70, 71, 98, and 99 were assigned by homology with other plant cytochrome c sequences Lee, M.C. Kim, C.S. Lee, J.S. Eun, M.Y. submitted to the EMBL Data Library August1997 Isolation and characterization of cytochrome C from rice. T02065 preliminary translated from GB/EMBL/DDBJ mRNA 1-85,'E',87-95,'NHRSVLI',103,'FPT' EMBLAF017367 NIDg2394299 PIDNAAB70265.1 PIDg2394300 strain Milyang 23 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-112 experimental domain cytochrome c homology 13-107 modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 23,26 experimental binding-site heme iron (His, Met) (axial ligands) 27,89 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 81,95 experimental 112 complete MASFSEAPPGNPKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTPGYSYSTA NKNMAVIWEENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLISYLKEATS
CCZM A00049 19-Feb-1984 17-Feb-1994 03-Mar-2000
cytochrome c maize maize Zea mays Boulter, D. unpublished results, cited in Handbook of Biochemistry and Molecular Biology, 3rd ed., vol.3, Fasman, G.D., ed., pp.284-285, Chemical Rubber Co., Cleveland 1976 A00049 protein 1-111 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 predicted 111 complete ASFSEAPPGNPKAGEKIFKTKCAQCHTVEKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNKAVVWEENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLIAYLKEATA
CCCS B00047 A00050 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] castor bean castor bean Ricinus communis Thompson, E.W. Richardson, M. Boulter, D. Biochem. J. 1211971439-446 The amino acid sequence of sesame (Sesamum indicum L.) and castor (Ricinus communis L.) cytochrome c. MUID72042446 B00047 protein 1-111 Brown, R.H. Boulter, D. Biochem. J. 1311973247-251 The amino acid sequence of cytochrome c from Allium porrum L. (leek). MUID73229095 annotation variant cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme hydroxyproline iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site 4-hydroxyproline (Pro) (partial) 79 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFBZAPPGBVKAGEKIFKTKCAQCHTVEKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNMAVQWGENTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKZATA
CCCN A00051 17-Mar-1987 17-Mar-1987 28-Jul-2000
cytochrome c [validated] sea-island cotton sea-island cotton Gossypium barbadense Thompson, E.W. Notton, B.A. Richardson, M. Boulter, D. Biochem. J. 1241971787-791 The amino acid sequence of cytochrome c from Abutilon theophrasti Medic. and Gossypium barbadense L. (cotton). MUID72074419 A00051 protein 1-111 Brown, R.H. Boulter, D. Biochem. J. 1311973247-251 The amino acid sequence of cytochrome c from Allium porrum L. (leek). MUID73229095 annotation variant cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme hydroxyproline iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site 4-hydroxyproline (Pro) (partial) 79 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFQZAPPGBAKAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNMAVQWGENTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKZSTA
CCAB A00052 17-Mar-1987 17-Mar-1987 28-Jul-2000
cytochrome c [validated] China jute China jute Abutilon theophrasti Thompson, E.W. Notton, B.A. Richardson, M. Boulter, D. Biochem. J. 1241971787-791 The amino acid sequence of cytochrome c from Abutilon theophrasti Medic. and Gossypium barbadense L. (cotton). MUID72074419 A00052 protein 1-111 Brown, R.H. Boulter, D. Biochem. J. 1311973247-251 The amino acid sequence of cytochrome c from Allium porrum L. (leek). MUID73229095 annotation variant cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme hydroxyproline iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site 4-hydroxyproline (Pro) (partial) 79 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFQZAPPGBAKAGEKIFKTKCAQCHTVEKGAGHKQGPNLNGLFGRQSGTTPGYSYSAAN KNMAVNWGENTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKZSTA
CCTO A00053 A11461 13-Jul-1981 31-Dec-1991 28-Jul-2000
cytochrome c [validated] tomato tomato Lycopersicon esculentum Scogin, R. Richardson, M. Boulter, D. Arch. Biochem. Biophys. 1501972489-492 The amino acid sequence of cytochrome c from tomato (Lycopersicon esculentum Mill.). MUID72234831 A00053 protein 1-97,'Q',99-111 Boulter, D. Ramshaw, J.A.M. Thompson, E.W. Richardson, M. Brown, R.H. Proc. R. Soc. Lond. B Biol. Sci. 1811972441-455 A phylogeny of higher plants based on the amino acid sequences of cytochrome c and its biological implications. A11461 protein 98 residue 98 in reference A00053 should have been shown as Glu cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFNEAPPGNPKAGEKIFKTKCAQCHTVEKGAGHKEGPNLNGLFGRQSGTTAGYSYSAAN KNMAVNWGENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLIAYLKEATA
CCPO A04610 A00053 31-Dec-1990 31-Dec-1991 03-Mar-2000
cytochrome c potato potato Solanum tuberosum Martinez, G. Rochat, H. Ducet, G. FEBS Lett. 471974212-217 The amino acid sequence of cytochrome c from Solanum tuberosum (potato). MUID75039137 A04610 protein 1-111 98-Asp was also found cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site blocked amino end (Ala) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 predicted 111 complete tentative ASFGEAPPGNPKAGEKIFKTKCAQCHTVDKGAGHKEGPNLNGLFGRQSGTTAGYSYSNAN KNMAVTWGENTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLIAYLKEATA
CCED A00054 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c European elder European elder Sambucus nigra Brown, R.H. Boulter, D. Biochem. J. 137197493-100 The amino acid sequences of cytochrome c from four plant sources. MUID74140224 A00054 protein 1-111 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFAEAPPGNPKAGEKIFKTKCNQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNMAVNWEEKTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKQSTA
CCBX A00055 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c box elder box elder Acer negundo Brown, R.H. Boulter, D. Biochem. J. 137197493-100 The amino acid sequences of cytochrome c from four plant sources. MUID74140224 A00055 protein 1-112 112-Ser was found in 50% of the molecules cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 112 complete ASFAEAPPGNPAAGEKIFKTKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNMAVNWGYNTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKQSTAA
CCLK A00056 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c leek leek Allium porrum Brown, R.H. Boulter, D. Biochem. J. 1311973247-251 The amino acid sequence of cytochrome c from Allium porrum L. (leek). MUID73229095 A00056 protein 1-111 one residue of trimethyllysine is placed at position 80, rather than 81, by homology with wheat (see A92043) there are amides at two of the three positions 5, 10, and 11 and at one of the three positions 68, 69, and 70 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme hydroxyproline iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site 4-hydroxyproline (Pro) (partial) 79 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete tentative ATF.SZAPPGBZKA.GQKIF.KL.KCAQCHTVEKGAGH.KQGPNLNGLF.GRQSGT.AAG Y.SY.SAANKN.MAVVW.ZZBTLY.DY.LLNPKKY.IPGTKM.VFPGL.KKPQ.DRADL. IAY.LKESTA
CCRM A00057 24-Apr-1984 17-Feb-1994 03-Mar-2000
cytochrome c cuckoopint cuckoopint Arum maculatum Boulter, D. unpublished results, cited by Dickerson, R.E., and Timkovich, R., in The Enzymes, 3rd ed., vol.11, part A, Boyer, P.D., ed., pp.397-547, Academic Press, New York 1975 A00057 protein 1-111 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 predicted binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 predicted 111 complete ASFAEAPPGNPKAGEKIFKTKCAQCHTVEKGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNMAVIWEESTLYDYLLNPKKYIPGTKMVFPGLKKPQERADLIAYLKESTA
CCND A00058 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c love-in-a-mist love-in-a-mist Nigella damascena Brown, R.H. Boulter, D. Biochem. J. 1331973251-254 The amino acid sequence of cytochrome c from Nigella damascena L. (love-in-a-mist). MUID73233117 A00058 protein 1-111 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 predicted 111 complete tentative AS.F.BZAPAGBSAS(G.E.K)I.F.KTKCAZCHTVBZGAGH.KZGP(N.L)H.G.L.F. GRQSGT.VAG.Y.SY.SAANKN.KAVN.W.EEKT.L.Y.DYLLNPKK.Y.IP(G.T.K.M )VFPGL.KKPZZRABL.LA.Y.LKESTA
CCNS A00059 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c common nasturtium common nasturtium Tropaeolum majus Brown, R.H. Boulter, D. Biochem. J. 137197493-100 The amino acid sequences of cytochrome c from four plant sources. MUID74140224 A00059 protein 1-111 any one of the Lys residues shown may be an Arg, or an Arg may be missing from the sequence cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete tentative ASFAEAPAGDNK.AGDKIFKNKCAQCHTVDKGAGHKQGPNLNGLFGRQSGTTAGYSY.SA ANKNK.AVLW.ZZATLY.DYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKESTA
CCWT A00060 23-Oct-1981 23-Oct-1981 28-Jul-2000
cytochrome c [validated] wheat common wheat Triticum aestivum Stevens, F.C. Glazer, A.N. Smith, E.L. J. Biol. Chem. 24219672764-2779 The amino acid sequence of wheat germ cytochrome c. MUID67169616 A00060 protein 1-112 the tentative assignment of 24-Gln and 69-Glu is based on indirect evidence (electrophoretic mobilities and comparisons with other cytochromes c) DeLange, R.J. Glazer, A.N. Smith, E.L. J. Biol. Chem. 24419691385-1388 Presence and location of an unusual amino acid, epsilon-N-trimethyllysine, in cytochrome c of wheat germ and Neurospora. MUID69128197 annotation methylation cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 112 complete ASFSEAPPGNPDAGAKIFKTKCAQCHTVDAGAGHKQGPNLHGLFGRQSGTTAGYSYSAAN KNKAVEWEENTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKKATSS
CCNG A00061 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c niger seed niger seed Guizotia abyssinica Ramshaw, J.A.M. Boulter, D. Phytochemistry 1419751945-1949 The amino acid sequence of cytochrome c from niger-seed, Guizotia abyssinica. A00061 protein 1-111 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete tentative ASFAEAPAGDAKAGEKIFK.TKCAZCHTVZKGAGHK.QGPNLNGLFGRQSGTTAGYSYSA ANKNK.AVAWZZBSLYDYLLNPKKYIPGTKMVFPGLKKPZZRADLIAYLKASTA
CCFS A00062 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c common sunflower common sunflower Helianthus annuus Ramshaw, J.A.M. Thompson, E.W. Boulter, D. Biochem. J. 1191970535-539 The amino acid sequence of Helianthus annuus L. (sunflower) cytochrome c deduced from chymotryptic peptides. MUID71112252 A00062 protein 1-111 the authors placed the amides at positions 24, 70, and 97 by homology with other cytochromes c cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete tentative ASF.AEAPAGDPTTGAKIF.KTKCAQCHTVEKGAGH.KQGPNLNGLF.GRQSGTTAGY.S Y.SAANKNM.AVIW.EENTLY.DYLLNPKKY.IPGTKM.VFPGL.KKPQERADLIAY.LK TSTA
CCPZ A00063 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c parsnip parsnip Pastinaca sativa Brown, R.H. Boulter, D. Biochem. J. 137197493-100 The amino acid sequences of cytochrome c from four plant sources. MUID74140224 A00063 protein 1-111 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ASFAEAPPGDKDVGGKIFKTKCAZCHTVZLGAGHKQGPNLNGLFGRQSGTTAGYSYSAAN KNKAVLWABBTLYDYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKHATA
CCFA A00064 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c common buckwheat common buckwheat Fagopyrum esculentum Thompson, E.W. Richardson, M. Boulter, D. Biochem. J. 1241971783-785 The amino acid sequence of cytochrome c of Fagopyrum esculentum Moench (buckwheat) and Brassica oleracea L. (cauliflower). MUID72074418 A00064 protein 1-111 the authors placed the amides at positions 10, 24, and 97 by homology with other cytochromes c there is one amide at position 108 or 111 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site blocked amino end (Ala) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 22,25 predicted binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete tentative ATFSEAPPGNIKSGEKIFKTKCAQ(C.H)TVEKGAGHKQGPNLNGLFGRQSGTTAGYSYS AANKNKAVTWGEDTLYEYLLNPKKYIPGTKMVFPGLKKPQERADLIAYLKBSTZ
CCSP A00065 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] spinach spinach Spinacia oleracea Brown, R.H. Richardson, M. Scogin, R. Boulter, D. Biochem. J. 1311973253-256 The amino acid sequence of cytochrome c from Spinacea oleracea L. (spinach). MUID73229096 A00065 protein 1-111 cv. Monster Viroflay cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 111 complete ATFSEAPPGNKDVGAKIFKTKCAQCHTVDLGAGHKQGPNLNGLFGRQSGTAASYSYSAAN KNKAVIWSEDTLYEYLLNPKKYIPGTKMVFPGLKKPQDRADLIAYLKDSTQ
CCGK A00066 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c ginkgo ginkgo Ginkgo biloba Ramshaw, J.A.M. Richardson, M. Boulter, D. Eur. J. Biochem. 231971475-483 The amino-acid sequence of the cytochrome c of Ginkgo biloba L. MUID72097686 A00066 protein 1-113 there is one amide at position 24 or 29, probably one at 69 or 70, and one at 97 or 98 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ala) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80,94 experimental 113 complete tentative ATFSEAPPGDPKAGEKIFKTKCAZ(C.H)TVZKGAGHKQGPNLHGLFGRQSGTTAGYSYS TGNKNKAVNWGZZTLYEYLLNPKKYIPGTKMVFPGLKKPZZRADLISYLKQATSQE
CCEI A00067 24-Apr-1984 30-Sep-1988 31-Mar-2000
cytochrome c green alga (Enteromorpha intestinalis) hollow green seaweed Enteromorpha intestinalis Meatyard, B.T. Boulter, D. Phytochemistry 1319742777-2782 The amino acid sequence of cytochrome c from Enteromorpha intestinalis. A00067 protein 1-111 69-Asx was also found the source may have been Enteromorpha intestinalis, E. linza, E. flexuosa, or a mixed culture of those species cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 12-106 modified-site acetylated amino end (Ser) 1 experimental binding-site heme (Cys) (covalent) 22,25 experimental binding-site heme iron (His, Met) (axial ligands) 26,88 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 80 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 94 absent 111 complete tentative STFABAPPGBPAK.GAK.IFK.AKCAZCHTVBAGAGHK.QGPNLNGAFGRTSGTAAGF.S Y.SAAB.KBKTADWBZBTLY.DYLLNPKKYIPGTKMVFAGLK.KPZBRADLIAFLK.DAT A
CCEG A00068 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] Euglena gracilis Euglena gracilis Pettigrew, G.W. Leaver, J.L. Meyer, T.E. Ryle, A.P. Biochem. J. 1471975291-302 Purification, properties and amino acid sequence of atypical cytochrome c from two protozoa, Euglena gracilis and Crithidia oncopelti. MUID76039443 A00068 protein 1-102 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-97 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 17 experimental binding-site heme iron (His, Met) (axial ligands) 18,79 predicted modified-site N6,N6,N6-trimethyllysine (Lys) 85 experimental 102 complete GDAERGKKLFESRAAQCHSAQKGVNSTGPSLWGVYGRTSGSVPGYAYSNANKNAAIVWEE ETLHKFLENPKKYVPGTKMAFAGIKAKKDRQDIIAYMKTLKD
CCCRCO A00069 A37571 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] Crithidia oncopelti Crithidia oncopelti Pettigrew, G.W. Leaver, J.L. Meyer, T.E. Ryle, A.P. Biochem. J. 1471975291-302 Purification, properties and amino acid sequence of atypical cytochrome c from two protozoa, Euglena gracilis and Crithidia oncopelti. MUID76039443 A00069 protein 1-112 Smith, G.M. Pettigrew, G.W. Eur. J. Biochem. 1101980123-130 Identification of N,N-dimethylproline as the N-terminal blocking group of Crithidia oncopelti cytochrome c557. MUID81066625 A37571 protein 1-5 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein methylated amino acid methylated amino end mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 14-108 modified-site dimethylated amino end (Pro) 1 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 3,82 experimental binding-site heme (Cys) (covalent) 27 experimental binding-site heme iron (His, Met) (axial ligands) 28,90 predicted 112 complete PPKAREPLPPGDAAKGEKIFKGRAAQCHTGAKGGANGVGPNLFGIVNRHSGTVEGFAYSK ANADSGVVWTPEVLDVYLENPKKFMPGTKMSFAGIKKPQERADLIAYLENLK
CCCRCF A00070 19-Feb-1984 19-Feb-1984 31-Mar-2000
cytochrome c Crithidia fasciculata Crithidia fasciculata Hill, G.C. Pettigrew, G.W. Eur. J. Biochem. 571975265-271 Evidence for the amino-acid sequence of Crithidia fasciculata cytochrome c555. MUID76022512 A00070 protein 1-113 64-Asp was also found Pettigrew, G.W. submitted to the Atlas July1977 annotation cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein methylated amino acid mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 14-108 modified-site blocked amino end (Pro) (probably dimethylated) 1 experimental modified-site N6,N6,N6-trimethyllysine (Lys) 3,82 experimental binding-site heme (Cys) (covalent) 27 predicted binding-site heme iron (His, Met) (axial ligands) 28,90 predicted 113 complete tentative (P)PKARAPLPPGDAARGEKLFK.GR.AAQCHTANQGGANGVG(P.N=L.Y=G.L.V.G) R.HSGTIEGYAY.SKANAESGVVWTPDVLDVYLENPKKFMPGTKMSFAGMKKPQERADVI AYLETLKG
CCTE A00071 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] Tetrahymena pyriformis Tetrahymena pyriformis Tarr, G.E. Fitch, W.M. Biochem. J. 1591976193-199 Amino acid sequence of cytochrome c from Tetrahymena pyriformis phenoset A. MUID77065147 A00071 protein 1-109 strain GL-7 of Phenoset A SGC5 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 15-106 binding-site heme (Cys) (covalent) 25,28 experimental binding-site heme iron (His, Met) (axial ligands) 29,88 predicted 109 complete GPKEPEVTVPEGDASAGRDIFDSQCSACHAIEGDSTAAPVLGGVIGRKAGQEKFAYSKGM KGSGITWNEKHLFVFLKNPSKHVPGTKMAFAGLPADKDRADLIAYLKSV
CCRF2G A32518 A00072 30-Nov-1979 30-Nov-1979 28-Jul-2000
cytochrome c2 [validated] Rhodopila globiformis Rhodopila globiformis Ambler, R.P. Meyer, T.E. Cusanovich, M.A. Kamen, M.D. Biochem. J. 2461987115-120 The amino acid sequence of the cytochrome c2 from the phototrophic bacterium Rhodopseudomonas globiformis. MUID88049600 A32518 protein 1-106 Cytochrome c2 is found mainly in purple, nonsulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some nonphotosynthetic bacteria. cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 9-102 binding-site heme (Cys) (covalent) 19,22 experimental binding-site heme iron (His, Met) (axial ligands) 23,84 predicted 106 complete GSAPPGDPVEGKHLFHTICILCHTDIKGRNKVGPSLYGVVGRHSGIEPGYNYSEANIKSG IVWTPDVLFKYIEHPQKIVPGTKMGYPGQPDPQKRADIIAYLETLK
CCAG2 A00073 22-May-1981 08-Oct-1981 03-Mar-2000
cytochrome c2 Agrobacterium tumefaciens (strain II Chrys) Agrobacterium tumefaciens Van Beeumen, J. Tempst, P. Stevens, P. Bral, D. Van Damme, J. De Ley, J. Protides of the Biological Fluids, Proc. 28th Colloq., Peeters, H., ed., pp.69-74, Pergamon Press, Oxford 1980 Cytochromes c of two different sequence classes in Agrobacterium tumefaciens. A00073 protein 1-111 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c homology 5-101 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,83 predicted 111 complete EGDVAKGEAAFKRCSACHAIGEGAKNKVGPQLNGIIGRTAGGDPDYNYSNAMKKAGGEGL VWTPQELRDFLSAPKKKIPGNKMALAGISKPEELDNLIAYLIFSASSKPAZ
JU0381 JU0381 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome c550 Thiobacillus novellus Thiobacillus novellus Yamanaka, T. Nagano, T. Shouji, K. Fukumori, Y. Viva Origino 19199172-73 Cytochrome c of the sulphur oxidizing bacterium, Thiobacillus novellus: structure, function and evolution. JU0381 protein 1-109 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c homology 4-100 binding-site heme (Cys) (covalent) 13,16 predicted binding-site heme iron (His, Met) (axial ligands) 17,82 predicted 109 complete XXPAKGANVFWKCMACHAVGEGAKNKVGPELNGIIGRKMGSIEGFNYSDTLKEHNAKGDV WTAEILSQYLANPKGYMPGVKMVFAGLPKEIRADDLEAYLKTFNADGTK
B40638 B40638 21-Sep-1993 27-Feb-1997 03-Mar-2000
isocytochrome c2 Rhodobacter sphaeroides Rhodobacter sphaeroides Rott, M.A. Witthuhn, V.C. Schilke, B.A. Soranno, M. Ali, A. Donohue, T.J. J. Bacteriol. 1751993358-366 Genetic evidence for the role of isocytochrome c2 in photosynthetic growth of Rhodobacter sphaeroides Spd mutants. MUID93123153 B40638 DNA 1-144 GBL02104 NIDg151899 PIDNAAA61341.1 PIDg151901 sequence extracted from NCBI backbone (NCBIN:122345, NCBIP:122347) This protein can substitute for cytochrome c2 in c2-deficient mutants. cycI cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 26-122 binding-site heme (Cys) (covalent) 35,38 predicted binding-site heme iron (His, Met) (axial ligands) 39,104 predicted 144 complete MRLTTILAGALALGAAQAAFAEGDPAAGEKAFRKCQACHQIGAEAQNKTGPVLTGVIGRP AASIEGFSYSKTLTEAAADGLVWDHAALETFLANPRKAMPGTKMAFPGIKKPQELADILA YLDTFSDGETREAEETPAAAPAEG
CCRD2 A00074 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2 Rhodomicrobium vannielii Rhodomicrobium vannielii Ambler, R.P. Meyer, T.E. Kamen, M.D. Proc. Natl. Acad. Sci. U.S.A. 731976472-475 Primary structure determination of two cytochromes c-2: close similarity to functionally unrelated mitochondrial cytochrome c. MUID76102814 A00074 protein 1-104 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 5-98 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete AGDPVKGEQVFKQCKICHQVGPTAKNGVGPEQNDVFGQKAGARPGFNYSDAMKNSGLTWD EATLDKYLENPKAVVPGTKMVFVGLKNPQDRADVIAYLKQLSGK
CCRF2V A36720 A93806 A00075 24-Apr-1984 30-Sep-1991 03-Mar-2000
cytochrome c2 precursor Rhodopseudomonas viridis Rhodopseudomonas viridis Grisshammer, R. Wiessner, C. Michel, H. J. Bacteriol. 17219905071-5078 Sequence analysis and transcriptional organization of the Rhodopseudomonas viridis cytochrome c-2 gene. MUID90368560 A36720 DNA 1-127 GBM59302 NIDg151874 PIDNAAA26092.1 PIDg151875 Ambler, R.P. Meyer, T.E. Kamen, M.D. Proc. Natl. Acad. Sci. U.S.A. 731976472-475 Primary structure determination of two cytochromes c-2: close similarity to functionally unrelated mitochondrial cytochrome c. MUID76102814 A93806 protein 21-33,'K',35-65,'S',67-103,'I',105-116,'L',118-127 Ambler, R.P. submitted to the Atlas June1977 annotation residue 34 is Leu cycA cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein photosynthesis domain signal sequence 1-20 predicted product cytochrome c2 21-127 experimental domain cytochrome c homology 24-117 modified-site blocked amino end (Gln) (in mature form) (probably pyrrolidone carboxylic acid) 21 experimental binding-site heme (Cys) (covalent) 33,36 predicted binding-site heme iron (His, Met) (axial ligands) 37,99 predicted 127 complete MRKLVFGLFVLAASVAPAAAQDAASGEQVFKQCLVCHSIGPGAKNKVGPVLNGLFGRHSG TIEGFAYSDANKNSGITWTEEVFREYIRDPKAKIPGTKMIFAGVKDEQKVSDLIAYIKQF NADGSKK
CCRF2A A00076 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2 Rhodopseudomonas acidophila Rhodopseudomonas acidophila Ambler, R.P. Meyer, T.E. Bartsch, R.G. Kamen, M.D. unpublished results, cited by Ambler, R.P., in Evolution of Protein Molecules, Matsubara, H., and Yamanaka, T., eds., pp.311-322, Japan Scientific Societies Press/Center for Academic Publications Japan, Tokyo 1978 A00076 protein 1-107 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 5-98 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 107 complete AGDPDAGQKVFLKCAACHKIGPGAKNGVGPSLNGVANRKAGQAEGFAYSDANKNSGLTWD EATFKEYITAPQKKVPGTKMTFPGLPNEADRDNIWAYLSQFKADGSK
CCNA5A A00077 28-May-1986 28-May-1986 03-Mar-2000
cytochrome c550 Nitrobacter winogradskyi Nitrobacter winogradskyi Tanaka, Y. Fukumori, Y. Yamanaka, T. Biochim. Biophys. Acta 707198214-20 The complete amino acid sequence of Nitrobacter agilis cytochrome c-550. MUID83049097 A00077 protein 1-109 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c homology 4-97 binding-site heme (Cys) (covalent) 13,16 predicted binding-site heme iron (His, Met) (axial ligands) 17,79 predicted 109 complete GDVEAGKAAFNKCKACHEIGESAKNKVGPELDGLDGRHSGAVEGYAYSPANKASGITWTE AEFKEYIKDPKAKVPGTKMVFAGIKKDSELDNLWAYVSQFDKDGKVKAK
S00034 S00034 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome c550 Aquaspirillum itersonii Aquaspirillum itersonii Woolley, K.J. Eur. J. Biochem. 1661987131-137 The soluble c-type cytochromes from the bacterium Aquaspirillum itersonii: the complete amino acid sequence of the cytochrome c-550. MUID87246667 S00034 protein 1-111 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c homology 4-107 binding-site heme (Cys) (covalent) 13,16 predicted binding-site heme iron (His, Met) (axial ligands) 17,90 predicted 111 complete GDAAKGANVAKSCGTCHSFEQGGAKKQGPNLFGITTRGPGKAEGFNYSPSYKAAAAKGFA WDAATLQDYITDPTAFLSNKTGDAAARDKMTFKLAKPDERADVIAYLATLK
CCQF2F A00078 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2, iso-1 Rhodospirillum fulvum Rhodospirillum fulvum Ambler, R.P. Meyer, T.E. Bartsch, R.G. Kamen, M.D. unpublished results, cited by Ambler, R.P., in Evolution of Protein Molecules, Matsubara, H., and Yamanaka, T., eds., pp.311-322, Japan Scientific Societies Press/Center for Academic Publications Japan, Tokyo 1978 A00078 protein 1-99 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 1-95 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,75 predicted 99 complete ADAPTAFNQCKACHSIEAGKNGVGPSLSGAYGRKVGLAPNYKYSAAHLASGMTIDEAMLT NYLANPKATIPGNKMGASFGGLKKPEDVKAVIEYLKTVK
CCQF2M A00079 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2, iso-1 Rhodospirillum molischianum Rhodospirillum molischianum Ambler, R.P. Meyer, T.E. Bartsch, R.G. Kamen, M.D. unpublished results, cited by Ambler, R.P., in Evolution of Protein Molecules, Matsubara, H., and Yamanaka, T., eds., pp.311-322, Japan Scientific Societies Press/Center for Academic Publications Japan, Tokyo 1978 A00079 protein 1-100 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 1-96 binding-site heme (Cys) (covalent) 11,14 predicted binding-site heme iron (His, Met) (axial ligands) 15,76 predicted 100 complete ADAPPPAFNQCKACHSIDAGKNGVGPSLSGAYGRKVGLAPNYKYSPAHLASGMTIDDAML TKYLANPKETIPGNKMGAAFGGLKNPADVAAVIAYLKTVK
CCQFM2 A00080 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2, iso-2 Rhodospirillum molischianum Rhodospirillum molischianum Ambler, R.P. Meyer, T.E. Bartsch, R.G. Kamen, M.D. unpublished results, cited by Ambler, R.P., in Evolution of Protein Molecules, Matsubara, H., and Yamanaka, T., eds., pp.311-322, Japan Scientific Societies Press/Center for Academic Publications Japan, Tokyo 1978 A00080 protein 1-97 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 1-93 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,75 predicted 97 complete ADAPAGFTLCKACHSVEAGKNGVGPSLAGVYGRKAGTISGFKFSDPHIKSGLTWDEPTLT KYLADPKTVIPGNKMVFAGLKNPDDVKAVIEYLKTLK
CCQFF2 A00081 31-May-1979 08-Oct-1981 31-Mar-2000
cytochrome c2, iso-2 Rhodospirillum fulvum Rhodospirillum fulvum Ambler, R.P. Daniel, M. Hermoso, J. Meyer, T.E. Bartsch, R.G. Kamen, M.D. Nature 2781979659-660 Cytochrome c-2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria. MUID79199667 A00081 protein 1-96 62-Phe is found in about 30% of the molecules cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 1-93 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,75 predicted 96 complete tentative ADAPPAFGMCKACHSVEAGKNGVGPS(L.A.G.V.Y)GRKAGTLAGFKFSDPHAKSGLTW DEPTLTKYLADPKGVIPGNKMVFAGLKNPADVA(A.V.I.A.Y)LKSL
CCRF2P B00086 B00089 A00082 22-May-1981 22-May-1981 17-Nov-2000
cytochrome c2 Rhodopseudomonas palustris (strain 2.1.6) Rhodopseudomonas palustris Ambler, R.P. Daniel, M. Hermoso, J. Meyer, T.E. Bartsch, R.G. Kamen, M.D. Nature 2781979659-660 Cytochrome c-2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria. MUID79199667 B00086 protein 1-114 ATCC 17001 Ambler, R.P. Meyer, T.E. Murray, S. submitted to the Atlas July1974 B00089 protein 1-114 amino-terminal blocking group cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis pyroglutamic acid domain cytochrome c homology 4-110 modified-site pyrrolidone carboxylic acid (Gln) 1 experimental binding-site heme (Cys) (covalent) 13,16 predicted binding-site heme iron (His, Met) (axial ligands) 17,93 predicted 114 complete QDAAKGEAVFKQCMTCHRADKNMVGPALGGVVGRKAGTAAGFTYSPLNHNSGEAGLVWTQ ENIIAYLPDPNAYLKKFLTDKGQADKATGSTKMTFKLANDQQRKDVAAYLATLK
CCRF7P A00083 22-May-1981 22-May-1981 03-Mar-2000
cytochrome c2 Rhodopseudomonas palustris (strain 2.1.37) Rhodopseudomonas palustris Ambler, R.P. Daniel, M. Hermoso, J. Meyer, T.E. Bartsch, R.G. Kamen, M.D. Nature 2781979659-660 Cytochrome c-2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria. MUID79199667 A00083 protein 1-114 ATCC 17007 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis pyroglutamic acid domain cytochrome c homology 4-110 modified-site pyrrolidone carboxylic acid (Gln) 1 experimental binding-site heme (Cys) (covalent) 13,16 predicted binding-site heme iron (His, Met) (axial ligands) 17,93 predicted 114 complete QDAKAGEAVFKQCMTCHRADKNMVGPALGGVVGRKAGTAAGFTYSPLNHNSGEAGLVWTA DNIINYLNDPNAFLKKFLTDKGKADQAVGVTKMTFKLANEQQRKDVVAYLATLK
CCQF2R S08213 A00084 24-Apr-1984 30-Sep-1991 28-Jul-2000
cytochrome c2 precursor [validated] Rhodospirillum rubrum Rhodospirillum rubrum Self, S.J. Hunter, C.N. Leatherbarrow, R.J. Biochem. J. 2651990599-604 Molecular cloning, sequencing and expression of cytochrome c(2) from Rhodospirillum rubrum. MUID90147629 S08213 DNA 1-135 EMBLX17605 NIDg46378 PIDNCAA35607.1 PIDg46379 Dus, K. Sletten, K. Kamen, M.D. J. Biol. Chem. 24319685507-5518 Cytochrome c-2 of Rhodospirillum rubrum. II. Complete amino acid sequence and phylogenetic relationships. MUID69080147 A00084 protein 24-67,'N',69-95,'N',97-135 Bhatia, G. Finzel, B.C. Kraut, J. submitted to the Brookhaven Protein Data Bank November1983 PDB2C2C annotation X-ray crystallography, 2.0 angstroms, oxidized form, residues 24-67,'N',69-95,'N',97-135 Bhatia, G. Finzel, B.C. Kraut, J. submitted to the Brookhaven Protein Data Bank November1983 PDB3C2C annotation X-ray crystallography, 1.68 angstroms, reduced form, residues 24-67,'N',69-95,'N',97-135 Salemme, F.R. Freer, S.T. Xuong, N.H. Alden, R.A. Kraut, J. J. Biol. Chem. 24819733910-3921 The structure of oxidized cytochrome c-2 of Rhodospirillum rubrum. MUID73187380 annotation X-ray crystallography, 2.0 angstroms Salemme, F.R. Freer, S.T. Alden, R.A. Kraut, J. Biochem. Biophys. Res. Commun. 54197347-52 Atomic coordinates for ferricytochrome c-2 of Rhodospirillum rubrum. MUID74003179 annotation X-ray crystallographic coordinates A mobile electron carrier in the cyclic photosynthetic electron transport system, cytochrome c2 accepts electrons from the cytochrome bc1 complex and turns them over to photochemically oxidized reaction center. cycA cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain signal sequence 1-23 predicted product cytochrome c2 24-135 experimental domain cytochrome c homology 28-131 binding-site heme (Cys) (covalent) 37,40 experimental binding-site heme iron (His, Met) (axial ligands) 41,114 experimental 135 complete MKKGFLAAGVFAAVAFASGAALAEGDAAAGEKVSKKCLACHTFDQGGANKVGPNLFGVFE NTAAHKDDYAYSESYTEMKAKGLTWTEANLAAYVKDPKAFVLEKSGDPKAKSKMTFKLTK DDEIENVIAYLKTLK
CCQF2P A00085 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c2 Rhodospirillum photometricum Rhodospirillum photometricum Hermoso, J. Pettigrew, G.W. Kamen, M.D. unpublished results, cited by Ambler, R.P., in Evolution of Protein Molecules, Matsubara, H., and Yamanaka, T., eds., pp.311-322, Japan Scientific Societies Press/Center for Academic Publications Japan, Tokyo 1978 A00085 protein 1-113 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c homology 5-109 binding-site heme (Cys) (covalent) 15,18 predicted binding-site heme iron (His, Met) (axial ligands) 19,92 predicted 113 complete tentative AGDAAVGEKIAKAKC(T)ACHD(L)NKGGPIKVGPPLFGVFGRTTGTFAGYSYSPGYTVM G(Q)KGHTWDDNALKAYLLDPKGYVQAKSGDPKANSKMIFRLEKDDDVANVIAYLHTMK
CCRF2C A25452 A00086 24-Apr-1984 30-Sep-1991 03-Mar-2000
cytochrome c2 precursor Rhodobacter capsulatus Rhodobacter capsulatus Daldal, F. Cheng, S. Applebaum, J. Davidson, E. Prince, R.C. Proc. Natl. Acad. Sci. U.S.A. 8319862012-2016 Cytochrome c2 is not essential for photosynthetic growth of Rhodopseudomonas capsulata. A25452 DNA 1-137 strain SB1003 Ambler, R.P. Daniel, M. Hermoso, J. Meyer, T.E. Bartsch, R.G. Kamen, M.D. Nature 2781979659-660 Cytochrome c-2 sequence variation among the recognised species of purple nonsulphur photosynthetic bacteria. MUID79199667 A00086 protein 22-137 strain St. Louis, ATCC 23782, and strain 2.3.1, ATCC 11166 the sequence from strain 2.3.1 differs from that shown in having 108-Thr and 115-Ser cycA cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain signal sequence 1-21 predicted product cytochrome c2 22-137 experimental domain cytochrome c homology 25-132 binding-site heme (Cys) (covalent) 34,37 predicted binding-site heme iron (His, Met) (axial ligands) 38,117 predicted 137 complete MKISLTAATVAALVLAAPAFAGDAAKGEKEFNKCKTCHSIIAPDGTEIVKGAKTGPNLYG VVGRTAGTYPEFKYKDSIVALGASGFAWTEEDIATYVKDPGAFLKEKLDDKKAKTGMAFK LAKGGEDVAAYLASVVK
CCBC5E JT0008 30-Sep-1988 30-Sep-1988 03-Mar-2000
cytochrome c551 Erythrobacter sp. Erythrobacter sp. Okamura, K. Miyata, T. Iwanaga, S. Takamiya, K.I. Nishimura, M. J. Biochem. 1011987957-963 Complete amino acid sequence of cytochrome c551 from Erythrobacter species strain OCh 114. MUID87279991 JT0008 protein 1-119 strain OCh 114 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c homology 5-111 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,96 predicted 119 complete EGDIEAGEKAFNKCKSCHQIVSDAGEEIVKGGRTGPNLYGVLGRQAGTADFRYGDDLVAA GEAGLVWDADNFVEYVTDPRAFLRAYLDDSKAKSKMAYKLRSGGEDIAAYLASVSGSSS
CCRF2S A38896 A42458 A25160 A00087 JC4794 T50720 24-Apr-1984 30-Sep-1991 17-Nov-2000
cytochrome c2 precursor [validated] Rhodobacter sphaeroides Rhodobacter sphaeroides MacGregor, B.J. Donohue, T.J. submitted to GenBank July1991 Evidence for two promoters for the cytochrome c-2 gene (cycA) of Rhodobacter sphaeroides. A38896 DNA 1-145 GBM64777 NIDg151891 PIDNAAA26099.1 PIDg151892 MacGregor, B.J. Donohue, T.J. J. Bacteriol. 17319913949-3957 Evidence for two promoters for the cytochrome c-2 gene (cycA) of Rhodobacter sphaeroides. MUID91286176 A42458 DNA 1-61;82-145 GBM64777 the sequence of residues 62-81 was omitted in reference A42458 Donohue, T.J. McEwan, A.G. Kaplan, S. J. Bacteriol. 1681986962-972 Cloning, DNA sequence, and expression of the Rhodobacter sphaeroides cytochrome c2 gene. MUID87056995 A25160 DNA 1-145 GBM14501 NIDg151895 PIDNAAA26101.1 PIDg151896 Ambler, R.P. Meyer, T.E. submitted to the Atlas July1974 A00087 protein 22-145 the source is designated as Rhodopseudomonas sphaeroides, strain 2.4.1 Gans, P. Simorre, J.P. Caffrey, M. Marion, D. Richaud, P. Vermeglio, A. J. Biochem. 11919961131-1142 Sequential 1H and 15N NMR resonance assignment and secondary structure of ferrocytochrome c2 from Rhodobacter sphaeroides. MUID96424998 sequence conformation by (1)H- and (15)N-NMR, residues 22-145 JC4794 protein 22-145 Axelrod, H.L. Feher, G. Allen, J.P. Chirino, A.J. Day, M.W. Hsu, B.T. Rees, D.C. submitted to the Brookhaven Protein Data Bank April1994 PDB2CXB annotation X-ray crystallography, 1.95 angstroms, residues 23-145 Axelrod, H.L. Feher, G. Allen, J.P. Chirino, A.J. Day, M.W. Hsu, B.T. Rees, D.C. submitted to the Brookhaven Protein Data Bank February1994 PDB1CXC annotation X-ray crystallography, 1.6 angstroms, residues 22-145 Choudhary, M. Kaplan, S. Nucleic Acids Res. 282000862-867 DNA sequence analysis of the photosynthesis region of Rhodobacter sphaeroides 2.4.1. MUID20115911 T50720 preliminary translated from GB/EMBL/DDBJ DNA 1-145 EMBLAF195122 PIDNAAF24264.1 strain 2.4.1 cycA cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein photosynthesis pyroglutamic acid domain signal sequence 1-21 predicted product cytochrome c2 22-145 experimental domain cytochrome c homology 27-138 modified-site pyrrolidone carboxylic acid (Gln) (in mature form) 22 experimental binding-site heme (Cys) (covalent) 36,39 experimental binding-site heme iron (His, Met) (axial ligands) 40,121 experimental 145 complete MKFQVKALAAIAAFAALPALAQEGDPEAGAKAFNQCQTCHVIVDDSGTTIAGRNAKTGPN LYGVVGRTAGTQADFKGYGEGMKEAGAKGLAWDEEHFVQYVQDPTKFLKEYTGDAKAKGK MTFKLKKEADAHNIWAYLQQVAVRP
CCPC50 S08269 A35409 B35121 A00088 24-Apr-1984 20-Aug-1994 28-Jul-2000
cytochrome c2 precursor [validated] cytochrome c550 Paracoccus denitrificans Paracoccus denitrificans Raitio, M. Pispa, J.M. Metso, T. Saraste, M. FEBS Lett. 2611990431-435 Are there isoenzymes of cytochrome c oxidase in Paracoccus denitrificans? MUID90184495 S08269 DNA 1-155 EMBLY07533 NIDg45477 PIDNCAA68820.1 PIDg45478 Van Spanning, R.J.M. Wansell, C. Harms, N. Oltmann, L.F. Stouthamer, A.H. J. Bacteriol. 17219903534 MUID90264363 erratum A35409 DNA 1-155 GBM27304 NIDg150573 PIDNAAA88364.1 PIDg150574 this is a revision to the sequence from reference A35121 Van Spanning, R.J.M. Wansell, C. Harms, N. Oltmann, L.F. Stouthamer, A.H. J. Bacteriol. 1721990986-996 Mutagenesis of the gene encoding cytochrome c-550 of Paracoccus denitrificans and analysis of the resultant physiological effects. MUID90130336 B35121 DNA 1-51,'SEEGFKYGEGIL',52-68,81-155 GBM27304 this sequence has been revised in reference A35409 Ambler, R.P. submitted to the Atlas February1981 A00088 protein 21-149 ATCC 13543 Benning, M.M. Meyer, T.E. Holden, H.M. submitted to the Brookhaven Protein Data Bank July1994 PDB1COT annotation X-ray crystallography, 1.7 angstroms, residues 22-142 Benning, M.M. Meyer, T.E. Holden, H.M. Arch. Biochem. Biophys. 3101994460-466 X-ray structure of the cytochrome C-2 isolated from Paracoccus denitrificans refined to 1.7-angstroms resolution. MUID94234725 annotation X-ray crystallography, 1.7 angstroms Ambler, R.P. Meyer, T.E. Kamen, M.D. Schichman, S.A. Sawyer, L. J. Mol. Biol. 1471981351-356 A reassessment of the structure of Paracoccus cytochrome c-550. MUID82033207 annotation 50% of the molecules lack the carboxyl-terminal Ala confirmation of the sequence altered some interpretations of the crystallographic structure Timkovich, R. Dickerson, R.E. J. Biol. Chem. 25119764033-4046 The structure of Paracoccus denitrificans cytochrome c550. MUID76213273 annotation X-ray crystallography, 2.45 angstroms cycA cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation pyroglutamic acid domain signal sequence 1-20 predicted product cytochrome c550 21-155 experimental domain cytochrome c homology 26-135 modified-site pyrrolidone carboxylic acid (Gln) (in mature form) 21 experimental binding-site heme (Cys) (covalent) 35,38 experimental binding-site heme iron (His, Met) (axial ligands) 39,120 experimental 155 complete MKISIYATLAAITLALPAAAQDGDAAKGEKEFNKCKACHMIQAPDGTDIIKGGKTGPNLY GVVGRKIASEEGFKYGEGILEVAEKNPDLTWTEADLIEYVTDPKPWLVKMTDDKGAKTKM TFKMGKNQADVVAFLAQNSPDAGGDGEAAAEGESN
CCTW5T A00112 04-Dec-1986 04-Dec-1986 17-Nov-2000
cytochrome c552 [validated] Thermus aquaticus Thermus aquaticus Titani, K. Ericsson, L.H. Hon-nami, K. Miyazawa, T. Biochem. Biophys. Res. Commun. 1281985781-787 Amino acid sequence of cytochrome c-552 from Thermus thermophilus HB8. MUID85199131 A00112 protein 1-131 the source was designated as Thermus thermophilus Than, M.E. Hof, P. Huber, R. Bourenkov, G.P. Bartunik, H.D. Buse, G. Soulimane, T. submitted to the Protein Data Bank June1997 PDB1C52 annotation X-ray crystallography, 1.28 angstroms, residues 1-131 Than, M.E. Hof, P. Huber, R. Bourenkov, G.P. Bartunik, H.D. Buse, G. Soulimane, T. J. Mol. Biol. 2711997629-644 Thermus thermophilus cytochrome-c552: a new highly thermostable cytochrome-c structure obtained by MAD phasing. MUID97428333 annotation X-ray crystallography, 1.28 angstroms This cytochrome appears to function as an electron donor to cytochrome oxidase; it may be a c2-type cytochrome but is distantly related to other cytochromes. T. aquaticus cytochrome c552 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein pyroglutamic acid domain cytochrome c6 homology 2-87 modified-site pyrrolidone carboxylic acid (Gln) 1 experimental binding-site heme (Cys) (covalent) 11,14 experimental binding-site heme iron (His, Met) (axial ligands) 15,69 experimental 131 complete QADGAKIYAQCAGCHQQNGQGIPGAFPPLAGHVAEILAKEGGREYLILVLLYGLQGQIEV KGMKYNGVMSSFAQLKDEEIAAVLNHIATAWGDAKKVKGFKPFTAEEVKKLRAKKLTPQQ VLAERKKLGLK
B81167 B81167 01-Sep-2000 01-Sep-2000 19-Jan-2001
cytochrome c552 NMB0717 precursor [similarity] Neisseria meningitidis (strain MC58 serogroup B) Neisseria meningitidis Tettelin, H. Saunders, N.J. Heidelberg, J. Jeffries, A.C. Nelson, K.E. Eisen, J.A. Ketchum, K.A. Hood, D.W. Peden, J.F. Dodson, R.J. Nelson, W.C. Gwinn, M.L. DeBoy, R. Peterson, J.D. Hickey, E.K. Haft, D.H. Salzberg, S.L. White, O. Fleischmann, R.D. Dougherty, B.A. Mason, T. Ciecko, A. Parksey, D.S. Blair, E. Cittone, H. Clark, E.B. Cotton, M.D. Utterback, T.R. Khouri, H. Qin, H. Vamathevan, J. Gill, J. Scarlato, V. Masignani, V. Pizza, M. Grandi, G. Sun, L. Smith, H.O. Fraser, C.M. Moxon, E.R. Rappuoli, R. Venter, J.C. Science 28720001809-1815 Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. MUID20175755 B81167 DNA 1-138 GBAE002426 GBAE002098 NIDg7225939 PIDNAAF41130.1 PIDg7225943 GSPDBGN00119 TIGRNMB0717 serogroup B, strain MC58 NMB0717 T. aquaticus cytochrome c552 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-26 predicted product cytochrome c552 27-138 predicted domain cytochrome c6 homology 33-114 binding-site heme (Cys) (covalent) 43,46 predicted binding-site heme iron (His, Met) (axial ligands) 47,97 predicted 138 complete MKETPMNTTRLPTALVLGCFCAAASAADNSIMTKGQKVYESNCVACHGKKGEGRGTMFPP LYRSDFIMKKPQVLLHSMVKGINGTIKVNGKTYNGFMPATAISDADIAAVATYIMNAFDN GGGSVTEKDVKQAKSKKN
F81938 F81938 01-Sep-2000 01-Sep-2000 02-Feb-2001
cytochrome c552 NMA0925 precursor [similarity] Neisseria meningitidis (strain Z2491 serogroup A) Neisseria meningitidis Parkhill, J. Achtman, M. James, K.D. Bentley, S.D. Churcher, C. Klee, S.R. Morelli, G. Basham, D. Brown, D. Chillingworth, T. Davies, R.M. Davis, P. Devlin, K. Feltwell, T. Hamlin, N. Holroyd, S. Jagels, K. Leather, S. Moule, S. Mungall, K. Quail, M.A. Rajandream, M.A. Rutherford, K.M. Simmonds, M. Skelton, J. Whitehead, S. Spratt, B.G. Barrell, B.G. Nature 4042000502-506 Complete DNA sequence of a serogroup A strain of Neisseria menigitidis Z2491. MUID20222556 F81938 DNA 1-163 GBAL162754 GBAL157959 NIDg7379424 PIDNCAB84197.1 PIDg7379630 GSPDBGN00124 NMASPNMA0925 serogroup A, strain Z2491 NMA0919 NMA0925 T. aquaticus cytochrome c552 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-21 predicted product cytochrome c552 22-163 predicted domain cytochrome c6 homology 28-109 binding-site heme (Cys) (covalent) 38,41 predicted binding-site heme iron (His, Met) (axial ligands) 42,92 predicted 163 complete MNTTRLPTALVLGCLCAAASAADNSIMTKGQKVYESNCVACHGKKGEGRGTMFPPLYRSD FIMKKPQVLLHSMVKGINGTIKVNGKTYNGFMPATAISDADIAAVATYIMNAFDNGGGSV TEKDVKQAKNKKKTKQTKCRLKPAIRLQTAFKSNLSNAVLSAP
CCPC54 A00097 S06255 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c554 Paracoccus sp. Paracoccus sp. Ambler, R.P. The Evolution of Metalloenzymes, Metalloproteins and Related Materials, Leigh, G.J., ed., pp.100-118, Symposium Press, London 1977 Cytochrome c and copper protein evolution in prokaryotes. A00097 protein 1-83 ATCC 12084 Ambler, R.P. Daniel, M. McLellan, L. Meyer, T.E. Cusanovich, M.A. Kamen, M.D. Biochem. J. 2481987365-371 Amino acid sequences of cytochrome c-554(548) and cytochrome c' from a halophilic denitrifying bacterium of the genus Paracoccus. MUID88133881 S06255 protein 1-83 ATCC 12084 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme homodimer iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 5-79 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,63 predicted 83 complete AGDAAAGEDKIGTCVACHGTDGQGLAPIYPNLTGQSATYLESSIKAYRDGQRKGGNAALM TPMAQGLSDEDIADIAAYYSSQE
CCMP55 A23321 A05021 28-Dec-1987 28-Dec-1987 03-Mar-2000
cytochrome c555 Methylococcus capsulatus Methylococcus capsulatus Ambler, R.P. Dalton, H. Meyer, T.E. Bartsch, R.G. Kamen, M.D. Biochem. J. 2331986333-337 The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus. MUID86158741 A23321 protein 1-96 strain Bath, NCIB 11132 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 8-79 binding-site heme (Cys) (covalent) 19,22 experimental binding-site heme iron (His, Met) (axial ligands) 23,59 predicted 96 complete APVDQATYNGFKIYKQQRCETCHGATGEGSAAFPNLLNSLKNLSKDQFKEVVLKGRNAMP PFEANKKVAEGIDDLYTYIKGRSDGTVPAGELEKPQ
CCML6 A00099 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f golden alga (Monochrysis lutheri) Monochrysis lutheri Laycock, M.V. Can. J. Biochem. 5019721311-1325 The amino acid sequence of cytochrome c-553 from the chrysophycean alga Monochrysis lutheri. MUID73080382 A00099 protein 1-83 Laycock, M.V. submitted to the Atlas December1974 annotation amidation states, residues 2, 5, 7, 8, 13, and 73 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein methylated amino acid photosynthesis domain cytochrome c6 homology 4-78 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,59 predicted modified-site N6-methyllysine (Lys) (partial) 24 experimental 83 complete GDIANGEQVFTGNCAACHSVZZZKTLELSSLWKAKSYLANFNGDESAIVYQVTNGKNAMP AFGGRLEDDEIANVASYVLSKAG
CCPF6 A00100 18-Aug-1982 18-Aug-1982 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f brown alga (Petalonia fascia) Petalonia fascia Sugimura, Y. Hase, T. Matsubara, H. Shimokoriyama, M. J. Biochem. 9019811213-1219 Studies on algal cytochromes. III. Amino acid sequence of cytochrome c-553 from a brown alga, Petalonia fascia. MUID82075747 A00100 protein 1-85 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 85 complete VDINNGESVFTANCSACHAGGNNVIMPEKTLKKDALEENEMNNIKSITYQVTNGKNAMPA FGGRLSETDIEDVANFVISQSQKGW
CCAU6 A00101 08-Oct-1981 08-Oct-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f brown alga (Alaria esculenta) Atlantic wakame, badderlocks, murlin, henware Alaria esculenta Laycock, M.V. Biochem. J. 1491975271-279 The amino acid sequence of cytochrome f from the brown alga Alaria esculenta (L.) Grev. MUID76061523 A00101 protein 1-86 Cytochrome c6 is a monoheme monomer. It functions as an electron carrier between membrane-bound cytochrome f and P700 in the photophosphorylation chain in chloroplasts and algae. It substitutes for plastocyanin in copper-deficient blue-green algae and in the chloroplasts of some eukaryote algae. cytochrome c6 cytochrome c6 homology acetylated amino end chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 modified-site acetylated amino end (Ile) 1 absent binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 86 complete IDINNGENIFTANCSACHAGGNNVIMPEKTLKKDALADNKMVSVNAITYQVTNGKNAMPA FGSRLAETDIEDVANFVLTQSDKGWD
CCBF6 A00102 17-May-1985 17-May-1985 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f yellow-green alga (Bumilleriopsis filiformis) Bumilleriopsis filiformis Ambler, R. unpublished results, cited by Dickerson, R.E., in The Evolution of Protein Structure and Function, Sigman, D.S., and Brazier, M.A.B., eds., pp.173-202, Academic Press, New York and London 1980 A00102 protein 1-86 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 86 complete ADIENGERIFTANCAACHAGGNNVIMPEKTLKKDALEANGMNAVSAITYQVTNGKNAMPA FGGRLSDSDIEDVANYVLSQSEQGWD
CCPR6 A00103 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f red alga (Porphyra tenera) Porphyra tenera Ambler, R.P. Meyer, T.E. Bartsch, R.G. submitted to the Atlas August1973 A00103 protein 1-85 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 85 complete ADLDNGEKVFSANCAACHAGGNNAIMPDKTLKKDVLEANSMNTIDAITYQVQNGKNAMPA FGGRLVDEDIEDAANYVLSQSEKGW
CCIA6 A00104 17-Dec-1982 17-Dec-1982 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Microcystis aeruginosa Microcystis aeruginosa Beecher, J. Margoliash, E. unpublished results, cited by Ulrich, E.L., Krogmann, D.W., and Markley, J.L., J. Biol. Chem. 257, 9356-9364 1982 A00104 protein 1-80 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 1-72 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,53 predicted 80 complete DGASIFSANCASCHMGGKNVVNAAKTLKKEDLVGGKNAVEAIVTQVTKGKGAMPAFGGRL GAEDIEAVANYVLAEAEKGW
CCAI6 A94488 A93182 A00105 17-Dec-1982 17-Dec-1982 31-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Anabaena variabilis Anabaena variabilis Beecher, J. Margoliash, E. unpublished results, cited by Ulrich, E.L., Krogmann, D.W., and Markley, J.L., J. Biol. Chem. 257, 9356-9364 1982 A94488 protein 1-86 Aitken, A. Nature 2631976793-796 Protein evolution in cyanobacteria. MUID77056395 A93182 protein 1-22;30-39;56-81,'D',83,'D',85-86 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 86 complete tentative ADSVNGAKIFSANCASCHAGGKNLGVAQKTLKKADLEKY(G.A.Y)SAMAIGAQVTNGKN AMPAFKGRLKPEEIZBVAAYVLGKAEAEWK
S03859 S03859 28-Feb-1990 13-Sep-1996 03-Mar-2000
cytochrome c6 cytochrome c553 Microcystis aeruginosa Microcystis aeruginosa Cohn, C.L. Hermodson, M.A. Krogmann, D.W. Arch. Biochem. Biophys. 2701989219-226 The amino acid sequence of cytochrome c553 from Microcystis aeruginosa. MUID89192371 S03859 protein 1-81 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 1-73 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,54 predicted 81 complete DGASIFSANCASCHMGGKNVVNAAKTLKKEDLVKYGKDSVEAIVTQVTKGMGAMPAFGGR LSAEDIEAVANYVLAQAEKGW
CCAI53 S22481 S18858 31-Dec-1992 31-Dec-1992 03-Mar-2000
cytochrome c6 precursor cytochrome c553 soluble cytochrome f Anabaena sp. (strain PCC 7937) Anabaena sp. Bovy, A. de Vrieze, G. Borrias, M. Weisbeek, P. Plant Mol. Biol. 191992491-492 Isolation and sequence analysis of a gene encoding a basic cytochrome c-553 from the cyanobacterium Anabaena SP.PCC 7937. MUID92322981 S22481 DNA 1-111 EMBLX63194 NIDg312896 PIDNCAA44876.1 PIDg39235 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain signal sequence 1-25 predicted product cytochrome c6 26-111 predicted domain cytochrome c6 homology 29-102 binding-site heme (Cys) (covalent) 39,42 predicted binding-site heme iron (His, Met) (axial ligands) 43,83 predicted 111 complete MKKIFSLVLLGIALFTFAFSSPALAADVANGAKIFSANCASCHAGGKNLVQAQKTLKKED LEKFGMYSAEAIIAQVTNGKNAMPAFKGRLKPDQIEDVAAYVLGQADKSWK
JQ1083 JQ1083 A05180 31-Dec-1991 13-Sep-1996 03-Nov-2000
cytochrome c6 precursor cytochrome c553 soluble cytochrome f Synechococcus sp. (strain PCC 7942) Synechococcus sp. Laudenbach, D.E. Herbert, S.K. McDowell, C. Fork, D.C. Grossman, A.R. Straus, N.A. Plant Cell 21990913-924 Cytochrome c-553 is not required for photosynthetic activity in the cyanobacterium Synechococcus. MUID93005680 JQ1083 DNA 1-111 GBS44426 NIDg256651 PIDNAAB23485.1 PIDg256652 Margoliash, E. unpublished results, cited by Dickerson, R.E., in The Evolution of Protein Structure and Function, Sigman, D.S., and Brazier, M.A.B., eds., pp.173-202, Academic Press, New York and London 1980 A05180 protein 25-39,'S',41-55,'E',57-61,'E',63-86,'A',88-94,'EG',97-100,'A',102-105,'G',107,'E',109 the source is designated as Anacystis nidulans This protein functions as a mobile carrier of electrons between the membrane-bound cytochrome b6-f complex and the p-700 reaction center of photosystem I in cyanobacteria and many eukaryotic algae. cytA cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain signal sequence 1-24 predicted product cytochrome c6 25-111 predicted domain cytochrome c6 homology 28-101 binding-site heme (Cys) (covalent) 38,41 predicted binding-site heme iron (His, Met) (axial ligands) 42,82 predicted 111 complete MKRILGTAIAALVVLLAFIAPAQAADLAHGGQVFSANCAACHLGGRNVVNPAKTLQKADL DQYGMASIEAITTQVTNGKGAMPAFGSKLSADDIADVASYVLDQSEKGWQG
A53328 A53328 S77507 03-May-1994 13-Sep-1996 16-Jun-2000
cytochrome c6 precursor Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Zhang, L. Pakrasi, H.B. Whitmarsh, J. J. Biol. Chem. 26919945036-5042 Photoautotrophic growth of the cyanobacterium Synechocystis sp. PCC 6803 in the absence of cytochrome c-553 and plastocyanin. MUID94148959 A53328 preliminary not compared with conceptual translation DNA 1-120 GBL25252 NIDg468928 PIDNAAA17489.1 PIDg468929 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S77507 preliminary DNA 1-120 EMBLD90905 GBAB001339 NIDg1652360 PIDNBAA17354.1 PIDg1652432 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain signal sequence 1-35 predicted product cytochrome c6 36-120 predicted domain cytochrome c6 homology 39-112 binding-site heme (Cys) (covalent) 49,52 predicted binding-site heme iron (His, Met) (axial ligands) 53,93 predicted 120 complete MFKLFNQASRIFFGIALPCLIFLGGIFSLGNTALAADLAHGKAIFAGNCAACHNGGLNAI NPSKTLKMADLEANGKNSVAAIVAQITNGNGAMPGFKGRISDSDMEDVAAYVLDQAEKGW
CCYC6L A00106 31-Jan-1980 31-Jan-1980 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Synechococcus lividus Synechococcus lividus Borden, D. Margoliash, E. submitted to the Atlas December1979 A00106 protein 1-87 Cytochrome c6 substitutes for plastocyanin in copper-deficient blue-green algae and the chloroplasts of some eukaryotic algae. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 87 complete ADLANGAKVFSGNCAACHMGGGNVVMANKTLKKEALEQFGMNSEDAIIYQVQHGKNAMPA FAGRLTDEQIQDVAAYVLDQAAKGWAG
CCYC6 A00107 31-Jan-1980 23-Oct-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Synechococcus sp. (ATCC 27167) Synechococcus sp. Aitken, A. Eur. J. Biochem. 1011979297-308 Purification and primary structure of cytochrome c-552 from the cyanobacterium, Synechococcus PCC 6312. MUID80068924 A00107 protein 1-87 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 87 complete ADIADGAKVFSANCAACHMGGGNVVMANKTLKKEALEQFGMNSADAIMYQVQNGKNAMPA FGGRLSEAQIENVAAYVLDQSSNKWAG
CCFZ6 A00108 17-Dec-1982 17-Dec-1982 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Aphanizomenon flos-aquae Aphanizomenon flos-aquae Sprinkle, J. Hermodson, M. Krogmann, D.W. unpublished results, cited by Ulrich, E.L., Krogmann, D.W., and Markley, J.L., J. Biol. Chem. 257, 9356-9364 1982 A00108 protein 1-87 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 87 complete ADTVSGAALFKANCAQCHVGGGNLVNRAKTLKKEALEKYNMYSAKAIIAQVTHGKGAMPA FGIRLKAEQIENVAAYVLEQADNGWKK
CCPB6 A00109 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Plectonema boryanum Plectonema boryanum Aitken, A. Eur. J. Biochem. 781977273-279 Purification and primary structure of cytochrome f from the cyanobacterium, Plectonema boryanum. MUID78023897 A00109 protein 1-85 CCAP 1462/2 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-77 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,58 predicted 85 complete ADAAAGGKVFNANCAACHASGGGQINGAKTLKKNALTANGKDTVEAIVAQVTNGKGAMPA FKGRLSDDQIQSVALYVLDKAEKGW
CCSG6 A00110 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Spirulina maxima Spirulina maxima Ambler, R.P. Bartsch, R.G. Nature 2531975285-288 Amino acid sequence similarity between cytochrome f from a blue-green bacterium and algal chloroplasts. MUID75100362 A00110 protein 1-89 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-81 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,62 predicted 89 complete GDVAAGASVFSANCAACHMGGRNVIVANKTLSKSDLAKYLKGFDDDAVAAVAYQVTNGKN AMPGFNGRLSPKQIEDVAAYVVDQAEKGW
CCPSS S13940 S68356 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c, nitrite reductase associated, precursor nirC protein Pseudomonas stutzeri (strain ZoBell) Pseudomonas stutzeri strain ZoBell Juengst, A. Wakabayashi, S. Matsubara, H. Zumft, W.G. FEBS Lett. 2791991205-209 The nirSTBM region coding for cytochrome cd(1)-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins. MUID91160715 S13940 DNA 1-113 EMBLX56813 NIDg45838 PIDNCAA40154.1 PIDg45843 strain ZoBell Palmedo, G. Seither, P. Koerner, H. Matthews, J.C. Burkhalter, R.S. Timkovich, R. Zumft, W.G. Eur. J. Biochem. 2321995737-746 Resolution of the nirD locus for heme d(1) synthesis of cytochrome cd(1) (respiratory nitrite reductase) from Pseudomonas stutzeri. MUID96028114 S68356 DNA 103-113 EMBLZ50198 strain ZoBell nirC cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein periplasmic space domain signal sequence 1-26 predicted product cytochrome c, nitrite reductase associated 27-113 predicted domain cytochrome c6 homology 35-106 binding-site heme (Cys) (covalent) 45,48 predicted binding-site heme iron (His, Met) (axial ligands) 49,87 predicted 113 complete MTVARHAVSRLGLALASFLLFPLALAAAPAAERQATLDHLLLQDCGSCHGLRMTGGLGPA LTREALAGKPRDSLIATVTHGRPGTAMPGWNALLDEQDIAYLVDRLLEGYPKP
CCKM6R A27113 A39341 30-Sep-1993 03-Oct-1995 03-Mar-2000
cytochrome c6 precursor cytochrome C552 Chlamydomonas reinhardtii Chlamydomonas reinhardtii Merchant, S. Bogorad, L. J. Biol. Chem. 26219879062-9067 The Cu(II)-repressible plastidic cytochrome c. Cloning and sequence of a complementary DNA for the pre-apoprotein. MUID87250547 A27113 mRNA 1-106,'S',108-148 GBJ02774 NIDg167406 PIDNAAA33081.1 PIDg167407 parts of this sequence, including the amino end of the mature protein, were determined by protein sequencing 107-Ile was observed in the protein sequence Hill, K.L. Li, H.H. Singer, J. Merchant, S. J. Biol. Chem. 266199115060-15067 Isolation and structural characterization of the Chlamydomonas reinhardtii gene for cytochrome c-6. Analysis of the kinetics and metal specificity of its copper-responsive expression. MUID91332023 A39341 DNA 1-148 GBM67448 NIDg167414 PIDNAAB00729.1 PIDg167415 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain transit peptide (chloroplast) 1-58 predicted product cytochrome c6 59-148 experimental domain cytochrome c6 homology 62-137 binding-site heme (Cys) (covalent) 72,75 predicted binding-site heme iron (His, Met) (axial ligands) 76,118 predicted 148 complete MLQLANRSVRAKAARASQSARSVSCAAAKRGADVAPLTSALAVTASILLTTGAASASAAD LALGAQVFNGNCAACHMGGRNSVMPEKTLDKAALEQYLDGGFKVESIIYQVENGKGAMPA WADRLSEEEIQAVAEYVFKQATDAAWKY
S35677 S35677 10-Dec-1993 13-Sep-1996 20-Apr-2000
cytochrome c6 [validated] cytochrome c552 green alga (Monoraphidium braunii) Monoraphidium braunii Campos, A.P. Aguiar, A.P. Hervas, M. Regalla, M. Navarro, J.A. Ortega, J.M. Xavier, A.V. de la Rosa, M.A. Teixeira, M. Eur. J. Biochem. 2161993329-341 Cytochrome c(6) from Monoraphidium braunii. A cytochrome with an unusual heme axial coordination. MUID93373943 S35677 protein 1-89 Sheldrick, G.M. submitted to the Brookhaven Protein Data Bank August1995 PDB1CTJ annotation X-ray crystallography, 1.1 angstroms, residues 1-89 Banci, L. Bertini, I. De la Rosa, M.A. Koulougliotis, D. Navarro, J.A. Walter, O. Biochemistry 3719984831-4843 Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii. MUID98206900 annotation conformation by (1)H-NMR Banci, L. Bertini, I. Quacquarini, G. Walter, O. Diaz, A. Hervas, M. De La Rosa, M.A. submitted to the Brookhaven Protein Data Bank March1996 PDB1CED annotation conformation by (1)H-NMR, reduced form, residues 1-89 Banci, L. Bertini, I. De La Rosa, M.A. Koulougliotis, D. Navarro, J.A. Walter, O. submitted to the Brookhaven Protein Data Bank January1998 PDB1A2S annotation conformation by (1)H-NMR, oxidized form, residues 1-89 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c6 homology 5-80 binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,61 experimental 89 complete EADLALGKAVFDGNCAACHAGGGNNVIPDHTLQKAAIEQFLDGGFNIEAIVYQIENGKGA MPAWDGRLDEDEIAGVAAYVYDQAAGNKW
CCBM6 A30021 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f green alga (Bryopsis maxima) Bryopsis maxima Okamoto, Y. Minami, Y. Matsubara, H. Sugimura, Y. J. Biochem. 10219871251-1260 Studies on algal cytochromes VI: some properties and amino acid sequence of cytochrome c-6 from a green alga, Bryopsis maxima. MUID88139277 A30021 protein 1-88 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 5-80 binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,61 predicted 88 complete GGDLEIGADVFTGNCAACHAGGANSVEPLKTLNKEDVTKYLDGGLSIEAITSQVRNGKGA MPAWSDRLDDEEIDGVVAYVFKNINEGW
CCEG6 A00111 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c6 cytochrome c553 soluble cytochrome f Euglena gracilis Euglena gracilis Pettigrew, G.W. Biochem. J. 1391974449-459 The purification and amino acid sequence of cytochrome c-552 from Euglena gracilis. MUID75090229 A00111 protein 1-87 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 1-75 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,56 predicted 87 complete GGADVFADNCSTCHVNGGNVISAGKVLSKTAIEEYLDGGYTKEAIEYQVRNGKGPMPAWE GVLSEDEIVAVTDYVYTQAGGAWANVS
S15453 S15453 13-Jan-1995 13-Sep-1996 03-Mar-2000
cytochrome c6 Euglena viridis Euglena viridis Ambler, R.P. Kamen, M.D. Bartsch, R.G. Meyer, T.E. Biochem. J. 276199147-52 Amino acid sequences of Euglena viridis ferredoxin and cytochromes c. MUID91248164 S15453 preliminary protein 1-87 cytochrome c6 cytochrome c6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein domain cytochrome c6 homology 1-75 binding-site heme (Cys) (covalent) 10,13 experimental binding-site heme iron (His, Met) (axial ligands) 14,56 predicted 87 complete SGAEVFGNNCSSCHVNGGNIIIPGHVLSQSAMEEYLDGGYTKEAIEYQVRNGKGPMPAWE GVLDESEIKEVTDYVYSQASGPWANAS
CCPSVM A00114 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c5 Pseudomonas mendocina Pseudomonas mendocina Ambler, R.P. Taylor, E. Biochem. Soc. Trans. 11973166-168 Amino acid sequence of cytochrome c-5 from Pseudomonas mendocina. A00114 protein 1-87 strain CH-110 This is a dimeric monoheme c-type cytochrome. It is unreactive with cytochrome c reductase or oxidase but seems to function as an intermediate in nitrate respiration of facultative anaerobic pseudmonads. It appears to be present also in the strictly anaerobic nitrogen-fixing Azotobacter. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c6 homology 8-84 binding-site heme (Cys) (covalent) 19,22 predicted binding-site heme iron (His, Met) (axial ligands) 23,63 predicted 87 complete AASAGGGARSADDIIAKHCNACHGAGVLGAPKIGDTAAWKERADHQGGLDGILAKAISGI NAMPPKGTCADCSDDELREAIQKMSGL
CCER51 S38755 A00115 30-Nov-1979 30-Nov-1979 03-Mar-2000
cytochrome c551 Ectothiorhodospira halophila Ectothiorhodospira halophila Ambler, R.P. Meyer, T.E. Kamen, M.D. Arch. Biochem. Biophys. 306199383-93 Amino acid sequences of cytochromes c-551 from the halophilic purple phototrophic bacteria, Ectothiorhodospira halophila and E. halochloris. MUID94028993 S38755 protein 1-78 Ambler, R.P. submitted to the Atlas August1979 A00115 protein 1-78 strain BN9626 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c6 homology 3-74 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,55 predicted 78 complete DGESIYINGTAPTCSSCHDRGVAGAPELNAPEDWADRPSSVDELVESTLAGKGAMPAYDG RADREDLVKAIEYMLSTL
CCCF55 A00116 13-Jul-1981 13-Jul-1981 03-Mar-2000
cytochrome c555 Chlorobium sp. Chlorobium sp. Van Beeumen, J. Ambler, R.P. Meyer, T.E. Kamen, M.D. Olson, J.M. Shaw, E.K. Biochem. J. 1591976757-774 The amino acid sequences of the cytochromes c-555 from two green sulphur bacteria of the genus Chlorobium. MUID77087088 A00116 protein 1-86 the source is designated as Chlorobium thiosulfatophilum Korszun, Z.R. Salemme, F.R. Proc. Natl. Acad. Sci. U.S.A. 7419775244-5247 Structure of cytochrome c555 of Chlorobium thiosulfatophilum: primitive low-potential cytochrome c. MUID78094383 annotation X-ray crystallography, 2.7 angstroms This basic c-type monoheme cytochrome has been found exclusively in the green photosynthetic bacteria, although its role in bacterial photosynthesis is not established. It has an unusually low redox potential compared with mitochondrial cytochrome c. It is reactive with cytochrome c oxidases but not with reductases. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 4-81 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,60 experimental 86 complete YDAAAGKATYDASCAMCHKTGMMGAPKVGDKAAWAPHIAKGMNVMVANSIKGYKGTKGMM PAKGGNPKLTDAQVGNAVAYMVGQSK
CCPH55 A00117 13-Jul-1981 13-Jul-1981 03-Mar-2000
cytochrome c555 Prosthecochloris aestuarii Prosthecochloris aestuarii Van Beeumen, J. Ambler, R.P. Meyer, T.E. Kamen, M.D. Olson, J.M. Shaw, E.K. Biochem. J. 1591976757-774 The amino acid sequences of the cytochromes c-555 from two green sulphur bacteria of the genus Chlorobium. MUID77087088 A00117 protein 1-99 the source is designated as Chlorobium limicola Olson, J.M. Int. J. Syst. Bacteriol. 281978128-129 annotation taxonomy cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 13-94 binding-site heme (Cys) (covalent) 23,26 predicted binding-site heme iron (His, Met) (axial ligands) 27,73 predicted 99 complete AVTKADVEQYDLANGKTVYDANCASCHAAGIMGAPKTGTARKWNSRLPQGLATMIEKSVA GYEGEYRGSKTFMPAKGGNPDLTDKQVGDAVAYMVNEVL
CCRFG2 A00089 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2 Rhodocyclus gelatinosus Rhodocyclus gelatinosus Ambler, R.P. Meyer, T.E. Kamen, M.D. Nature 2781979661-662 Anomalies in amino acid sequences of small cytochromes c and cytochromes c' from two species of purple photosynthetic bacteria. MUID79199668 A00089 protein 1-85 This sequence is more closely related to the sequences of cytochrome c551 from Pseudomonas and Azotobacter than to the sequences of cytochrome c2 from other species of Rhodopseudomonas. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 1-81 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,61 predicted 85 complete ATPAELATKAGCAVCHQPTAKGLGPSYQEIAKKYKGQAGAPALMAERVRKGSVGIFGKLP MTPTPPARISDADLKLVIDWILKTP
CCPS5A B34141 B34255 PC4130 A90346 B90272 B83582 A00091 24-Apr-1984 12-May-1994 06-Oct-2000
cytochrome c551 precursor [validated] cytochrome c8 Pseudomonas aeruginosa Pseudomonas aeruginosa Nordling, M. Young, S. Karlsson, B.G. Lundberg, L.G. FEBS Lett. 2591990230-232 The structural gene for cytochrome c-551 from Pseudomonas aeruginosa. The nucleotide sequence shows a location downstream of the nitrite reductase gene. MUID90092552 B34141 DNA 1-104 EMBLX51319 NIDg45305 PIDNCAA35703.1 PIDg45307 Arai, H. Sanbongi, Y. Igarashi, Y. Kodama, T. FEBS Lett. 2611990196-198 Cloning and sequencing of the gene encoding cytochrome c-551 from Pseudomonas aeruginosa. MUID90169115 B34255 DNA 1-104 GBX51631 NIDg45316 PIDNCAA35958.1 PIDg45318 Kawasaki, S. Arai, H. Igarashi, Y. Kodama, T. Gene 167199587-91 Sequencing and characterization of the downstream region of the genes encoding nitrite reductase and cytochrome c-551 (nirSM) from Pseudomonas aeruginosa: Identification of the gene necessary for biosynthesis of heme d1. MUID96144254 PC4130 DNA 'C',95-104 DDBJD50473 NIDg1217594 Ambler, R.P. Biochem. J. 891963349-378 The amino acid sequence of Pseudomonas cytochrome c-551. A90346 protein 23-104 strain P6009 Ambler, R.P. Biochem. J. 13719743-14 The evolutionary stability of cytochrome c-551 in Pseudomonas aeruginosa and Pseudomonas fluorescens biotype C. MUID74140216 B90272 protein 23-104 nine strains were analyzed the sequences from eight strains appear to be identical with that shown the sequence of strain 129/1224 differs from that shown in having 24-Ala Detlefsen, D.J. Thanabal, V. Pecoraro, V.L. Wagner, G. submitted to the Brookhaven Protein Data Bank May1993 PDB2PAC annotation conformation by (1)H-NMR, residues 23-104 Detlefsen, D.J. Thanabal, V. Pecoraro, V.L. Wagner, G. Biochemistry 3019919040-9046 Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional (1)H NMR. MUID91369910 annotation conformation by (1)H-NMR Matsuura, Y. Takano, T. Dickerson, R.E. submitted to the Brookhaven Protein Data Bank July1981 PDB351C annotation X-ray crystallography, 1.6 angstroms, oxidized, residues 23-104 Matsuura, Y. Takano, T. Dickerson, R.E. submitted to the Brookhaven Protein Data Bank July1981 PDB451C annotation X-ray crystallography, 1.6 angstroms, reduced, residues 23-104 Matsuura, Y. Takano, T. Dickerson, R.E. J. Mol. Biol. 1561982389-409 Structure of cytochrome c-551 from Pseudomonas aeruginosa refined at 1.6 angstrom resolution and comparison of the two redox forms. MUID82216851 annotation X-ray crystallography, 1.6 angstroms Stover, C.K. Pham, X.Q. Erwin, A.L. Mizoguchi, S.D. Warrener, P. Hickey, M.J. Brinkman, F.S.L. Hufnagle, W.O. Kowalik, D.J. Lagrou, M. Garber, R.L. Goltry, L. Tolentino, E. Westbrook-Wadman, S. Yuan, Y. Brody, L.L. Coulter, S.N. Folger, K.R. Kas, A. Larbig, K. Lim, R.M. Smith, K.A. Spencer, D.H. Wong, G.K.S. Wu, Z. Paulsen, I.T. Reizer, J. Saier, M.H. Hancock, R.E.W. Lory, S. Olson, M.V. Nature 4062000959-964 Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. MUID20437337 B83582 preliminary DNA 1-104 GBAE004488 GBAE004091 NIDg9946372 PIDNAAG03907.1 GSPDBGN00131 PASPPA0518 strain PAO1 This monoheme cytochrome is unreactive with mitochondrial cytochrome c oxidase or reductase. It functions in nitrite and nitrate respiration in Pseudomonas. nirM PA0518 electron donor to Pseudomonas cytochrome oxidase (EC 1.9.3.2) nitrate respiration cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein nitrate respiration domain signal sequence 1-22 predicted product cytochrome c551 23-104 experimental domain cytochrome c6 homology 23-100 binding-site heme (Cys) (covalent) 34,37 experimental binding-site heme iron (His, Met) (axial ligands) 38,83 experimental 104 complete MKPYALLSLLATGTLLAQGAWAEDPEVLFKNKGCVACHAIDTKMVGPAYKDVAAKFAGQA GAEAELAQRIKNGSQGVWGPIPMPPNAVSDDEAQTLAKWVLSQK
CCQF2T A00090 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c2 Rhodocyclus tenuis Rhodocyclus tenuis Ambler, R.P. Meyer, T.E. Kamen, M.D. Nature 2781979661-662 Anomalies in amino acid sequences of small cytochromes c and cytochromes c' from two species of purple photosynthetic bacteria. MUID79199668 A00090 protein 1-92 This sequence is more closely related to the sequences of cytochrome c551 from Pseudomonas and Azotobacter than to the sequences of cytochrome c2 from other species of Rhodospirillum. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein photosynthesis domain cytochrome c6 homology 1-83 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,66 predicted 92 complete ADESALAQTKGCLACHNPEKKVVGPAYGWVAKKYAGQAGAEAKLVAKVMAGGQGVWAKQL GAEIPMPANNVTKEEATRLVKWVLSLKQIDYK
CCPS5F A00092 A90272 13-Jul-1981 13-Jul-1981 03-Nov-2000
cytochrome c551 [validated] Pseudomonas fluorescens (biotype C) Pseudomonas fluorescens Ambler, R.P. Wynn, M. Biochem. J. 1311973485-498 The amino acid sequences of cytochromes c-551 from three species of Pseudomonas. MUID73224976 A00092 protein 1-82 strain C18, ATCC 17400 Ambler, R.P. Biochem. J. 13719743-14 The evolutionary stability of cytochrome c-551 in Pseudomonas aeruginosa and Pseudomonas fluorescens biotype C. MUID74140216 A90272 protein 1-82 the sequence from strain 50 differs from that shown at least in having 18-Val, 29-Asp, and 47-Arg the sequences from strains 181 and 217 differ in having 1-Asp, 46-Ser, 63-Ala, and 65-Pro the sequence from strain 191 differs in having 1-Asp, 46-Asp, and 70-Gln the sequence from strain 204 differs in having 1-Asp and probably 65-Pro the sequence from strain 8376 is identical with that shown nirM cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 1-78 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,61 predicted 82 complete EDGAALFKSKPCAACHTIDSKMVGPALKEVAAKNAGVKDADKTLAGHIKNGTQGNWGPIP MPPNQVTDAEALTLAQWVLSLK
CCPS5S A00093 13-Jul-1981 13-Jul-1981 03-Nov-2000
cytochrome c551 [validated] Pseudomonas stutzeri (strain 221) Pseudomonas stutzeri Ambler, R.P. Wynn, M. Biochem. J. 1311973485-498 The amino acid sequences of cytochromes c-551 from three species of Pseudomonas. MUID73224976 A00093 protein 1-82 nirM cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 1-78 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,61 predicted 82 complete QDGEALFKSKPCAACHSIDAKLVGPAFKEVAAKYAGQDGAADLLAGHIKNGSQGVWGPIP MPPNPVTEEEAKILAEWILSQK
CCPS5B S13939 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c551 precursor Pseudomonas stutzeri (strain ZoBell) Pseudomonas stutzeri Juengst, A. Wakabayashi, S. Matsubara, H. Zumft, W.G. FEBS Lett. 2791991205-209 The nirSTBM region coding for cytochrome cd(1)-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins. MUID91160715 S13939 DNA 1-104 EMBLX56813 NIDg45838 PIDNCAA40153.1 PIDg45842 strain ZoBell, ATCC 14405 nirM cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain signal sequence 1-22 predicted product cytochrome c551 23-104 predicted domain cytochrome c6 homology 23-100 binding-site heme (Cys) (covalent) 34,37 predicted binding-site heme iron (His, Met) (axial ligands) 38,83 predicted 104 complete MKKILIPMLALGGALAMQPALAQDGEALFKSKPCAACHSVDTKMVGPALKEVAAKNAGVE GAADTLALHIKNGSQGVWGPIPMPPNPVTEEEAKILAEWVLSLK
CCPS5M A00094 13-Jul-1981 13-Jul-1981 03-Nov-2000
cytochrome c551 [validated] Pseudomonas mendocina Pseudomonas mendocina Ambler, R.P. Wynn, M. Biochem. J. 1311973485-498 The amino acid sequences of cytochromes c-551 from three species of Pseudomonas. MUID73224976 A00094 protein 1-82 strain CH110 nirM cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 1-78 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,61 predicted 82 complete ASGEELFKSKPCGACHSVQAKLVGPALKDVAAKNAGVDGAADVLAGHIKNGSTGVWGAMP MPPNPVTEEEAKTLAEWVLTLK
CCPS5D A00095 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c551 Pseudomonas sp. Pseudomonas sp. Ambler, R.P. Syst. Zool. 221973554-565 Bacterial cytochromes C and molecular evolution. A00095 protein 1-82 NCIB 9496, ATCC 13867 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 1-78 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,61 predicted 82 complete STGEELFKAKACVACHSVDKKLVGPAFHDVAAKYGAQGDGVAHITNSIKTGSKGNWGPIP MPPNAVSPEEAKTLAEWIVTLK
CCAV5 A00096 24-Apr-1984 24-Apr-1984 03-Mar-2000
cytochrome c551 Azotobacter vinelandii Azotobacter vinelandii Ambler, R.P. Syst. Zool. 221973554-565 Bacterial cytochromes C and molecular evolution. A00096 protein 1-82 strain O, NCIB 8789, ATCC 12837 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 1-78 binding-site heme (Cys) (covalent) 12,15 predicted binding-site heme iron (His, Met) (axial ligands) 16,61 predicted 82 complete ETGEELYKTKGCTVCHAIDSKLVGPSFKEVTAKYAGQAGIADTLAAKIKAGGSGNWGQIP MPPNPVSEAEAKTLAEWVLTHK
S32485 S32485 A32226 06-Jan-1995 27-Feb-1997 03-Mar-2000
cytochrome c552 precursor Hydrogenobacter thermophilus Hydrogenobacter thermophilus Sanbongi, Y. Yang, J.H. Igarashi, Y. Kodama, T. Eur. J. Biochem. 19819917-12 Cloning, nucleotide sequence and expression of the cytochrome c-552 gene from Hydrogenobacter thermophilus. MUID91249816 S32485 preliminary DNA 1-98 EMBLX57735 NIDg43674 PIDNCAA40902.1 PIDg43675 strain TK-6 Sanbongi, Y. Ishii, M. Igarashi, Y. Kodama, T. J. Bacteriol. 171198965-69 Amino acid sequence of cytochrome c-552 from a thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus. MUID89123087 A32226 protein 19-98 strain TK-6 primary electron acceptor for molecular hydrogen activated by hydrogenase hydrogen oxidation cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-18 predicted domain cytochrome c6 homology 17-94 product cytochrome c552 19-98 experimental binding-site heme (Cys) (covalent) 28,31 predicted binding-site heme iron (His, Met) (axial ligands) 32,77 predicted 98 complete MKKFLLVAVVGLAGITFANEQLAKQKGCMACHDLKAKKVGPAYADVAKKYAGRKDAVDYL AGKIKKGGSGVWGSVPMPPQNVTDAEAKQLAQWILSIK
S27723 S75611 S27723 17-Apr-1993 23-May-1997 16-Jun-2000
cytochrome cytM precursor protein sll1245 Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S75611 nucleic acid sequence not shown translation not shown DNA 1-128 EMBLD90912 GBAB001339 NIDg1653228 PIDNBAA18172.1 PIDg1653257 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 Malakhov, M.P. Wada, H. Los, D.A. Sakamoto, T. Murata, N. submitted to the EMBL Data Library April1992 Structure and expression of the cytM gene, encoding cytochrome from synechocystis PCC6803. S27723 DNA 24-128 EMBLD10716 NIDg217098 PIDNBAA01559.1 PIDg217102 cytM cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein product cytochrome cytM 55-128 predicted domain cytochrome c6 homology 57-128 atypical binding-site heme (Cys) (covalent) 68,71 predicted binding-site heme iron (His, Met) (axial ligands) 72,108 predicted 128 complete MAPVIEKSPTVATVNASPTGIWIMAGIVSLVILAVALFSFMNFDPYVSQVLALKGDADRG RAIFQANCAVCHGIQADGYIGPSLWGVSQRRSQSHIIHQVVSGQTPPMPQFEPNPQEMAD LLNYLKTL
CCDV5M A00113 19-Feb-1984 19-Feb-1984 03-Mar-2000
cytochrome c553 Desulfovibrio vulgaris (strain Miyazaki) Desulfovibrio vulgaris Nakano, K. Kikumoto, Y. Yagi, T. J. Biol. Chem. 258198312409-12412 Amino acid sequence of cytochrome c-553 from Desulfovibrio vulgaris Miyazaki. MUID84032425 A00113 protein 1-79 Cytochrome c553 has been reported as the natural electron acceptor for a formate dehydrogenase. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c6 homology 1-76 binding-site heme (Cys) (covalent) 10,13 predicted binding-site heme iron (His, Met) (axial ligands) 14,57 predicted 79 complete ADGAALYKSCVGCHGADGSKQAMGVGHAVKGQKADELFKKLKGYADGSYGGEKKAVMTNL VKRYSDEEMKAMADYMSKL
A44752 A44752 A05098 17-Feb-1994 17-Feb-1994 03-Mar-2000
cytochrome c553 precursor Desulfovibrio vulgaris (strain Hildenborough) Desulfovibrio vulgaris van Rooijen, G.J.H. Bruschi, M. Voordouw, G. J. Bacteriol. 17119893575-3578 Cloning and sequencing of the gene encoding cytochrome C-553 from Desulfovibrio vulgaris Hildenborough. MUID89255138 A44752 DNA 1-103 EMBLM27062 NIDg145082 PIDNAAA23356.1 PIDg145083 part of this sequence, including the amino end of the mature protein, was confirmed by protein sequencing Bruschi, M. Le Gall, J. Biochim. Biophys. Acta 271197248-60 c-type cytochromes of Desulfovibrio vulgaris the primary structure of cytochrome c-553. MUID72218157 A05098 protein 25-38,'S',40-42,'G',78-86,'G',87-100,44-63,65-77,'KAM',101-103 NCIB 8303 the residues line has been changed based on information from reference A44752 Cytochrome c553 has been reported as the natural electron acceptor for a formate dehydrogenase. cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-24 predicted product cytochrome c553 25-103 experimental domain cytochrome c6 homology 25-100 binding-site heme (Cys) (covalent) 34,37 predicted binding-site heme iron (His, Met) (axial ligands) 38,81 predicted 103 complete MKRVLLLSSLCAALSFGLAVSGVAADGAALYKSCIGCHGADGSKAAMGSAKPVKGQGAEE LYKKMKGYADGSYGGERKAMMTNAVKKYSDEELKALADYMSKL
F71843 F71843 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome c553 precursor Helicobacter pylori (strain J99) Helicobacter pylori strain J99 Alm, R.A. Ling, L.S.L. Moir, D.T. King, B.L. Brown, E.D. Doig, P.C. Smith, D.R. Noonan, B. Guild, B.C. deJonge, B.L. Carmel, G. Tummino, P.J. Caruso, A. Uria-Nickelsen, M. Mills, D.M. Ives, C. Gibson, R. Merberg, D. Mills, S.D. Jiang, Q. Taylor, D.E. Vovis, G.F. Trust, T.J. Nature 3971999176-180 Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori. MUID99120557 F71843 DNA 1-96 GBAE001542 GBAE001439 NIDg4155739 PIDNAAD06721.1 PIDg4155742 strain J99 jhp1148 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-19 predicted product cytochrome c553 20-96 predicted domain cytochrome c6 homology 20-92 binding-site heme (Cys) (covalent) 29,32 predicted binding-site heme iron (His) (axial ligand) 33 predicted 96 complete MKKVIVALGVLAFANVLMATDVKALVKGCAACHGVKFEKKALGKSKIVNMMSEKEIEEDL MAFKSGANKNPVMTAQAKKLSDEDIKALAKYIPTLK
C64673 C64673 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome c553 precursor Helicobacter pylori (strain 26695) Helicobacter pylori Tomb, J.F. White, O. Kerlavage, A.R. Clayton, R.A. Sutton, G.G. Fleischmann, R.D. Ketchum, K.A. Klenk, H.P. Gill, S. Dougherty, B.A. Nelson, K. Quackenbush, J. Zhou, L. Kirkness, E.F. Peterson, S. Loftus, B. Richardson, D. Dodson, R. Khalak, H.G. Glodek, A. McKenney, K. Fitzegerald, L.M. Lee, N. Adams, M.D. Hickey, E.K. Berg, D.E. Gocayne, J.D. Utterback, T.R. Peterson, J.D. Kelley, J.M. Cotton, M.D. Weidman, J.M. Fujii, C. Bowman, C. Watthey, L. Wallin, E. Hayes, W.S. Borodovsky, M. Karpk, P.D. Smith, H.O. Fraser, C.M. Venter, J.C. Nature 3881997539-547 The complete genome sequence of the gastric pathogen Helicobacter pylori. MUID97394467 C64673 nucleic acid sequence not shown translation not shown DNA 1-96 GBAE000628 GBAE000511 NIDg2314386 PIDNAAD08272.1 PIDg2314390 TIGRHP1227 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-19 predicted product cytochrome c553 20-96 predicted domain cytochrome c6 homology 20-92 binding-site heme (Cys) (covalent) 29,32 predicted binding-site heme iron (His) (axial ligand) 33 predicted 96 complete MKKVIMALGVLAFANALMATDVKALAKSCAACHGVKFEKKALGKSKIVNMMSEAEIEKDL MDFKSGANKNPIMSAQAKKLSDEDIKALAKYIPTLK
A36437 A36437 10-Sep-1999 10-Sep-1999 03-Mar-2000
flavocytochrome c, heme-containing chain Chlorobium limicola f.sp. thiosulfatophilum (strain Tassajara) Chlorobium limicola f.sp. thiosulfatophilum Van Beeumen, J. Van Bun, S. Meyer, T.E. Bartsch, R.G. Cusanovich, M.A. J. Biol. Chem. 26519909793-9799 Complete amino acid sequence of the cytochrome subunit and amino-terminal sequence of the flavin subunit of flavocytochrome c (sulfide dehydrogenase) from Chlorobium thiosulfatophilum. MUID90277669 A36437 preliminary protein 1-87 cytochrome c6 cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c6 homology 9-79 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His) (axial ligand) 22 predicted 87 complete APEQSKSIPRGEILSLSCAGCHGTDGKSESIIPTIYGRSAEYIESALLDFKSGARPSTVM GRHAKGYSDEEIHQIAEYFGSLSTMNN
S31922 S65941 S65915 S31922 06-Jan-1995 02-Jul-1996 03-Mar-2000
cytochrome c552, membrane-bound Paracoccus denitrificans Paracoccus denitrificans Turba, A. Jetzek, M. Ludwig, B. Eur. J. Biochem. 2311995259-265 Purification of Paracoccus denitrificans cytochrome c(552) and sequence analysis of the gene. MUID95354697 S65941 DNA 1-176 EMBLX70367 NIDg49208 PIDNCAA49830.1 PIDg49209 strain PD1235 S65915 protein 66-76;132-139;164-176 cycM electron transfer from the ubiquinol--cytochrome-c reductase (bc1) complex to the cytochrome-c oxidase (aa3) complex (probable) oxidative phosphorylation respiratory chain membrane-bound cytochrome cycM cytochrome c homology chromoprotein electron transfer heme inner membrane iron metalloprotein transmembrane protein domain intracellular 1-9 predicted domain transmembrane 10-26 predicted domain periplasmic 27-176 predicted domain cytochrome c homology 81-172 binding-site heme (Cys) (covalent) 90,93 predicted binding-site heme iron (His, Met) (axial ligands) 94,154 predicted 176 complete MFDTMTVTKAAGALIGSLLFLLLMSWAASGIFHVGTSGHGAEGEEHAQAYTYPVESAGGA EGEAVDEGPDFATVLASADPAAGEKVFGKCKACHKLDGNDGVGPHLNGVVGRTVAGVDGF NYSDPMKAHGGDWTPEALQEFLTNPKAVVKGTKMAFAGLPKIEDRANLIAYLEGQQ
S31938 S31938 S35337 06-Jan-1995 02-Jul-1996 03-Mar-2000
membrane-bound cytochrome cycY Rhodobacter capsulatus Rhodobacter capsulatus Daldal, F. submitted to the EMBL Data Library February1993 S31938 DNA 1-199 EMBLZ21797 NIDg49366 PIDNCAA79860.1 PIDg49367 Jenney Jr., F.E. Daldal, F. EMBO J. 1219931283-1292 A novel membrane-associated c-type cytochrome, cyt c(y), can mediate the photosynthetic growth of Rhodobacter capsulatus and Rhodobacter sphaeroides. MUID93223669 S35337 DNA 'MRQPHMPTAGGA',1-199 EMBLZ21797 strain MT-1131 it is uncertain which Met is the initiator cycY electron transfer from the ubiquinol--cytochrome-c reductase (bc1) complex to the photosynthetic reaction center photosynthesis in this organism, both this protein and cytochrome c2 can mediate electron transfer during photosynthesis membrane-bound cytochrome cycM cytochrome c homology chromoprotein electron transfer heme inner membrane iron metalloprotein photosynthesis transmembrane protein domain intracellular 1-9 predicted domain transmembrane 10-26 predicted domain periplasmic 27-199 predicted domain cytochrome c homology 102-194 binding-site heme (Cys) (covalent) 112,115 predicted binding-site heme iron (His, Met) (axial ligands) 116,176 predicted 199 complete MLVKTHITKIGVTLFAVALFYGFIYMLSNSLFATRPATAVAVGADGKALLPSVDEAAMPA KAPAAAAPAAETAEAAAPAEPAAPPPPAYVEVDPATITGDAKAGEEKFNKTCKACHKIDG KNAVGPHLNGVIGRATATVEGFKYSTAMKNHVGNWTPERLDIYLVSPKAEVPGTKMSFVG LPEAADRANVIAYLNTLPR
A41331 A41331 28-May-1992 02-Jul-1996 03-Mar-2000
membrane-bound cytochrome cycM Bradyrhizobium japonicum Bradyrhizobium japonicum Bott, M. Ritz, D. Hennecke, H. J. Bacteriol. 17319916766-6772 The Bradyrhizobium japonicum cycM gene encodes a membrane-anchored homolog of mitochondrial cytochrome c. MUID92041558 A41331 DNA 1-184 GBM77189 NIDg152080 PIDNAAA26198.1 PIDg152081 strain 110spc4, a spectinomycin-resistant derivative of strain 3I1b110 cycM electron transfer from the ubiquinol--cytochrome-c reductase (bc1) complex to the cytochrome-c oxidase (aa3) complex (probable) oxidative phosphorylation respiratory chain membrane-bound cytochrome cycM cytochrome c homology chromoprotein electron transfer heme inner membrane iron metalloprotein transmembrane protein domain intracellular 1-8 predicted domain transmembrane 9-25 predicted domain periplasmic 26-184 predicted domain cytochrome c homology 75-169 binding-site heme (Cys) (covalent) 84,87 predicted binding-site heme iron (His, Met) (axial ligands) 88,151 predicted 184 complete MDSFELNKILGAVLGTCLILLVTSFTANALFSPKMPEKPGFEIAVKEDAGHGKEGGAAAA ASEPIEKLLQTASVEKGAAAAKKCGACHTFEKGGPNRVGPNLYGVVGEARGEGRNGFNFS AAMKGKGGTWTFDDLNKFIANPKGFIPGTAMGFAGIPKDSERADVIAYLNSLSEHPKPLP TASK
T46966 T46966 03-Nov-2000 03-Nov-2000 03-Nov-2000
diheme cytochrome soxD precursor [similarity] cytochrome diheme c-type Paracoccus denitrificans Paracoccus denitrificans Wodara, C. Bardischewsky, F. Friedrich, C.G. J. Bacteriol. 17919975014-5023 Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: Essential role of of sulfite dehydrogenase in lithotrophic sulfur oxidation. MUID97405897 T46966 translated from GB/EMBL/DDBJ DNA 1-384 EMBLX79242 NIDg2253074 PIDNCAA55825.1 PIDg2222779 strain GB17 soxD may be a required electron acceptor for soxC sulfite dehydrogenase (by analogy with P. versutus) thiosulfate oxidation Paracoccus denitrificans diheme cytochrome soxD cytochrome c homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-19 predicted product c-type cytochrome soxD 20-384 predicted domain cytochrome c homology 283-379 binding-site heme (Cys) (covalent) 70,73 predicted binding-site heme iron (His, Met) (axial ligands) 74,121 predicted binding-site heme (Cys) (covalent) 292,295 predicted binding-site heme iron (His, Met) (axial ligands) 296,361 predicted 384 complete MSKSLELFLGSVLAASVLAGPAMADKLGLGREALPEEISAWDTAVLPDGQGLRPGSGDVA TGDALFADNCASCHGDFAEGLDSWPVLAGGDGSLTDPRPVKTIGSYWPYLSTVYDYVHRS MPFGSAQTLSVDDTYAITAFLLYSNGLVEDDFVLTHENFTQVVLPNAEGFYPDDRDQTEY PLFSKEPCMTDCAVGVEITKRAVDLNVTPEDPDGRPAGSMPDLGAAAAPAEPAEPVEKKA EAAPAEAPAPAAAPEVVVKAAAMAPEAPAPAGAATAADPTLLAEGEKVFKKCAACHKVGD DAKNGTGPLLNGIVGRAAGDIEGFKYSKPLLAMASEGLVWDDASLHAFLENPKGFMKGTK MSFAGLKKEDERAAVIAYLATFAK
CCPS4A A00098 17-May-1985 17-May-1985 03-Mar-2000
cytochrome c4 Pseudomonas aeruginosa Pseudomonas aeruginosa Ambler, R. unpublished results, cited by Dickerson, R.E., in The Evolution of Protein Structure and Function, Sigman, D.S., and Brazier, M.A.B., eds., pp.173-202, Academic Press, New York and London 1980 A00098 protein 1-181 Cytochrome c4 is a diheme, high potential cytochrome that appears to be the result of gene duplication and fusion of a smaller monoheme protein similar to Pseudomonas cytochrome c551. Although the exact function of c4 is unknown, it is produced in significant quantities when P. aeruginosa is grown anaerobically. cytochrome c4 cytochrome c6 homology chromoprotein duplication electron transfer heme iron metalloprotein oxidative phosphorylation domain cytochrome c6 homology 5-77 domain cytochrome c6 homology 99-177 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,58 predicted binding-site heme (Cys) (covalent) 110,113 predicted binding-site heme iron (His, Met) (axial ligands) 114,157 predicted 181 complete AGDAAAGQAKAAVCGACHGABBBGSAPPFPKLAGQGERYLLKQMHDIKDGKRTVLEEMTG LLTBLSBZDIAALADYASQKMSVGMALBBPVAGGEALFRGGKIAEGMPACTGCHGSSPVG IATAGFPHLGGQHATYVAKQLTDFREGTRNDDGTKIMQSIAAIKLSNKDIAAISSYIQGL H
I39740 I39740 S56043 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome c4 precursor Azotobacter vinelandii Azotobacter vinelandii Ng, T.C. Laheri, A.N. Maier, R.J. Biochim. Biophys. Acta 12301995119-129 Cloning, sequencing, and mutagenesis of the cytochrome c4 gene from Azotobacter vinelandii: characterization of the mutant strain and a proposed new branch in the respiratory chain. MUID95345104 I39740 preliminary translated from GB/EMBL/DDBJ DNA 1-210 GBL37290 NIDg600179 PIDNAAA87314.1 PIDg600180 cycA cytochrome c4 cytochrome c6 homology chromoprotein duplication electron transfer heme iron metalloprotein oxidative phosphorylation domain signal sequence 1-21 predicted product cytochrome c4 22-210 predicted domain cytochrome c6 homology 25-105 domain cytochrome c6 homology 128-206 binding-site heme (Cys) (covalent) 34,37 predicted binding-site heme iron (His) (axial ligand) 38 predicted binding-site heme (Cys) (covalent) 139,142 predicted binding-site heme iron (His) (axial ligand) 143 predicted 210 complete MNKALVTLLLTLGITGLAHAAGDAAAGQGKAAVCGACHGPDGNSAAPNFPKLAGQGERYL LKQMQDIKAGTKPGAPEGSGRKVLEMTGMLDNFSDQDLADLAAYFTSQKPTVGAADPQLV EAGETLYRGGKLADGMPACTGCHSPNGEGNTPAAYPRLSGQHAQYVAKQLTDFREGARTN DGDNMIMRSIAAKLSNKDIAAISSYIQGLH
C47169 C47169 A39859 10-Sep-1999 10-Sep-1999 03-Mar-2000
flavocytochrome c, heme-containing chain Chromatium vinosum Chromatium vinosum Dolata, M.M. Van Beeumen, J.J. Ambler, R.P. Meyer, T.E. Cusanovich, M.A. J. Biol. Chem. 268199314426-14431 Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin. MUID93300842 C47169 preliminary DNA 1-199 GBL13419 NIDg290007 PIDNAAA23316.1 PIDg290010 Van Beeumen, J.J. Demol, H. Samyn, B. Bartsch, R.G. Meyer, T.E. Dolata, M.M. Cusanovich, M.A. J. Biol. Chem. 266199112921-12931 Covalent structure of the diheme cytochrome subunit and amino-terminal sequence of the flavoprotein subunit of flavocytochrome c from Chromatium vinosum. MUID91302306 A39859 preliminary protein 26-199 cytochrome c4 cytochrome c6 homology chromoprotein duplication electron transfer heme iron metalloprotein periplasmic space binding-site heme (Cys) (covalent) 36,39 predicted binding-site heme iron (His) (axial ligand) 40 predicted binding-site heme (Cys) (covalent) 126,129 predicted binding-site heme iron (His) (axial ligand) 130 predicted 199 complete MTQSTPRLMLAASVLALGLASNAGAEPTAEMLTNNCAGCHGTHGNSVGPASPSIAQMDPM VFVEVMEGFKSGEIASTIMGRIAKGYSTADFEKMAGYFKQQTYQPAKQSFDTALADTGAK LHDKYCEKCHVEGGKPLADEEDYHILAGQWTPYLQYAMSDFREERRPMEKKMASKLRELL KAEGDAGLDALFAFYASQQ
F75267 F75267 17-Mar-2000 17-Mar-2000 17-Mar-2000
probable cytochrome c4 Deinococcus radiodurans (strain R1) Deinococcus radiodurans White, O. Eisen, J.A. Heidelberg, J.F. Hickey, E.K. Peterson, J.D. Dodson, R.J. Haft, D.H. Gwinn, M.L. Nelson, W.C. Richardson, D.L. Moffat, K.S. Qin, H. Jiang, L. Pamphile, W. Crosby, M. Shen, M. Vamathevan, J.J. Lam, P. McDonald, L. Utterback, T. Zalewski, C. Makarova, K.S. Aravind, L. Daly, M.J. Minton, K.W. Fleischmann, R.D. Ketchum, K.A. Nelson, K.E. Salzberg, S. Smith, H.O. Venter, J.C. Fraser, C.M. Science 28619991571-1577 Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1. MUID20036896 F75267 preliminary DNA 1-229 GBAE002078 GBAE000513 NIDg6460306 PIDNAAF12028.1 PIDg6460307 TIGRDR2487 GSPDBGN00077 strain R1 DR2487 1 cytochrome c4 cytochrome c6 homology chromoprotein duplication electron transfer heme iron metalloprotein domain cytochrome c6 homology 51-122 domain cytochrome c6 homology 146-225 binding-site heme (Cys) (covalent) 60,63 predicted binding-site heme iron (His, Met) (axial ligands) 64,103 predicted binding-site heme (Cys) (covalent) 157,160 predicted binding-site heme iron (His, Met) (axial ligands) 161,206 predicted 229 complete MSRFSSRLLWLAVPALLGTSVFAATTPGTTPQGTAAPKNPLALQFKTPSAARGAAIAGTC AGCHGKTGVSVQADIPSLAGQIPNYTQFQLAAFRAKLRPSNVMQQVASKLSDQDIADLSA YYAAQAVGPAWKAEPAARARGQKLFTAGDPARNVIACAVCHGSNGRGLNANHIASVTNLP PEYALEVLKEFHEAPTFGGLVPPETMRIAVKPLTDKDLKDVATYISSMK
D55582 D55582 S42232 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome-c oxidase (EC 1.9.3.1) fixP chain cb-type cytochrome-c oxidase 32K chain cytochrome b410 fixP protein Azorhizobium caulinodans Azorhizobium caulinodans Mandon, K. Kaminski, P.A. Elmerich, C. J. Bacteriol. 17619942560-2568 Functional analysis of the fixNOQP region of Azorhizobium caulinodans. MUID94222833 D55582 preliminary nucleic acid sequence not shown DNA 1-292 GBX74410 Mandon, K. Kaminski, P.A. Mougel, C. Desnoues, N. Dreyfus, B. Elmerich, C. FEMS Microbiol. Lett. 1141993185-190 Role of the fixGHI region of Azorhizobium caulinodans in free-living and symbiotic nitrogen fixation. MUID94109675 S42232 preliminary nucleic acid sequence not shown translation not shown DNA 1-53,'W',54-292 EMBLX74410 NIDg456310 PIDNCAA52432.1 PIDg580702 the nucleotide sequence was submitted to the EMBL Data Library, July 1993 GTG Rhizobium cytochrome-c oxidase fixP chain cytochrome c6 homology chromoprotein duplication electron transfer heme iron membrane-associated complex metalloprotein oxidoreductase respiratory chain domain cytochrome c6 homology 116-196 domain cytochrome c6 homology 211-285 binding-site heme (Cys) (covalent) 126,129 predicted binding-site heme iron (His, Met) (axial ligands) 130,177 predicted binding-site heme (Cys) (covalent) 221,224 predicted binding-site heme iron (His, Met) (axial ligands) 225,266 predicted 292 complete MSTSHESHHAPVDGAGGPSTTGHEWDGIQELNNPLPRWWLWTFYATIIWAFGYVAYPAWP LVSNYTSGVLGWNSRSAVVEQISDLQKLRAASSAKLANVPLEDIEKNPELLSLARAEGKV AFADNCAPCHGAGGGGAKGFPNLNDDDWLWGGTLAQIQQTITHGIRSGDDEGHQGNMLAF GSILSKADISNVADYVRSLSGAAPGDTPAAKKGAEIFAANCATCHGENGKGNQELGSKNL TDGIWLYGGDKATIVQTITNGRGGVMPAWGPRLSPTTIKALTVYVHTLGGGQ
D47468 D47468 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome-c oxidase (EC 1.9.3.1) fixP chain cb-type cytochrome-c oxidase 32K chain cytochrome b410 fixP protein Bradyrhizobium japonicum Bradyrhizobium japonicum Preisig, O. Anthamatten, D. Hennecke, H. Proc. Natl. Acad. Sci. U.S.A. 9019933309-3313 Genes for a microaerobically induced oxidase complex in Bradyrhizobium japonicum are essential for a nitrogen-fixing endosymbiosis. MUID93234486 D47468 preliminary not compared with conceptual translation DNA 1-290 GBL07487 NIDg152196 PIDNAAA26206.1 PIDg152202 110spc4 sequence extracted from NCBI backbone (NCBIP:129656) Rhizobium cytochrome-c oxidase fixP chain cytochrome c6 homology chromoprotein duplication electron transfer heme iron membrane-associated complex metalloprotein oxidoreductase respiratory chain domain cytochrome c6 homology 112-194 binding-site heme (Cys) (covalent) 122,125 predicted binding-site heme iron (His, Met) (axial ligands) 126,173 predicted binding-site heme (Cys) (covalent) 219,222 predicted binding-site heme iron (His, Met) (axial ligands) 223,264 predicted 290 complete MTDHSEFDSVSGKTTTGHEWDGIKELNTPLPRWWVICFYLTIVWAIGYWIVYPAWPLISS NTTGLFGYSSRADVAVELANLEKIRGDKMAALGAASLADVEKDPALLALARAKGKTVFGD NCAPCHGSGGAGAKGFPNLNDDDWLWGGTLDQIMQTIQFGARSGHAKTHEGQMLAFGKDG VLKGDEIVTVANYVRSLSGLPTRKGYDAAKGEKIFVENCVACHGDGGKGNQEMGAPNLTD KIWLYGSDEAALIETISQGRAGVMPAWEGRLDPSTIKAMAVYVHSLGGGK
S39991 S39991 S32844 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome-c oxidase (EC 1.9.3.1) fixP chain cb-type cytochrome-c oxidase 32K chain cytochrome b410 fixP protein Rhizobium meliloti Rhizobium meliloti Kahn, D.D. submitted to the EMBL Data Library March1993 S39991 DNA 1-289 EMBLZ21854 NIDg49403 PIDNCAA79904.1 PIDg49411 Rhizobium cytochrome-c oxidase fixP chain cytochrome c6 homology chromoprotein duplication electron transfer heme iron membrane-associated complex metalloprotein oxidoreductase respiratory chain domain cytochrome c6 homology 113-194 binding-site heme (Cys) (covalent) 123,126 predicted binding-site heme iron (His, Met) (axial ligands) 127,175 predicted binding-site heme (Cys) (covalent) 218,221 predicted binding-site heme iron (His, Met) (axial ligands) 222,263 predicted 289 complete MADKHKHVDEVSGVETTGHEWDGIRELNNPMPRWWVYSFYATIIWAIGYAIAYPSWPMLT EATKGMLGYSSRAEVSVELAAAKAAQAGNLEQIASSSVEEIIANPQLQQFAVSAGASAFK VNCAQCHGSGAAGGQGFPNLNDDDWLWGGKPQEIYQTIAHGVRHAPDGETRVSEMPPFGD MLTPELMQQTAAYVVSLTQAPSQPHLVQQGKQVFADNCASCHGADAKGNREMGAPNLADA IWLKGEGEQAVITQMKTPKHGVMPAWLPRLGDDTVKQLAVFVHSLGGGE
S49348 S65861 H54235 G54235 I54235 A59014 S49348 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome-c oxidase (EC 1.9.3.1) fixP chain cb-type cytochrome-c oxidase 32K chain ccoP protein cytochrome b410 fixP protein homolog Rhodobacter capsulatus Rhodobacter capsulatus Thoeny-Meyer, L. Beck, C. Preisig, O. Hennecke, H. Mol. Microbiol. 141994705-716 The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus. MUID95198544 S65861 preliminary nucleic acid sequence not shown DNA 1-297 EMBLX80134 NIDg556812 PIDNCAA56436.1 PIDg556816 Gray, K.A. Grooms, M. Myllykallio, H. Moomaw, C. Slaughter, C. Daldal, F. Biochemistry 3319943120-3127 Rhodobacter capsulatus contains a novel cb-type cytochrome c oxidase without a CuA center. MUID94176508 H54235 protein 86-88,'D',90-107 pMTo-404/MT-RBC1 cells sequence extracted from NCBI backbone (NCBIP:144522) G54235 protein 'AT',263-266,'X',268,'X',270-274,'X',276 pMTo-404/MT-RBC1 cells sequence extracted from NCBI backbone (NCBIP:144520) I54235 protein 285-296,'S' pMTo-404/MT-RBC1 cells sequence extracted from NCBI backbone (NCBIP:144524) A59014 protein 91,'M',93-101;251,'I',253,'T',255-256,'SL',259-260 pMTo-404/MT-RBC1 cells ccoP this cytochrome-c oxidase complex catalyzes the oxidation of four molecules of reduced cytochrome c2 using one oxygen molecule and four protons producing two molecules of water respiratory chain Rhizobium cytochrome-c oxidase fixP chain cytochrome c6 homology chromoprotein duplication electron transfer heme iron membrane-associated complex metalloprotein oxidoreductase respiratory chain domain cytochrome c6 homology 209-290 binding-site heme (Cys) (covalent) 121,124 predicted binding-site heme iron (His, Met) (axial ligands) 125,174 predicted binding-site heme (Cys) (covalent) 219,222 predicted binding-site heme iron (His, Met) (axial ligands) 223,264 predicted 297 complete MSKKPTTKKEVQTTGHQWDGIEELNTPLPRWWLWTFYATIIWGVAYSIAMPAWPIFSDKA TPGLLGSSTRADVEKDIAKFAEMNKAVEEKLVATDLTAIAADPELVTYTRNAGAAVFRTW CAQCHGAGAGGNTGFPSLLDGDWLHGGAIETIYTNVKHGIRDPLDPDTLLVANMPAHLTD ELLEPAQIDEVVQYVLQISGQPADEVKATAGQQIFAENCASCHGEDAKGLVEMGAPNLTD GIWLYGGDVATLTSTIQYGRGGVMPSWSWAADGAKPRLSEAQIRAVASYVHSLGGGQ
C70784 C70784 20-Apr-2000 20-Apr-2000 16-Jun-2000
probable diheme cytochrome qcrC Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 C70784 nucleic acid sequence not shown translation not shown DNA 1-280 GBZ70283 GBAL123456 NIDg3261561 PIDNCAA94263.1 PIDg1237047 strain H37Rv qcrC Streptomyces coelicolor probable diheme cytochrome qcrC cytochrome c6 homology chromoprotein heme iron metalloprotein domain cytochrome c6 homology 63-136 atypical domain cytochrome c6 homology 164-235 binding-site heme (Cys) (covalent) 73,76 predicted binding-site heme iron (His) (axial ligand) 77 predicted binding-site heme (Cys) (covalent) 174,177 predicted binding-site heme iron (His) (axial ligand) 178 predicted 280 complete MTKLGFTRSGGSKSGRTRRRLRRRLSGGVLLLIALTIAGGLAAVLTPTPQVAVADESSSA LLRTGKQLFDTSCVSCHGANLQGVPDHGPSLIGVGEAAVYFQVSTGRMPAMRGEAQAPRK DPIFDEAQIDAIGAYVQANGGGPTVVRNPDGSIATQSLRGNDLGRGGDLFRLNCASCHNF TGKGGALSSGKYAPDLAPANEQQILTAMLTGPQNMPKFSNRQLSFEAKKDIIAYVKVATE ARQPGGYLLGGFGPAPEGMAMWIIGMVAAIGLALWIGARS
T35532 T35532 20-Apr-2000 20-Apr-2000 19-May-2000
probable diheme cytochrome qcrC precursor Streptomyces coelicolor Streptomyces coelicolor Seeger, K. Harris, D. Bentley, S.D. Parkhill, J. Barrell, B.G. Rajandream, M.A. submitted to the EMBL Data Library March1999 T35532 translated from GB/EMBL/DDBJ DNA 1-269 EMBLAL049497 PIDNCAB39877.1 GSPDBGN00070 SCOEDBSC6G10.23c strain A3(2) qcrC SC6G10.23c Streptomyces coelicolor probable diheme cytochrome qcrC cytochrome c6 homology chromoprotein heme iron metalloprotein domain signal sequence 1-27 predicted domain cytochrome c6 homology 50-122 atypical domain cytochrome c6 homology 145-216 binding-site heme (Cys) (covalent) 60,63 predicted binding-site heme iron (His) (axial ligand) 64 predicted binding-site heme (Cys) (covalent) 155,158 predicted binding-site heme iron (His) (axial ligand) 159 predicted 269 complete MKKLSARRRHPLAALVVLLLALACTGGLYAAFAPASKAQADESAQSLAIDEGKKLYAVGC ASCHGTGGQGTSDGPSLVGVGAAAVDFQVGTGRMPAQQPGAQVPKKKVIYSQAEIDQLAA YIASLGAGPAIPSEEKYGPEGADIAKGGELFRTNCAQCHNFTGKGGALTHGKYAPSLEGV DPKHIYEAMQTGPQNMPSFPDTTLSEQNKKDIIAYLDAVNGDDTESPGGLSLGGLGPVSE GLFAWVFGLGALIAVAVWVAARTAKAKKS
T46967 T46967 03-Nov-2000 03-Nov-2000 03-Nov-2000
diheme cytochrome soxE precursor [similarity] cytochrome monoheme c-type Paracoccus denitrificans Paracoccus denitrificans Wodara, C. Bardischewsky, F. Friedrich, C.G. J. Bacteriol. 17919975014-5023 Cloning and characterization of sulfite dehydrogenase, two c-type cytochromes, and a flavoprotein of Paracoccus denitrificans GB17: Essential role of of sulfite dehydrogenase in lithotrophic sulfur oxidation. MUID97405897 T46967 translated from GB/EMBL/DDBJ DNA 1-236 EMBLX79242 NIDg2253074 PIDNCAA55828.1 PIDg2253075 strain GB17 soxE Paracoccus denitrificans diheme cytochrome soxE cytochrome c homology cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-18 predicted product c-type cytochrome soxE 19-236 predicted domain cytochrome c homology 30-127 domain cytochrome c6 homology 163-232 binding-site heme (Cys) (covalent) 40,43 predicted binding-site heme iron (His, Met) (axial ligands) 44,109 predicted binding-site heme (Cys) (covalent) 172,175 predicted binding-site heme iron (His, Met) (axial ligands) 176,213 predicted 236 complete MRQRKLLSALFTVAAAGATPAAAEEIGDTVHGAVLFRKECAICHRIGQDARNAVGPRLNG VFGRRAAALADFNYSRAMKRKGNDGLTWTLETLDAYIENPKALVTGTRMSYRGLADPQAR ADLMAYMRDHSDRPQDIPEAEPTARRNAPVLSEEVLALRGDPEFGAYLSAECTTCHQRDG SDQGIPSIAGWPQEDFVVAMHAYKQKLRPHPVMQMMAGRLSEEEIAALAAFFATLE
B41377 B41377 28-May-1992 02-Jul-1996 15-Sep-2000
cytochrome c-L precursor [validated] cytochrome c551i cytochrome c552 moxG protein Paracoccus denitrificans Paracoccus denitrificans Van Spanning, R.J.M. Wansell, C.W. De Boer, T. Hazelaar, M.J. Anazawa, H. Harms, N. Oltmann, L.F. Stouthamer, A.H. J. Bacteriol. 17319916948-6961 Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth. MUID92041581 B41377 DNA 1-177 GBM57684 NIDg150589 PIDNAAA25583.1 PIDg150591 Chen, L. Durley, R.C.E. Matthews, F.S. Davidson, V.L. Science 264199486-90 Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c-551i. MUID94188715 annotation X-ray crystallography, 2.4 angstroms, residues 23-177 Chen, L. Mathews, F.S. submitted to the Brookhaven Protein Data Bank October1993 PDB2MTA annotation X-ray crystallography, 2.4 angstroms, residues 23-169 moxG associates in a heterotetramer with methylamine dehydrogenase large and small chains and amicyanin to form a soluble electron transfer chain; the complex forms a dimer in crystals electron acceptor for methanol dehydrogenase; can also accept an electron transferred to amicyanin from methylamine dehydrogenase; electron donor to cytochrome-c oxidase methanol oxidation methylamine oxidation cytochrome c-L cytochrome c6 homology chromoprotein electron transfer heme heterotetramer iron metalloprotein periplasmic space domain signal sequence 1-22 predicted product cytochrome c-L 23-177 experimental domain cytochrome c6 homology 69-142 binding-site heme (Cys) (covalent) 79,82 experimental binding-site heme iron (His, Met) (axial ligands) 83,123 experimental 177 complete MTKPRILAAFAMTLIIPVAAMAAPQFFNIIDGSPLNFDDAMEEGRDTEAVKHFLETGENV YNEDPEILPEAEELYAGMCSGCHGHYAEGKIGPGLNDAYWTYPGNETDVGLFSTLYGGAT GQMGPMWGSLTLDEMLRTMAWVRHLYTGDPKDASWLTDEQKAGFTPFQPKSSGEDQS
S01249 S01249 S02658 30-Sep-1989 02-Jul-1996 21-Jul-2000
cytochrome c-L precursor Methylobacterium sp. Methylobacterium sp. Nunn, D.N. Anthony, C. Nucleic Acids Res. 1619887722 The nucleotide sequence and deduced amino acid sequence of the genes for cytochrome cL and a hypothetical second subunit of the methanol dehydrogenase of Methylobacterium AM1. MUID88319960 S01249 DNA 1-197 EMBLX07856 NIDg44527 PIDNCAA30704.1 PIDg44528 Nunn, D.N. Anthony, C. Biochem. J. 2561988673-676 The nucleotide sequence and deduced amino acid sequence of the cytochrome c(L) gene of Methylobacterium extorquens AM1, a novel class of c-type cytochrome. MUID89134152 S02658 DNA 1-197 source designated as Methylobacterium extorquens AM1 part of this sequence was confirmed by protein sequencing moxG electron acceptor for methanol dehydrogenase; electron donor to cytochrome-c oxidase methanol oxidation cytochrome c-L cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein periplasmic space domain signal sequence 1-25 predicted product cytochrome c-L 26-197 predicted domain cytochrome c6 homology 80-153 binding-site heme (Cys) (covalent) 90,93 predicted binding-site heme iron (His, Met) (axial ligands) 94,134 predicted 197 complete MMNRVKIGTALLGLTLAGIALPALAQPQSGPQTGVVFRNTVTGEALDVSQGKEGGRDTPA VKKFLETGENLYIDDKSCLRNGESLFATSCSGCHGHLAEGKLGPGLNDNYWTYPSNTTDV GLFATIFGGANGMMGPHNENLTPDEMLQTIAWIRHLYTGPKQDAVWLNDEQKKAYTPYKQ GEVIPKDAKGQCKPLDE
A45079 A45079 10-Jun-1993 02-Jul-1996 03-Mar-2000
photosynthetic reaction center cytochrome c551 photosynthetic reaction center complex 18K protein Chlorobium vibrioforme Chlorobium vibrioforme Okkels, J.S. Kjaer, B. Hansson, O. Svendsen, I. Moller, B.L. Scheller, H.V. J. Biol. Chem. 267199221139-21145 A membrane-bound monoheme cytochrome c551 of a novel type is the immediate electron donor to P840 of the Chlorobium vibrioforme photosynthetic reaction center complex. MUID93016035 A45079 DNA protein 1-206 GBM95751 NIDg144472 PIDNAAA23110.1 PIDg144473 f. thiosulfatophilum 8327 sequence extracted from NCBI backbone (NCBIN:116201, NCBIP:116202) part of this sequence, including the amino end of the mature protein, confirmed by protein sequencing authors predicted the Met axial ligand based on its predicted location on the periplasmic side of the membrane cycA tightly bound to the photosynthetic reaction center complex electron donor to photooxidized P840 of the photosynthetic reaction center complex Chlorobium photosynthetic reaction center cytochrome c551 chromoprotein electron transfer heme iron metalloprotein photosynthesis transmembrane protein product photosynthetic reaction center cytochrome c551 1-206 experimental domain intracellular 1-9 predicted domain transmembrane 10-32 predicted domain periplasmic 33-48 predicted domain transmembrane 49-67 predicted domain transmembrane 78-95 predicted domain periplasmic 96-206 predicted binding-site heme (Cys) (covalent) 152,155 predicted binding-site heme iron (His, Met) (axial ligands) 156,182 predicted 206 complete MDNKSNGKLIALAIGGAVLMGTLFFLVSFLTGYSPAPNHSAILTPLRSFMGWFLLIFCAS LIIMGLGKMSGAISDKWFLSFPLSIFVIVMVMFFSLRFYWEKGRTTTVDGKYIRSVEQLN DFLNKPAATSDLPPVPADFDFAAAEKLTDAKCNKCHTLGSVADLFRTKYKKTGQVKLIVK RMQGFPGANISDDEVIEIGTWLQEKF
S00680 A31481 S00680 A29720 30-Jun-1989 15-Oct-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor bc1 complex cytochrome c1 complex III cytochrome c1 cytochrome c1 heme protein human man Homo sapiens Suzuki, H. Hosokawa, Y. Nishikimi, M. Ozawa, T. J. Biol. Chem. 26419891368-1374 Structural organization of the human mitochondrial cytochrome c-1 gene. MUID89109139 A31481 not compared with conceptual translation DNA 1-325 GBJ04444 Nishikimi, M. Ohta, S. Suzuki, H. Tanaka, T. Kikkawa, F. Tanaka, M. Kagawa, Y. Ozawa, T. Nucleic Acids Res. 1619883577 Nucleotide sequence of a cDNA encoding the precursor to human cytochrome c1. MUID88233946 S00680 mRNA 1-325 EMBLX06994 NIDg30302 PIDNCAA30052.1 PIDg30303 Nishikimi, M. Suzuki, H. Ohta, S. Sakurai, T. Shimomura, Y. Tanaka, M. Kagawa, Y. Ozawa, T. Biochem. Biophys. Res. Commun. 145198734-39 Isolation of a cDNA clone for human cytochrome c1 from a lambda-gt11 expression library. MUID87241521 A29720 mRNA 99-325 GBM16597 NIDg181237 PIDNAAA35730.1 PIDg181238 GDBCYC1 GDB119827 OMIM123980 8q24.3-8q24.3 43/3; 109/2; 151/3; 202/2; 258/1; 291/3 the transmembrane complex includes cytochrome b (see PIR:CBHU), cytochrome c1, Rieske iron-sulfur protein, and other accessory proteins cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain transit peptide (mitochondrion) 1-84 predicted product cytochrome c1 85-325 predicted domain cytochrome c1 heme protein homology 90-315 domain transmembrane 288-306 predicted binding-site heme (Cys) (covalent) 121,124 predicted binding-site heme iron (His, Met) (axial ligands) 125,244 predicted 325 complete MAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVM LSALGMLAAGGAGLAVALHSAVSASDLEVHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQV CASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYP NSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQ AIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLV PLVYTIKRHKWSVLKSRKLAYRPPK
CCBO1 A00118 31-Mar-1981 31-Mar-1981 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 bovine cattle Bos primigenius taurus Wakabayashi, S. Matsubara, H. Kim, C.H. King, T.E. J. Biol. Chem. 25719829335-9344 Structural studies of bovine heart cytochrome c-1. MUID82265565 A00118 protein 1-241 This is the heme-containing component of the cytochrome c1 complex, which is located in the inner membrane of the mitochondrion and functions as electron donor to cytochrome c in the mitochondrial respiratory chain. the transmembrane complex includes cytochrome b (see PIR:CBBO), cytochrome c1, Rieske iron-sulfur protein (see PIR:A34660), and other accessory proteins (see PIR:CCBO11, PIR:CCBO17, PIR:A24864, PIR:ZPBOC1, and PIR:ZPBOC2) cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome c1 heme protein homology 6-231 domain transmembrane 203-222 predicted binding-site heme (Cys) (covalent) 37,40 experimental binding-site heme iron (His, Met) (axial ligands) 41,160 predicted 241 complete SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEDE AKALAEEVEVQDGPNEDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRAR HGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIGMAPPIYNEVLEFDDGTPATMS QVAKDVCTFLRWAAEPEHDHRKRMGLKMLLMMGLLLPLVYAMKRHKWSVLKSRKLAYRPP K
JQ0347 JQ0347 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome c1 Rhodopseudomonas viridis Rhodopseudomonas viridis Verbist, J. Lang, F. Gabellini, N. Oesterhelt, D. Mol. Gen. Genet. 2191989445-452 Cloning and sequencing of the fbcF, B and C genes encoding the cytochrome b/c1 complex from Rhodopseudomonas viridis. MUID90158506 JQ0347 DNA 1-282 strain 133 This protein is one of the three subunits of the ubiquinol-cytochrome C2 oxidoreductase complex which is coupled with another membrane-protein complex at the reaction center in a cyclic electron-transport system which catalyzes the synthesis of ATP. fbcC cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c1 heme protein homology 31-278 binding-site heme (Cys) (covalent) 62,65 predicted binding-site heme iron (His, Met) (axial ligands) 66,207 predicted 282 complete MTIKLRFVASLALVFGLAAASVPAQASGGDTPHLQSWSFAGPFGQYDKAQLRRGFQVFQN VCVSCHTLENGGFRNLPSRAAPNWPLDEVRQLAASWPVQVKDINDKGDPMQRAPKLPDRI PSQYANEAAARIIHNGAVPPDLSVIAKARTFQRGFPWWVTDIFTQYNENGVDYIVALLNG YEDPPERFKVPDGSFYNKYFPGHIIGMTPPIADGLVTYGDGTPETQLQYSKDVAAFLMWA AEPTLDVRKRIGWWVLGFLVIFTGLLVATKIVVWRPVKKGLA
CCBY1H A22737 S66948 A26500 28-Dec-1987 28-Dec-1987 21-Jul-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor protein O2816 protein YOR065w yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Sadler, I. Suda, K. Schatz, G. Kaudewitz, F. Haid, A. EMBO J. 319842137-2143 Sequencing of the nuclear gene for the yeast cytochrome c1 precursor reveals an unusually complex amino-terminal presequence. MUID85027167 A22737 DNA 1-309 EMBLX00791 NIDg1197521 PIDNCAA25375.1 PIDg3610 Bohn, C. Bolotin-Fukuhara, M. Daignan-Fornier, B. Dang, D.V. Valens, M. submitted to the Protein Sequence Database July1996 S66948 DNA 1-309 EMBLZ74973 NIDg1420210 PIDNCAA99258.1 PIDg1420211 GSPDBGN00015 MIPSYOR065w strain S288C SGDCYT1 SGDCTC1 MIPSYOR065w SGDS0005591 MIPSYOR065w 15R nuclear cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain transit peptide (mitochondrion) 1-61 predicted product cytochrome c1 62-309 predicted domain cytochrome c1 heme protein homology 70-296 domain transmembrane 269-286 predicted binding-site heme (Cys) (covalent) 101,104 predicted binding-site heme iron (His, Met) (axial ligands) 105,225 predicted 309 complete MFSNLSKRWAQRTLSKSFYSTATGAASKSGKLTQKLVTAGVAAAGITASTLLYADSLTAE AMTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSH TNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLI VKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGT PATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKF VFNPPKPRK
A27187 A27187 05-Oct-1988 15-Oct-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor bc1 complex cytochrome c1 complex III cytochrome c1 cytochrome c1 heme protein Neurospora crassa Neurospora crassa Roemisch, J. Tropschug, M. Sebald, W. Weiss, H. Eur. J. Biochem. 1641987111-115 The primary structure of cytochrome c-1 from Neurospora crassa. MUID87161871 A27187 mRNA 1-332 GBX05235 NIDg3005 PIDNCAA28860.1 PIDg3006 the authors translated the codon AGT for residue 316 as Arg cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain transit peptide (mitochondrion) 1-70 predicted product cytochrome c1 71-332 predicted domain cytochrome c1 heme protein homology 79-305 domain transmembrane 278-296 predicted binding-site heme (Cys) (covalent) 110,113 predicted binding-site heme iron (His, Met) (axial ligands) 114,234 predicted 332 complete MLARTCLRSTRTFASAKNGAFKFAKRSASTQSSGAAAESPLRLNIAAAAATAVAAGSIAW YYHLYGFASAMTPAEEGLHATKYPWVHEQWLKTFDHQALRRGFQVYREVCASCHSLSRVP YRALVGTILTVDEAKALAEENEYDTEPNDQGEIEKRPGKLSDYLPDPYKNDEAARFANNG ALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGASVGAGLNFNPYFPGTGIAMARVLYD GLVDYEDGTPASTSQMAKDVVEFLNWAAEPEMDDRKRMGMKVLVVTSVLFALSVYVKRYK WAWLKSRKIVYDPPKSPPPATNLALPQQRAKS
S20014 S20014 S21975 S36371 16-Sep-1992 15-Oct-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor (clone pC(1)3II) bc1 complex cytochrome c1 complex III cytochrome c1 cytochrome c1 heme protein potato potato Solanum tuberosum Braun, H.P. Emmermann, M. Kruft, V. Schmitz, U.K. Mol. Gen. Genet. 2311992217-225 Cytochrome c(1) from potato: a protein with a presequence for targeting to the mitochondrial intermembrane space. MUID92140360 S20014 mRNA 1-320 EMBLX62124 Schmitz, U. submitted to the EMBL Data Library September1991 S21975 DNA 1-211,'A',213-320 EMBLX62124 NIDg21438 PIDNCAA44055.1 PIDg21439 Wegener, S. Schmitz, U.K. Curr. Genet. 241993256-259 The presequence of cytochrome c(1) from potato mitochondria is encoded on four exons. MUID94037151 S36371 not compared with conceptual translation DNA 1-87,'S',89-201,'N',203-320 GBS66866 NIDg440952 PIDNAAB28813.1 PIDg440953 cyc1 nuclear 2/1; 13/1; 42/1; 104/2; 197/3; 221/3; 269/3; 282/3 cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain transit peptide (mitochondrion) 1-77 predicted product cytochrome c1 78-320 predicted domain cytochrome c1 heme protein homology 85-310 domain transmembrane 282-301 predicted binding-site heme (Cys) (covalent) 116,119 predicted binding-site heme iron (His, Met) (axial ligands) 120,239 predicted 320 complete MSLGKKIRIGFDGFGRINRFITRGAAQRNDSKLPSRNDALKHGLDGLGSAGSKSFRALAA IGAGVSGLLSFATIAYSDEAEHGLECPNYPWPHEGILSSYDHASIRRGHQVYQQVCASCH SMSLISYRDLVGVAYTEEETKAMAAEIEVVDGPNDEGEMFTRPGKLSDRFPQPYANEAAA RFANGGAYPPDLSLITKARHNGQNYVFALLTGYRDPPAGVSIREGLHYNPYFPGGAIAMP KMLNDGAVEYEDGIPATEAQMGKDVVSFLSWAAEPEMEERKLMGFKWIFVLSLALLQAAY YRRLRWSVLKSRKLVLDVVN
JQ0021 JQ0021 S02075 17-Feb-1994 17-Feb-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 complex III polypeptide IV ubiquinol--cytochrome-c reductase polypeptide IV Euglena gracilis Euglena gracilis Mukai, K. Wakabayashi, S. Matsubara, H. J. Biochem. 1061989479-482 Molecular cloning and nucleotide sequence of a cDNA encoding Euglena gracilis cytochrome c1. MUID90110031 JQ0021 mRNA 1-243 part of this sequence, including the amino end of the mature protein, was confirmed by protein sequencing Mukai, K. Yoshida, M. Toyosaki, H. Yao, Y. Wakabayashi, S. Matsubara, H. Eur. J. Biochem. 1781989649-656 An atypical heme-binding structure of cytochrome c1 of Euglena gracilis mitochondrial complex III. MUID89107187 S02075 protein 1-46 Cytochrome c1 is a subunit of the cytochrome bc1 complex, which is one of the oligomeric enzymes in the respiratory chain of the mitochondrial inner membrane. cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein product ubiquinol--cytochrome-c reductase cytochrome c1 1-243 experimental domain cytochrome c1 heme protein homology 5-233 region cytochrome c binding 57-74,165-172 predicted domain transmembrane 207-221 predicted binding-site heme (Cys) (covalent) 39 experimental binding-site heme iron (His, Met) (axial ligands) 40,159 predicted 243 complete GVDSHPPALPWPHFQWFQGLDWRSVRRGKEVYEQVFAPCHSLSFIKYRHFEAFMSKEEVK NMAASFEVDDDPDEKGEARKRPGKRFDTVVQPYKNEQEARYANNGALPPDLSVITNARHG GVDYIYALLTGYGRPVPGGVQLSTTQWYNPYFHGGIIGMPPPLTDDMIEYEDGTPASVPQ MAKDVTCFLEWCSNPWWDERKLLGYKTIATLAVIAVSSGYYNRFLSGLWRSRRLAFRPFN YSK
CCQF1R S12258 A38815 31-Dec-1991 31-Dec-1991 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor Rhodospirillum rubrum Rhodospirillum rubrum Majewski, C. Trebst, A. Mol. Gen. Genet. 2241990373-382 The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc(1)-complex. MUID91094774 S12258 DNA 1-272 EMBLX55387 NIDg46382 PIDNCAA39060.1 PIDg46386 the authors translated the codon CCG for residue 111 as Thr, GCC for residue 112 as Pro, and GAC for residue 113 as Ala A38815 protein 25-50 petC cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase transmembrane protein domain signal sequence 1-24 predicted product cytochrome c1 25-272 experimental domain cytochrome c1 heme protein homology 30-271 domain transmembrane 244-261 predicted binding-site heme (Cys) (covalent) 61,64 predicted binding-site heme iron (His, Met) (axial ligands) 65,200 predicted 272 complete MTTIVKRALVAAGMVLAIGGAAQANEGGVSLHKQDWSWKGIFGRYDQPQLQRGFQVFHEV CSTCHGMKRVAYRNLSALGFSEDGIKELAAEKEFPAGPDDNGDMFTRPGTPADHIPSPFA NDKAAAAANGGAAPPDLSLLAKARPGGPNYIYSLLEGYASDSPGEPAEWWVKQQQEKGLE VAFNEAKYFNDYFPGHAISMPPPLMDDLITYEDGTAATKDQMAQDVVAYLNWAAEPELDA RKSLGLKVLLFLGVLTAMLLALKLAIWRDVKH
C25405 C25405 E25405 05-Oct-1988 22-Jul-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor Rhodobacter capsulatus (strain GA) Rhodobacter capsulatus Gabellini, N. Sebald, W. Eur. J. Biochem. 1541986569-579 Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c-1. MUID86136096 source is designated as Rhodopseudomonas sphaeroides C25405 DNA 1-280 GBX03476 NIDg46007 PIDNCAA27196.1 PIDg46010 E25405 protein 22-39 fbcC petC cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase respiratory chain transmembrane protein domain signal sequence 1-21 predicted product cytochrome c1 22-280 experimental domain cytochrome c1 heme protein homology 24-276 domain transmembrane 249-266 predicted binding-site heme (Cys) (covalent) 55,58 predicted binding-site heme iron (His, Met) (axial ligands) 59,205 predicted 280 complete MKKLLISAVSALVLGSGAALANSNVQDHAFSFEGIFGKFDQAQLRRGFQVYSEVCSTCHG MKFVPIRTLSDDGGPQLDPTFVREYAAGLDTIIDKDSGEERDRKETDMFPTRVGDGMGPD LSVMAKARAGFSGPAGSGMNQLFKGIGGPEYIYRYVTGFPEENPACAPEGIDGYYYNEVF QVGGVPDTCKDAAGIKTTHGSWAQMPPALFDDLVTYEDGTPATVDQMGQDVASFLMWAAE PKLVARKQMGLVAVVMLGLLSVMLYLTNKRLWAPYKRQKA
C29336 C29336 31-Dec-1988 22-Jul-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor Rhodobacter capsulatus (strain SB 1003) Rhodobacter capsulatus strain SB 1003 Davidson, E. Daldal, F. J. Mol. Biol. 195198713-24 Primary structure of the bc-1 complex of Rhodopseudomonas capsulata. Nucleotide sequence of the pet operon encoding the Rieske, cytochrome b, and cytochrome c-1 apoproteins. MUID88011223 C29336 DNA 1-279 EMBLX05630 NIDg46093 PIDNCAA29118.1 PIDg46096 fbcC petC cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase respiratory chain transmembrane protein domain signal sequence 1-21 predicted product cytochrome c1 22-279 predicted domain cytochrome c1 heme protein homology 24-275 domain transmembrane 248-265 predicted binding-site heme (Cys) (covalent) 55,58 predicted binding-site heme iron (His, Met) (axial ligands) 59,204 predicted 279 complete MKKLLISAVSALVLGSGAAFANSNVPDHAFSFEGIFGKYDQAQLRRGFQVYNEVCSACHG MKFVPIRTLADDGGPQLDPTFVREYAAGLDTIIDKDSGEERDRKETDMFPTRVGDGMGPD LSVMAKARAGFSGPAGSGMNQLFKGMGGPEYIYNYVIGFEENPECAPEGIDGYYYNKTFQ IGGVPDTCKDAAGVKITHGSWARMPPPLVDDQVTYEDGTPATVDQMAQDVSAFLMWAAEP KLVARKQMGLVAMVMLGLLSVMLYLTNKRLWAPYKGHKA
S13870 S13870 B34591 A34935 31-Dec-1988 22-Jul-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor Rhodobacter sphaeroides Rhodobacter sphaeroides Yun, C.H. Beci, R. Crofts, A.R. Kaplan, S. Gennis, R.B. Eur. J. Biochem. 1941990399-411 Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc(1) complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant. MUID91099313 S13870 DNA 1-285 EMBLX56157 NIDg46425 PIDNCAA39625.1 PIDg46428 the authors translated the codon CGG for residue 49 as Glu and GCA for residue 59 as Ser the sequence from Fig. 6 is inconsistent with that from Fig. 2 in lacking 27-His and having 120-Pro Andrews, K.M. Crofts, A.R. Gennis, R.B. Biochemistry 2919902645-2651 Large-scale purification and characterization of a highly active four-subunit cytochrome bc-1 complex from Rhodobacter sphaeroides. MUID90268011 B34591 protein 23-42 Purvis, D.J. Theiler, R. Niederman, R.A. J. Biol. Chem. 26519901208-1215 Chromatographic and protein chemical analysis of the ubiquinol-cytochrome c-2 oxidoreductase isolated from Rhodobacter sphaeroides. MUID90110107 A34935 protein 66-70,'T',72,'T',74-79,'X',81-82,'XX',85 fbcC In this organism, ubiquinol--cytochrome-c reductase consists of cytochrome b, cytochrome c1, a Rieske iron-sulfur protein, and a 14K polypeptide. electron transfer from dihydroquinol to cytochrome c2 respiratory chain cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase respiratory chain transmembrane protein domain signal sequence 1-22 predicted product cytochrome c1 23-285 experimental domain cytochrome c1 heme protein homology 27-278 domain transmembrane 251-268 predicted binding-site heme (Cys) (covalent) 58,61 predicted binding-site heme iron (His, Met) (axial ligands) 62,207 predicted 285 complete MIRKLTLTAATALALSGGAAMAAGGGHVEDVPFSFEGPFGTFDQHQLQRGLQVYTEVCAA CHGMKFVPIRSLSEPGGPELPEDQVRAYATQFTVTDEETGEDREGKPTDHFPHSALENAA DLSLMAKARAGFHGPMGTGISQLFNGIGGPEYIYSVLTGFPEEPPKCAEGHEPDGFYYNR AFQNGSVPDTCKDANGVKTTAGSWIAMPPPLMDDLVEYADGHDASVHAMAEDVSAFLMWA AEPKLMARKQAGFTAVMFLTVLSVLLYLTNKRLWAGVKGKKKTNV
C29413 C29413 31-Mar-1989 15-Oct-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 precursor bc1 complex cytochrome c1 complex III cytochrome c1 cytochrome c1 heme protein Paracoccus denitrificans Paracoccus denitrificans Kurowski, B. Ludwig, B. J. Biol. Chem. 262198713805-13811 The genes of the Paracoccus denitrificans bc-1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits. MUID88007612 C29413 DNA 1-450 GBM17522 NIDg150569 PIDNAAA25573.1 PIDg150572 Paracoccus cytochrome c1 heme protein cytochrome c1 heme protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein oxidoreductase transmembrane protein domain signal sequence 1-24 predicted product cytochrome c1 25-450 predicted domain cytochrome c1 heme protein homology 214-444 domain transmembrane 417-433 predicted binding-site heme (Cys) (covalent) 245,248 predicted binding-site heme iron (His, Met) (axial ligands) 249,373 predicted 450 complete MTLRNASLTAVAALTVALAGGAVAQDASTAPGTTAPAGSSYHTNEAAPAAADTAPAAEAA DEPAAEEAEAGEAEVTEEPAATETPAEEPAADEPAATEEPDAEAEPAAEEAQATTEEAPA EEPAAEEPAAEEPAEEPAADAPAEEAAAEEAPAEPEAAAEEPAAEEPEATEEEAPAEEAA AEEAPAEEVVEDEAAADHGDAAAQEAGDSHAAAHIEDISFSFEGPFGKFDQHQLQRGLQV YTEVCSACHGLRYVPLRTLADEGGPQLPEDQVRAYAANFDITDPETEEDRPRVPTDHFPT VSGEGMGPDLSLMAKARAGFHGPYGTGLSQLFNGIGGPEYIHAVLTGYDGEEKEEAGAVL YHNAAFAGNWIQMAAPLSDDQVTYEDGTPATVDQMATDVAAFLMWTAEPKMMDRKQVGFV SVIFLIVLAALLYLTNKKLWQPIKHPRKPE
CCPS2S S13938 S03857 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c552 precursor Pseudomonas stutzeri Pseudomonas stutzeri Juengst, A. Wakabayashi, S. Matsubara, H. Zumft, W.G. FEBS Lett. 2791991205-209 The nirSTBM region coding for cytochrome cd(1)-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins. MUID91160715 S13938 DNA 1-291 EMBLX56813 NIDg45838 PIDNCAA40152.1 PIDg45841 Denariaz, C.M. Liu, M.Y. Payne, W.J. LeGall, J. Marquez, L. Dunford, H.B. van Beeumen, J. Arch. Biochem. Biophys. 2701989114-125 Cytochrome c peroxidase activity of a protease-modified form of cytochrome c-552 from the denitrifying bacterium Pseudomonas perfectomarina. MUID89192360 S03857 protein 24-58,'D',60-228,'N',230-267,'S',269,'N' the source is designated as Pseudomonas perfectomarina nirB cytochrome c552 chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-23 predicted product cytochrome c552 24-291 experimental binding-site heme (Cys) (covalent) 68,71 predicted binding-site heme iron (His) (axial ligand) 72 predicted binding-site heme (Cys) (covalent) 157,161 predicted binding-site heme iron (His) (axial ligand) 162 predicted 291 complete MKKTLMASAVGAVIAFGTHGAMAAAPADWSSVAATDVTLFYPGVSPVEWITKGTEHGGAR ALKKGETCAGCHSEEASDMGEKMASGKKLEPSPIAGKAPFINAKVQAANDGENLYLRFTW KQPAASGAAPMDADNPVKIAYMLEGGSKVELAEAGGCWGSCHGDARTMPGAADTKTKYVK DGSLANGVYYDLNQWRSGENKAFDGYVATERVMEGGQALVDAQGKLDGDTWTVVFTRKFA GGEGDVTLAPGNLYNFGFAIHDDSATGRYHHVSLGYSLGIDAQGDITAAKQ
O4PSZ S13937 30-Sep-1991 30-Sep-1991 03-Mar-2000
denitrification system component nirT precursor membrane-bound tetraheme cytochrome Pseudomonas stutzeri Pseudomonas stutzeri Juengst, A. Wakabayashi, S. Matsubara, H. Zumft, W.G. FEBS Lett. 2791991205-209 The nirSTBM region coding for cytochrome cd(1)-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins. MUID91160715 S13937 DNA 1-201 EMBLX56813 NIDg45838 PIDNCAA40151.1 PIDg45840 nirT denitrification system component nirT nirT homology chromoprotein electron transfer heme iron metalloprotein transmembrane protein domain signal sequence 1-28 predicted domain nirT homology 19-193 product denitrification system component nirT 29-201 predicted domain transmembrane 29-45 predicted binding-site heme (Cys) (covalent) 58,61 predicted binding-site heme iron (His) (axial ligand) 62 predicted binding-site heme (Cys) (covalent) 88,91 predicted binding-site heme iron (His) (axial ligand) 92 predicted binding-site heme (Cys) (covalent) 148,151 predicted binding-site heme iron (His) (axial ligand) 152 predicted binding-site heme (Cys) (covalent) 180,183 predicted binding-site heme iron (His) (axial ligand) 184 predicted 201 complete MTDKDGNKQQKGGILALLRRPSTRYSLGGILIVGIVAGIVFWGGFNTALEATNTETFCIS CHEMGDNVYPEYKETIHYANRTGVRATCPDCHVPRDWTHKMVRKVEASKELWGKIVGTID TAEKFEAKRLTLARREWARMRASDSRECRNCHSLESMSSDMQKQRARKQHEMAREDNLTC IACHKGIAHHLPEGMTEEDED
S56137 S56137 S50165 10-Sep-1999 10-Sep-1999 03-Mar-2000
membrane-bound tetraheme cytochrome napC cytochrome c, tetraheme Thiosphaera pantotropha Thiosphaera pantotropha Berks, B.C. Richardson, D.J. Reilly, A. Willis, A.C. Ferguson, S.J. Biochem. J. 3091995983-992 The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha. MUID95366980 S56137 nucleic acid sequence not shown DNA 1-237 EMBLZ36773 NIDg600089 PIDNCAA85348.1 PIDg600095 napC denitrification system component nirT nirT homology chromoprotein electron transfer heme iron metalloprotein transmembrane protein domain nirT homology 23-198 domain transmembrane 29-49 predicted binding-site heme (Cys) (covalent) 62,65 predicted binding-site heme iron (His) (axial ligand) 66 predicted binding-site heme (Cys) (covalent) 92,95 predicted binding-site heme iron (His) (axial ligand) 96 predicted binding-site heme (Cys) (covalent) 152,155 predicted binding-site heme iron (His) (axial ligand) 156 predicted binding-site heme (Cys) (covalent) 185,188 predicted binding-site heme iron (His) (axial ligand) 189 predicted 237 complete MGWIRASIRWIWGRVTWFWRVISRPSSFLSIGFLTLGGFICGVIFWGGFNTALEITNTEK FCTSCHEMRDNVYQELMPTVHFSNRSGVRASCPDCHVPHEWTDKIARKMQASKEVWGKIF GTISTREKFLEKRLELAKHEWARLKANDSLECRNCHAAVAMDFTKQTRRAPQIHERYLIS GEKTCIDCHKGIAHQLPDMTGIEPGWLEPPELRGEEQAWLGGGAEAVHRYLATVETR
H64062 H64062 10-Sep-1999 10-Sep-1999 03-Mar-2000
membrane-bound tetraheme cytochrome nirT denitrification system component nirT Haemophilus influenzae (strain Rd KW20) Haemophilus influenzae Fleischmann, R.D. Adams, M.D. White, O. Clayton, R.A. Kirkness, E.F. Kerlavage, A.R. Bult, C.J. Tomb, J.F. Dougherty, B.A. Merrick, J.M. McKenney, K. Sutton, G. FitzHugh, W. Fields, C. Gocayne, J.D. Scott, J. Shirley, R. Liu, L.I. Glodek, A. Kelley, J.M. Weidman, J.F. Phillips, C.A. Spriggs, T. Hedblom, E. Cotton, M.D. Utterback, T.R. Hanna, M.C. Nguyen, D.T. Saudek, D.M. Brandon, R.C. Fine, L.D. Fritchman, J.L. Fuhrmann, J.L. Geoghagen, N.S.M. Gnehm, C.L. McDonald, L.A. Small, K.V. Fraser, C.M. Smith, H.O. Venter, J.C. Science 2691995496-512 Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. MUID95350630 H64062 nucleic acid sequence not shown translation not shown DNA 1-200 GBU32719 GBL42023 NIDg1573310 PIDNAAC22009.1 PIDg1573318 TIGRHI0348 named as homolog to a protein from Pseudomonas stutzeri nirT denitrification system component nirT nirT homology chromoprotein electron transfer heme iron metalloprotein transmembrane protein domain nirT homology 17-188 domain transmembrane 22-42 predicted binding-site heme (Cys) (covalent) 55,58 predicted binding-site heme iron (His) (axial ligand) 59 predicted binding-site heme (Cys) (covalent) 83,86 predicted binding-site heme iron (His) (axial ligand) 87 predicted binding-site heme (Cys) (covalent) 143,146 predicted binding-site heme iron (His) (axial ligand) 147 predicted binding-site heme (Cys) (covalent) 175,178 predicted binding-site heme iron (His) (axial ligand) 179 predicted 200 complete MSEKKPNILKRFWQWFRKPSRMAIGTIIILSAIGGILSWVGFNYGLEKTNTEQFCASCHM QDAYPEYLHSVHYQTRTGVGASCPDCHVPHEFGAKMKRKIIAAKEVYAHYTGKVDTLEKF NAHRLEMAQNEWARMKANDSKECRNCHNVDRMTFNDQRSVAARMHQKMKTEGKTCIDCHK GIAHQLPDMSGVESGFKDEK
S34221 B64841 S43697 S34221 06-Jan-1995 05-Dec-1997 03-Mar-2000
membrane-bound tetraheme cytochrome torC Escherichia coli Escherichia coli Blattner, F.R. Plunkett III, G. Bloch, C.A. Perna, N.T. Burland, V. Riley, M. Collado-Vides, J. Glasner, J.D. Rode, C.K. Mayhew, G.F. Gregor, J. Davis, N.W. Kirkpatrick, H.A. Goeden, M.A. Rose, D.J. Mau, B. Shao, Y. Science 27719971453-1462 The complete genome sequence of Escherichia coli K-12. MUID97426617 B64841 nucleic acid sequence not shown translation not shown DNA 1-390 GBAE000201 GBU00096 NIDg2367113 PIDNAAC74081.1 PIDg1787230 UWGPb0996 strain K-12, substrain MG1655 Mejean, V. Iobbi-Nivol, C. Lepelletier, M. Giordano, G. Chippaux, M. Pascal, M.C. Mol. Microbiol. 1119941169-1179 TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon. MUID94293785 S43697 preliminary DNA 1-72,'CELN',77-193,'DV',196-390 EMBLX73888 NIDg556701 PIDNCAA52094.1 PIDg556702 strain K-12 torC electron transfer trimethylamine N-oxide respiratory chain membrane-bound tetraheme cytochrome torC nirT homology chromoprotein electron transfer heme inner membrane iron metalloprotein transmembrane protein domain intracellular 1-16 predicted domain nirT homology 9-183 domain transmembrane 17-33 predicted domain periplasmic 34-390 predicted binding-site heme (Cys) (covalent) 48,51 predicted binding-site heme iron (His) (axial ligand) 52 predicted binding-site heme (Cys) (covalent) 77,80 predicted binding-site heme iron (His) (axial ligand) 81 predicted binding-site heme (Cys) (covalent) 138,141 predicted binding-site heme iron (His) (axial ligand) 142 predicted binding-site heme (Cys) (covalent) 170,173 predicted binding-site heme iron (His) (axial ligand) 174 predicted binding-site heme (Cys) (covalent) 329,332 predicted binding-site heme iron (His) (axial ligand) 333 predicted 390 complete MRKLWNALRRPSARWSVLALVAIGIVIGIALIVLPHVGIKVTSTTEFCVSCHSMQPVYEE YKQSVHFQNASGVRAECHDCHIPPDIPGMVKRKLEASNDIYQTFIAHSIDTPEKFEAKRA ELAEREWARMKENNSATCRSCHNYDAMDHAKQHPEAARQMKVAAKDNQSCIDCHKGIAHQ LPDMSSGFRKQFDELRASANDSGDTLYSIDIKPIYAAKGDKEASGSLLPASEVKVLKRDG DWLQIEITGWTESAGRQRVLTQFPGKRIFVASIRGDVQQQVKTLEKTTVADTNTEWSKLQ ATAWMKKGDMVNDIKPIWAYADSLYNGTCNQCHGAPEIAHFDANGWIGTLNGMIGFTSLD KREERTLLKYLQMNASDTAGKAHGDKKEEK
I64083 I64083 18-Aug-1995 26-Jul-1996 03-Mar-2000
membrane-bound tetraheme cytochrome torC Haemophilus influenzae (strain Rd KW20) Haemophilus influenzae Fleischmann, R.D. Adams, M.D. White, O. Clayton, R.A. Kirkness, E.F. Kerlavage, A.R. Bult, C.J. Tomb, J.F. Dougherty, B.A. Merrick, J.M. McKenney, K. Sutton, G. FitzHugh, W. Fields, C. Gocayne, J.D. Scott, J. Shirley, R. Liu, L.I. Glodek, A. Kelley, J.M. Weidman, J.F. Phillips, C.A. Spriggs, T. Hedblom, E. Cotton, M.D. Utterback, T.R. Hanna, M.C. Nguyen, D.T. Saudek, D.M. Brandon, R.C. Fine, L.D. Fritchman, J.L. Fuhrmann, J.L. Geoghagen, N.S.M. Gnehm, C.L. McDonald, L.A. Small, K.V. Fraser, C.M. Smith, H.O. Venter, J.C. Science 2691995496-512 Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. MUID95350630 I64083 nucleic acid sequence not shown translation not shown DNA 1-368 GBU32747 GBL42023 NIDg1573635 PIDNAAC22304.1 PIDg1573642 TIGRHI0644 named as homolog to a protein from Escherichia coli torC GTG electron transfer trimethylamine N-oxide respiratory chain membrane-bound tetraheme cytochrome torC nirT homology chromoprotein electron transfer heme inner membrane iron metalloprotein transmembrane protein domain intracellular 1-8 predicted domain nirT homology 7-173 domain transmembrane 9-25 predicted domain periplasmic 26-368 predicted binding-site heme (Cys) (covalent) 39,42 predicted binding-site heme iron (His) (axial ligand) 43 predicted binding-site heme (Cys) (covalent) 68,71 predicted binding-site heme iron (His) (axial ligand) 72 predicted binding-site heme (Cys) (covalent) 128,131 predicted binding-site heme iron (His) (axial ligand) 132 predicted binding-site heme (Cys) (covalent) 160,163 predicted binding-site heme iron (His) (axial ligand) 164 predicted binding-site heme (Cys) (covalent) 316,319 predicted binding-site heme iron (His) (axial ligand) 320 predicted 368 complete MAMSKMKKIVTALCLVGVGVGALWGSQWIMHKTSTPEFCASCHSMSYPQQEWEGSSHFAN AKGVRAQCSDCHIPKEGWHYVKAKFIALKDLWYEAQGKIENKEKYEAHRAEMAQRVWKDM KANDSETCRSCHSFDAMELSKQTKLAKQTHTEAQTNGQTCIDCHKGIVHFLPEVHGDQNT QKSSAVQGGTLSDGSAIFATEMVKATNDKGNEVRLMPYAELMQWKVDGDQIQGTLHGWQQ VGAEAVVYQELGKRITLALMDEDARNHVQVLKIVHDAVTDSDWKEISVAVNVAKEKMTSD LTTLNQYGNQLNQTQCSGCHAAIGADHYTANQWIGVVNSMKDRTSMKKDEVRALTIYLQR NAKDMAKQ
A39303 A39303 I40619 S34211 03-Aug-1992 02-Jul-1996 03-Mar-2000
cytochrome c554 precursor Chloroflexus aurantiacus Chloroflexus aurantiacus Dracheva, S. Williams, J.C. Van Driessche, G. Van Beeumen, J.J. Blankenship, R.E. Biochemistry 30199111451-11458 The primary structure of cytochrome c-554 from the green photosynthetic bacterium Chloroflexus aurantiacus. MUID92075661 A39303 DNA 1-414 GBM77813 NIDg144448 PIDNAAA23100.1 PIDg144449 part of this sequence was confirmed by protein sequencing Watanabe, Y. Feick, R.G. Shiozawa, J.A. Arch. Microbiol. 1631995124-130 Cloning and sequencing of the genes encoding the light-harvesting B806-866 polypeptides and initial studies on the transcriptional organization of puf2B, puf2A and puf2C in Chloroflexus aurantiacus. MUID95225715 I40619 translated from GB/EMBL/DDBJ DNA 1-51 EMBLX73899 NIDg313697 PIDNCAA52106.1 PIDg313700 immediate electron donor to the oxidized bacteriochlorophyll dimer (BChl2) cytochrome c554 chromoprotein electron transfer heme iron metalloprotein periplasmic space photosynthesis domain signal sequence 1-24 predicted product cytochrome c554 25-414 predicted binding-site heme iron (Met, His) (axial ligands) 119,135 predicted binding-site heme (Cys) (covalent) 131,134 predicted binding-site heme iron (Met, His) (axial ligands) 154,183 predicted binding-site heme (Cys) (covalent) 179,182 predicted binding-site heme iron (Met, His) (axial ligands) 283,298 predicted binding-site heme (Cys) (covalent) 294,297 predicted binding-site heme iron (Met, His) (axial ligands) 330,382 predicted binding-site heme (Cys) (covalent) 378,381 experimental 414 complete MQSSRPSDRQLAIVVSVAVGIVVAVITTATFWWVYDLTLGRAQREAAQTAGARWSPSDGI KVITSSPPVTPTDGRQNWMGTQAWNEGVQAGQAWIQQYPNTVNVQVLIGMSSAQIWTYMQ QYVSGALGVGCQYCHNINNFASDEYPQKIAARNMLRLVRDVNAEFIVNLPNWQGNYVQCA TCHNNAPNNLEGFGAQFINSVPPIKVTVDPLDANGMAILDPAQKPEAIREPVLLKDAILF YIYNYQVWKPFDPNDPESGRGSLALTYDGGRTQDQVTINQNVMNYQAWSLGVGCTFCHNS RNFVAYELNPAGDNVLNPLYAYNKLKAQRMLLLTTWLAENWPRYGAIAKPEIPTGSGAAS RYSYQRLGDGQIYNVPGCYTCHQGNNIPLASINQANIPSGDAGIVVLPPQIRGR
A59036 A59036 A59037 23-Apr-1999 23-Apr-1999 23-Mar-2001
cytochrome c554, tetraheme, precursor hydroxylamine oxidoreductase-linked cytochrome c554 Nitrosomonas europaea Nitrosomonas europaea Hommes, N.G. Sayavedra-Soto, L.A. Arp, D.J. Gene 146199487-89 Sequence of hcy, a gene encoding cytochrome c-554 from Nitrosomonas europaea. MUID94341575 A59036 translated from GB/EMBL/DDBJ DNA 1-235 GBU05951 NIDg454393 PIDNAAA60464.1 PIDg454394 submitted to GenBank, January 1994 Bergmann, D.J. Arciero, D.M. Hooper, A.B. J. Bacteriol. 17619943148-3153 Organization of the hao gene cluster of Nitrosomonas europaea: genes for two tetraheme c-cytochromes. MUID94252980 A59037 translated from GB/EMBL/DDBJ DNA 1-235 GBU08288 NIDg476339 PIDNAAA19967.1 PIDg476340 submitted to GenBank, April 1994 Iverson, T.M. Arciero, D.M. Hsu, B.T. Logan, M.S.P. Hooper, A.B. Rees, D.C. Nat. Struct. Biol. 519981005-1012 Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. MUID99023199 PDB1BVB annotation X-ray crystallography, 2.6 angstroms the His-126 is a ligand through the 3'-nitrogen For hydroxylamine oxidase, see PIR:A36954. hcy cycA there are at least three copies of this gene, two of which may have identical amino acid sequences transfers two electrons from hydroxylamine oxidase to two molecules of cytochrome c552 Nitrosomonas cytochrome c554 chromoprotein electron transfer heme iron metalloprotein periplasmic space domain signal sequence 1-24 predicted product cytochrome c554, tetraheme 25-235 experimental binding-site heme (Cys) (covalent) 35,38 experimental binding-site heme iron (His) (axial ligands) 39,126 experimental binding-site heme iron (His) (axial ligands) 51,162 experimental binding-site heme (Cys) (covalent) 84,87 experimental binding-site heme iron (His) (axial ligand) 88 experimental binding-site heme (Cys) (covalent) 112,115 experimental binding-site heme iron (His) (axial ligands) 116,203 experimental binding-site heme (Cys) (covalent) 158,161 experimental 235 complete MKIMIACGLVAAALFTLTSGQSLAADAPFEGRKKCSSCHKAQAQSWKDTAHAKAMESLKP NVKKEAKQKAKLDPAKDYTQDKDCVGCHVDGFGQKGGYTIESPKPMLTGVGCESCHGPGR NFRGDHRKSGQAFEKSGKKTPRKDLAKKGQDFHFEERCSACHLNYEGSPWKGAKAPYTPF TPEVDAKYTFKFDEMVKEVKAMHEHYKLEGVFEGEPKFKFHDEFQASAKPAKKGK
S00139 S00139 07-Sep-1990 19-Jul-1996 15-Sep-2000
photosynthetic reaction center cytochrome precursor [validated] Rhodopseudomonas viridis Rhodopseudomonas viridis Weyer, K.A. Lottspeich, F. Gruenberg, H. Lang, F. Oesterhelt, D. Michel, H. EMBO J. 619872197-2202 Amino acid sequence of the cytochrome subunit of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. S00139 not compared with conceptual translation DNA 1-356 EMBLX05768 NIDg46474 PIDNCAA29223.1 PIDg758274 parts of this sequence, including the amino and carboxyl ends of the mature protein, were confirmed by protein sequencing Weyer, K.A. Schaefer, W. Lottspeich, F. Michel, H. Biochemistry 2619872909-2914 The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein. annotation in the mature form the amino-terminal cysteine has a free alpha-amino group Deisenhofer, J. Michel, H. Science 24519891463-1473 The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis. annotation X-ray crytallography of the reaction center, 2.3 angstroms Deisenhofer, J. Epp, O. Miki, K. Huber, R. Michel, H. submitted to the Brookhaven Protein Data Bank February1988 PDB1PRC annotation X-ray crystallography, 2.3 angstroms, residues 21-352 pufC the photosynthetic reaction center is a heterotetramer of H (see PIR:A22841), L (see PIR:A25102), M (see PIR:B25102), and cytochrome chains reduces photo-oxidized bacteriochlorophyll b photosynthesis photosynthetic reaction center cytochrome blocked amino end chromoprotein electron transfer heme heterotetramer iron lipoprotein membrane protein metalloprotein photosynthesis domain signal sequence 1-20 predicted product photosynthetic reaction center cytochrome 21-356 experimental binding-site sn-2,3-diacylglycerol (Cys) (covalent) 21 experimental modified-site fatty acylated amino end (Cys) (in mature form) 21 absent binding-site heme (Cys) (covalent) 107,110 experimental binding-site heme iron (His) (axial ligand) 111 experimental binding-site heme (Cys) (covalent) 152,155 experimental binding-site heme iron (His) (axial ligand) 156 experimental binding-site heme (Cys) (covalent) 264,267 experimental binding-site heme iron (His) (axial ligand) 268 experimental binding-site heme (Cys) (covalent) 325,328 experimental binding-site heme iron (His) (axial ligand) 329 experimental 356 complete MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPP ALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEA KYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETP THVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKER RPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMN YLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK
G49964 G49964 06-Oct-1994 19-Jul-1996 16-Jun-2000
photosynthetic reaction center cytochrome precursor Rhodocyclus gelatinosus Rhodocyclus gelatinosus Nagashima, K.V. Matsuura, K. Ohyama, S. Shimada, K. J. Biol. Chem. 26919942477-2484 Primary structure and transcription of genes encoding B870 and photosynthetic reaction center apoproteins from Rubrivivax gelatinosus. MUID94132007 G49964 DNA 1-366 GBD16822 NIDg464211 PIDNBAA04102.1 PIDg533363 sequence extracted from NCBI backbone (NCBIN:143423, NCBIP:143430) source designated as Rubrivivax gelatinosus pufC in this organism the photosynthetic reaction center is a heterotetramer of H, L (see PIR:E49964), M (see PIR:F49964), and cytochrome chains. re-reduces photo-oxidized bacteriochlorophyll b photosynthesis photosynthetic reaction center cytochrome blocked amino end chromoprotein electron transfer heme iron lipoprotein membrane protein metalloprotein photosynthesis domain signal sequence 1-22 predicted product photosynthetic reaction center cytochrome 23-366 predicted binding-site sn-2,3-diacylglycerol (Cys) (covalent) 23 predicted modified-site fatty acylated amino end (Cys) (in mature form) 23 predicted binding-site heme (Cys) (covalent) 107,110 predicted binding-site heme iron (His) (axial ligand) 111 predicted binding-site heme (Cys) (covalent) 151,154 predicted binding-site heme iron (His) (axial ligand) 155 predicted binding-site heme (Cys) (covalent) 249,252 predicted binding-site heme iron (His) (axial ligand) 253 predicted binding-site heme (Cys) (covalent) 309,312 predicted binding-site heme iron (His) (axial ligand) 313 predicted 366 complete MALAVRISTLTVAVTAAALLAGCERPPVDAVQRGYRGTGMQHIVNPRTLAEQIPTQQAPV ATPVADNSGPRANQVFQNVKVLGHLSVAEFTRQMAAINEWVAPTEGCNYCHTENLADDSK YQKVVSRRMLEMTQKVNTQWTHHVAATGVTCYTCHRGNPVPKEIWFTAVPQNKRADFIGN LDGQNQAAKVVGLTSLPYDPFTTFLKEETNVRVYGTTALPTGTSKADIKQAEKTYGLMMH FSGALGVNCTYCHNTNGFGSWDNAAPQRATAWYGIRMARDLNNNFMEGLTKTFPAHRLGP TGDVAKINCSTCHQGAYKPLYGAQMAKDYPGLKPAPAAAAASAVEAAPVDAAASAAPVAT VATAAK
S14271 S14271 21-Nov-1993 09-Aug-1996 17-Nov-2000
membrane-bound alcohol dehydrogenase (EC 1.1.-.-) cytochrome c precursor membrane-bound alcohol dehydrogenase 44K chain Acetobacter polyoxogenes Acetobacter polyoxogenes strain NBI1028 Tamaki, T. Fukaya, M. Takemura, H. Tayama, K. Okumura, H. Kawamura, Y. Nishiyama, M. Horinouchi, S. Beppu, T. Biochim. Biophys. Acta 10881991292-300 Cloning and sequencing of the gene cluster encoding two subunits of membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes. MUID91159482 S14271 DNA 1-468 GBD00635 NIDg216185 PIDNBAA00529.1 PIDg216187 strain NBI1028 heterodimer of 72K and 44K (cytochrome c) chains membrane-bound alcohol dehydrogenase cytochrome c cytochrome c6 homology alcohol metabolism blocked amino end chromoprotein electron transfer heme iron membrane protein metalloprotein oxidoreductase domain signal sequence 1-23 predicted product membrane-bound alcohol dehydrogenase cytochrome c chain 24-468 predicted domain cytochrome c6 homology 320-403 binding-site heme (Cys) (covalent) 45,48 predicted binding-site heme iron (His) (axial ligand) 49 predicted binding-site heme (Cys) (covalent) 193,196 predicted binding-site heme iron (His) (axial ligand) 197 predicted binding-site heme (Cys) (covalent) 330,333 predicted binding-site heme iron (His) (axial ligand) 334 predicted 468 complete MINRLKVTFSAAAFSLLAGTALAQTPDADSALVQKGAYVARLGDCVACHTALHGQSYAGG LEIKSPIGTIYSTNITPDPTYGIGRYTFAEFDEAVRHGIRKDGSTLYPAMPYPSFSRMTK EDMQALYAYFMHGVKPVAQPDKQPDISWPLSMRWPLGIWRMMFSPSPKDFTPAPGTDPEI ARGDYLVTGPGHCGACHTPRGFAMQEKALDAAGGPDFLSGGAPIDNWVAPSLRNDPVVGL GRWSEDDIYTFLKSGRIDHSAVFGGMGDVVAWSTQYFTDDDLHAIAKYLKSLPPVPPSQG NYTYDPSTANMLASGNTASVPGADTYVKECAICHRNDGGGVARMFPPLAGNPVVVTENPT SLVNVIAHGGVLPPSNWAPSAVAMPGYSKSLSAQQIADVVNFIRTSWGNKAPGTVTAADV TKLRDTGAPVSSSGWNSVSSGWSVFLPQPYGSGWTFAPQTHTGQDAAQ
B49340 B49340 07-Apr-1994 09-Aug-1996 17-Nov-2000
membrane-bound alcohol dehydrogenase (EC 1.1.-.-) cytochrome c precursor membrane-bound alcohol dehydrogenase 44K chain Acetobacter pasteurianus Acetobacter pasteurianus Takemura, H. Kondo, K. Horinouchi, S. Beppu, T. J. Bacteriol. 17519936857-6866 Induction by ethanol of alcohol dehydrogenase activity in Acetobacter pasteurianus. MUID94042848 B49340 preliminary DNA 1-472 GBD13893 NIDg517067 PIDNBAA02993.1 PIDg452587 strain NCI1380 heterodimer of 72K and 44K (cytochrome c) chains membrane-bound alcohol dehydrogenase cytochrome c cytochrome c6 homology alcohol metabolism blocked amino end chromoprotein electron transfer heme iron membrane protein metalloprotein oxidoreductase domain signal sequence 1-24 predicted product membrane-bound alcohol dehydrogenase cytochrome c chain 25-472 predicted domain cytochrome c6 homology 321-404 binding-site heme (Cys) (covalent) 46,49 predicted binding-site heme iron (His) (axial ligand) 50 predicted binding-site heme (Cys) (covalent) 194,197 predicted binding-site heme iron (His) (axial ligand) 198 predicted binding-site heme (Cys) (covalent) 331,334 predicted binding-site heme iron (His) (axial ligand) 335 predicted 472 complete MMMNRLKTALGAVAVGLLAGTSLAYAQNADEDLIKKGEYVARLGDCVACHTALNGQKYAG GLSIKTPIGTIYSTNITPDPTYGIGTYTFKEFDEAVRHGVRKDGATLYPGMPYPSFARMT QDDMKALYAYFMHGVQPIAEKNHPTDISWPMSMRWPLSIWRSVFAPAPKDFTPAPGTDAE TARGEYLITGPGHCGACHTPRGFGMQEKALDGAGGPDFLAGGGVIDNWIAPSLRNDPVLG LGRWSDEDLFLFLKSGRTDHSAAFGGMADVVGWSTQYFTDADLHAMVKYLKSLPPVPPAR GDYSYDASTAQMLDSNNFSGNAGAKTYVEQCAICHRNDGGGVARMFPPLAGNPVVVSDNP TSVAHIVVDGGVLPPTNWAPSAVAMPDYKNILSDQQIADVVNFIRSAWGNRAPANTTAAD IQKLRLDHTPLPTPGWANATEDSATWGLFMPQPYGAGWSFAPQTHAGVDEAQ
S00219 S00219 I52694 31-Dec-1988 22-Jul-1994 21-Jul-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) 11K protein precursor complex III 11K protein cytochrome bc1 complex 11K protein mitochondrial hinge protein human man Homo sapiens Ohta, S. Goto, K. Arai, H. Kagawa, Y. FEBS Lett. 2261987171-175 An extremely acidic amino-terminal presequence of the precursor for the human mitochondrial hinge protein. MUID88083627 S00219 mRNA 1-91 EMBLM36647 NIDg188564 PIDNAAA36317.1 PIDg188565 Liu, A.Y. Bradner, R.C. Cancer Res. 5319932460-2465 Elevated expression of the human mitochondrial hinge protein gene in cancer. MUID93265436 I52694 translated from GB/EMBL/DDBJ DNA 1-56 GBS61826 NIDg385936 PIDNAAD13930.1 PIDg4261630 GDBUQCRH GDB141852 22q13-22q13 ubiquinol--cytochrome-c reductase 11K protein ubiquinol--cytochrome-c reductase 11K protein homology mitochondrion oxidative phosphorylation oxidoreductase respiratory chain domain transit peptide (mitochondrion) 1-13 predicted product ubiquinol--cytochrome-c reductase 11K protein 14-91 predicted domain ubiquinol--cytochrome-c reductase 11K protein homology 23-91 disulfide-bonds 37-81,53-67 predicted 91 complete MGLEDEQKMLTESGDPEEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERDSSR SHTEEDCTEELFDFLHARDHCVAHKLFNNLK
CCBO11 A00119 18-Apr-1984 18-Apr-1984 07-May-1999
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) 11K protein cytochrome bc1 complex 11Kprotein mitochondrial hinge protein bovine cattle Bos primigenius taurus Wakabayashi, S. Takeda, H. Matsubara, H. Kim, C.H. King, T.E. J. Biochem. 9119822077-2085 Identity of the heme-not-containing protein in bovine heart cytochrome c-1 preparation with the protein mediating c-1-c complex formation-a protein with high glutamic acid content. MUID83007120 A00119 protein 1-78 Mukai, K. Miyazaki, T. Wakabayashi, S. Kuramitsu, S. Matsubara, H. J. Biochem. 9819851417-1425 Dissociation of bovine cytochrome c-1 subcomplex and the status of cysteine residues in the subunits. MUID86111722 annotation disulfide bonds This is one of the nonheme components of the cytochrome c1 complex, which is located in the inner membrane of the mitochondrion and functions as electron donor to cytochrome c in the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1. ubiquinol--cytochrome-c reductase 11K protein ubiquinol--cytochrome-c reductase 11K protein homology mitochondrial inner membrane mitochondrion oxidative phosphorylation oxidoreductase respiratory chain domain ubiquinol--cytochrome-c reductase 11K protein homology 10-78 disulfide-bonds 24-68,40-54 experimental 78 complete GDPKEEEEEEEELVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEEDCTEELLD FLHARDHCVAHKLFNSLK
S48690 S48690 S55873 S45021 10-Sep-1999 10-Sep-1999 10-Sep-1999
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) 11K protein potato potato Solanum tuberosum Braun, H.P. Jaensch, L. Kruft, V. Schmitz, U.K. FEBS Lett. 347199490-94 The 'Hinge' protein of cytochrome c reductase from potato lacks the acidic domain and has no cleavable presequence. MUID94283637 S48690 mRNA 1-69 EMBLX79273 NIDg488711 PIDNCAA55860.1 PIDg488712 S55873 protein 2-16,'X',18-19 nuclear ubiquinol--cytochrome-c reductase 11K protein ubiquinol--cytochrome-c reductase 11K protein homology mitochondrion oxidative phosphorylation oxidoreductase respiratory chain product ubiquinol--cytochrome-c reductase 2-69 experimental domain ubiquinol--cytochrome-c reductase 11K protein homology 3-69 disulfide-bonds 17-59,21-55,31-45 predicted 69 complete MSDEEVVDPKATLEVSCKPKCVRQLKEYQACTKRVEGDESGHKHCTGQYFDYWHCIDKCV AAKLFDHLK
RDBYUC S56288 A00120 S62244 S63838 25-Feb-1985 19-Oct-1995 21-Jul-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) 17K protein protein R014 protein YFR033c ubiquinol--cytochrome-c reductase chain VI yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Murakami, Y. Naitou, M. Hagiwara, H. Shibata, T. Ozawa, M. Sasanuma, S.I. Sasanuma, M. Tsuchiya, Y. Soeda, E. Yokoyama, K. Yamazaki, M. Tashiro, H. Eki, T. submitted to the EMBL Data Library May1995 Analysis of the nucleotide sequence of chromosome VI from Saccaromyces cerevisiae. S56288 DNA 1-147 EMBLD50617 NIDg836685 PIDNBAA09272.1 PIDg836788 GSPDBGN00006 MIPSYFR033c Van Loon, A.P.G.M. De Groot, R.J. De Haan, M. Dekker, A. Grivell, L.A. EMBO J. 319841039-1043 Amino acid sequence homology among fructose-1,6-bisphosphates. MUID84236098 A00120 DNA 1,'D',3-147 EMBLX00551 NIDg3597 PIDNCAA25220.1 PIDg3598 strain FL100 Murakami, Y. submitted to the EMBL Data Library December1994 S62244 DNA 1-147 EMBLD44602 NIDg893419 PIDNBAA08044.1 PIDg893428 Eki, T. Naitou, M. Hagiwara, H. Abe, M. Ozawa, M. Sasanuma, S.I. Sasanuma, M. Tsuchiya, Y. Shibata, T. Watanabe, K. Ono, A. Yamazaki, M.A. Tashiro, H. Hanaoka, F. Murakami, Y. Yeast 121996177-190 Fifteen open reading frames in a 30.8 kb region of the right arm of chromosome VI from Saccharomyces cerevisiae. MUID96287654 S63838 nucleic acid sequence not shown translation not shown DNA 1-147 EMBLD44602 NIDg893419 PIDNBAA08044.1 PIDg893428 the nucleotide sequence was submitted to the EMBL Data Library, July 1995 This highly acidic protein is one of the components of the ubiquinol--cytochrome-c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain and is located in the inner membrane. This protein may mediate the formation of the complex between cytochromes c and c1. SGDQCR6 SGDCR17 MIPSYFR033c SGDS0001929 MIPSYFR033c 6R nuclear ubiquinol--cytochrome-c reductase 17K protein ubiquinol--cytochrome-c reductase 11K protein homology electron transfer mitochondrial inner membrane mitochondrion oxidative phosphorylation oxidoreductase respiratory chain domain ubiquinol--cytochrome-c reductase 11K protein homology 71-147 disulfide-bonds 101-123 predicted 147 complete MGMLELVGEYWEQLKITVVPVVAAAEDDDNEQHEEKAAEGEEKEEENGDEDEDEDEDEDD DDDDDEDEEEEEEVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHK EDCVEEFFHLQHYLDTATAPRLFDKLK
A34660 A46063 A34660 A24011 S00003 S14162 S65406 31-Mar-1991 22-Apr-1995 05-May-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein precursor [validated] cytochrome bc1 complex chain 9 cytochrome bc1 complex iron-sulfur protein Rieske iron-sulfur protein ubiquinol--cytochrome-c reductase 8K protein ubiquinol--cytochrome-c reductase chain 5 ubiquinol--cytochrome-c reductase chain 9 bovine cattle Bos primigenius taurus Brandt, U. Yu, L. Yu, C.A. Trumpower, B.L. J. Biol. Chem. 26819938387-8390 The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex. MUID93231976 A46063 mRNA 1-274 GBS58789 NIDg299557 PIDNAAB26197.1 PIDg299558 heart sequence extracted from NCBI backbone (NCBIN:129525, NCBIP:129529) Usui, S. Yu, L. Yu, C.A. Biochem. Biophys. Res. Commun. 1671990575-579 Cloning and sequencing of a cDNA encoding the Rieske iron-sulfur protein of bovine heart mitochondrial ubiquinol-cytochrome c reductase. MUID90211231 A34660 mRNA 1-8,'RHSR',13,'SYRPRPA',21,'WR',25-28,'WYSRSSK',39-60,'AA',64-274 GBM34336 NIDg163043 PIDNAAA30515.1 PIDg163044 the authors translated the codon AAG for residue 34 as Arg this sequence has been revised in reference A46063 Borchart, U. Machleidt, W. Schagger, H. Link, T.A. von Jagow, G. FEBS Lett. 1911985125-130 Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of beef heart ubiquinol:cytochrome c reductase. MUID86030649 A24011 protein 1-78 heart 53-Glu reacts rapidly and specifically with dicyclohexyl carbodiimide Schaegger, H. Borchart, U. Machleidt, W. Link, T.A. von Jagow, G. FEBS Lett. 2191987161-168 Isolation and amino acid sequence of the 'Rieske' iron sulfur protein of beef heart ubiquinol:cytochrome c reductase. MUID87247298 S00003 protein 79-149,'A',151-268,'G',270-274 Cocco, T. Lorusso, M. Sardanelli, A.M. Minuto, M. Ronchi, S. Tedeschi, G. Papa, S. Eur. J. Biochem. 1951991731-734 Structural and functional characteristics of polypeptide subunits of the bovine heart ubiquinol - cytochrome-c reductase complex. MUID91153313 S14162 protein 79-90;142-149,'A',151-162 Link, T.A. Saynovits, M. Assmann, C. Iwata, S. Ohnishi, T. von Jagow, G. Eur. J. Biochem. 237199671-75 Isolation, characterisation and crystallisation of a water-soluble fragment of the Rieske iron-sulfur protein of bovine heart mitochondrial bc(1) complex. MUID96203910 S65406 protein 146-150 Iwata, S. Saynovits, M. Link, T.A. Michel, H. submitted to the Brookhaven Protein Data Bank February1996 PDB1RIE annotation X-ray crystallography, 1.5 angstroms Iwata, S. Lee, J.W. Okada, K. Lee, J.K. Iwata, M. Rasmussen, B. Link, T.A. Ramaswamy, S. Jap, B.K. Science 281199864-71 Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. MUID98316377 annotation X-ray crystallography, 4.0 angstroms After cleavage the transit peptide remains bound in the complex as ubiquinol--cytochrome-c reductase chain 9 (8K protein). nuclear the ubiquinol--cytochrome-c reductase complex consists of two subunits with 10 chains each and two chains of chain 9 (iron-sulfur protein) shared between the two subunits the transmembrane complex includes cytochrome b (see PIR:CBBO), cytochrome c1 (see PIR:CCBO1), Rieske iron-sulfur protein, and other accessory proteins (see PIR:CCBO11, PIR:CCBO17, PIR:A24864, PIR:ZPBOC1, and PIR:ZPBOC2) ubiquinol--cytochrome-c reductase iron-sulfur protein Rieske [2Fe-2S] homology 2Fe-2S acetylated amino end electron transfer membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain Rieske iron-sulfur protein domain transit peptide (mitochondrion) 1-78 experimental product ubiquinol--cytochrome-c reductase chain 9 1-78 experimental product ubiquinol--cytochrome-c reductase chain 5 79-274 experimental domain Rieske [2Fe-2S] homology 207-254 modified-site acetylated amino end (Met) 1 experimental binding-site 2Fe-2S cluster (Cys, His, Cys, His) (covalent) 217,219,236,239 experimental disulfide-bonds 222-238 experimental active-site His 239 predicted 274 complete MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAA GRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTAT TTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRT KKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHG SHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG
RDNCUF A24612 28-Dec-1987 28-Dec-1987 20-Apr-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein [similarity] Neurospora crassa Neurospora crassa Harnisch, U. Weiss, H. Sebald, W. Eur. J. Biochem. 149198595-99 The primary structure of the iron-sulfur subunit of ubiquinol-cytochrome c reductase from Neurospora, determined by cDNA and gene sequencing. MUID85203899 A24612 DNA 1-231 GBX02472 NIDg3001 PIDNCAA26308.1 PIDg3002 92/1; 121/3; 172/1 ubiquinol--cytochrome-c reductase iron-sulfur protein Rieske [2Fe-2S] homology 2Fe-2S electron transfer membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain Rieske iron-sulfur protein domain Rieske [2Fe-2S] homology 164-211 binding-site 2Fe-2S cluster (Cys, His, Cys, His) (covalent) 174,176,193,196 predicted disulfide-bonds 179-195 predicted active-site His 196 predicted 231 complete MAPVSIVSRAAMRAAAAPARAVRALTTSTALQGSSSSTFESPFKGESKAAKVPDFGKYMS KAPPSTNMLFSYFMVGTMGAITAAGAKSTIQEFLKNMSASADVLAMAKVEVDLNAIPEGK NVIIKWRGKPVFIRHRTPAEIEEANKVNVATLRDPETDADRVKKPEWLVMLGVCTHLGCV PIGEAGDYGGWFCPCHGSHYDISGRIRKGPAPLNLEIPLYEFPEEGKLVIG
RDQFBR S12256 A38813 31-Dec-1991 31-Dec-1991 20-Apr-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein [validated] cytochrome bc1 complex iron-sulfur protein Rhodospirillum rubrum Rhodospirillum rubrum Majewski, C. Trebst, A. Mol. Gen. Genet. 2241990373-382 The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc(1)-complex. MUID91094774 S12256 DNA 1-183 EMBLX55387 NIDg46382 PIDNCAA39058.1 PIDg46384 A38813 protein 2-35 petA ubiquinol--cytochrome-c reductase iron-sulfur protein Rieske [2Fe-2S] homology 2Fe-2S electron transfer membrane-associated complex metalloprotein oxidoreductase respiratory chain Rieske iron-sulfur protein product ubiquinol--cytochrome-c reductase iron-sulfur protein 2-183 experimental domain Rieske [2Fe-2S] homology 111-163 binding-site 2Fe-2S cluster (Cys, His, Cys, His) (covalent) 121,123,145,148 predicted disulfide-bonds 126-147 predicted active-site His 148 predicted 183 complete MAEAEHTASTPGGESSRRDFLIYGTTAVGAVGVALAVWPFIDFMNPAADTLALASTEVDV SAIAEGQAITVTWRGKPVFVRHRTQKEIVVARAVDPASLRDPQTDEARVQQAQWLVMVGV CTHLGCIPLGQKAGDPKGDFDGWFCPCHGSHYDSAGRIRKGPAPLNLPVPPYAFTDDTTV LIG
A29336 A29336 A25405 D25405 S22633 S21003 31-Dec-1988 22-Jul-1994 16-Jul-1999
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein cytochrome b-c1 complex Rieske iron-sulfur protein Rhodobacter capsulatus Rhodobacter capsulatus Davidson, E. Daldal, F. J. Mol. Biol. 195198713-24 Primary structure of the bc-1 complex of Rhodopseudomonas capsulata. Nucleotide sequence of the pet operon encoding the Rieske, cytochrome b, and cytochrome c-1 apoproteins. MUID88011223 A29336 DNA 1-191 EMBLX05630 NIDg46093 PIDNCAA29116.1 PIDg581499 Gabellini, N. Sebald, W. Eur. J. Biochem. 1541986569-579 Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c-1. MUID86136096 source is designated as Rhodopseudomonas sphaeroides A25405 DNA 1-47,'S',49-113,'S',115,'A',117-191 EMBLX03476 NIDg46007 PIDNCAA27194.1 PIDg581491 D25405 protein 49-67 Tokito, M.K. Daldal, F. Mol. Microbiol. 619921645-1654 petR, located upstream of the fbcFBC operon encoding the cytochrome bc(1) complex, is homologous to bacterial response regulators and necessary for photosynthetic and respiratory growth of Rhodobacter capsulatus. MUID92356828 S22633 DNA 1-23 EMBLZ12113 NIDg49287 PIDNCAA78099.1 PIDg581500 the authors translated the codon AAC for residue 7 as Gln fbcF petA GTG ubiquinol--cytochrome-c reductase iron-sulfur protein Rieske [2Fe-2S] homology 2Fe-2S electron transfer membrane-associated complex metalloprotein oxidoreductase respiratory chain Rieske iron-sulfur protein domain Rieske [2Fe-2S] homology 123-171 binding-site 2Fe-2S cluster (Cys, His, Cys, His) (covalent) 133,135,153,156 predicted disulfide-bonds 138-155 predicted active-site His 156 predicted 191 complete MSHAEDNAGTRRDFLYHATAATGVVVTGAAVWPLINQMNASADVKAMASIFVDVSAVEVG TQLTVKWRGKPVFIRRRDEKDIELARSVPLGALRDTSAENANKPGAEATDENRTLPAFDG TNTGEWLVMLGVCTHLGCVPMGDKSGDFGGWFCPCHGSHYDSAGRIRKGPAPRNLDIPVA AFVDETTIKLG
S13868 S13868 C34591 31-Dec-1988 22-Jul-1994 20-Apr-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) Rieske iron-sulfur protein [validated] Rhodobacter sphaeroides Rhodobacter sphaeroides Yun, C.H. Beci, R. Crofts, A.R. Kaplan, S. Gennis, R.B. Eur. J. Biochem. 1941990399-411 Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc(1) complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant. MUID91099313 S13868 DNA 1-187 EMBLX56157 NIDg46425 PIDNCAA39623.1 PIDg581533 Andrews, K.M. Crofts, A.R. Gennis, R.B. Biochemistry 2919902645-2651 Large-scale purification and characterization of a highly active four-subunit cytochrome bc-1 complex from Rhodobacter sphaeroides. MUID90268011 C34591 protein 2-6,'X',8-10,'XX',13-14,'X',16-19 fbcF GTG ubiquinol--cytochrome-c reductase iron-sulfur protein Rieske [2Fe-2S] homology 2Fe-2S electron transfer membrane-associated complex metalloprotein oxidoreductase photosynthesis respiratory chain Rieske iron-sulfur protein product ubiquinol--cytochrome-c reductase iron-sulfur protein 2-187 experimental domain Rieske [2Fe-2S] homology 119-167 binding-site 2Fe-2S cluster (Cys, His, Cys, His) (covalent) 129,131,149,152 predicted disulfide-bonds 134-151 predicted active-site His 152 predicted 187 complete MSNAEDHAGTRRDFLYYATAGAGAVATGAAVWPLINQMNPSADVQALASIFVDVSSVEPG VQLTVKFLGKPIFIRRRTEADIELGRSVQLGQLVDTNARNANIDAGAEATDQNRTLDEAG EWLVMWGVCTHLGCVPIGGVSGDFGGWFCPCHGSHYDSAGRIRKGPAPENLPIPLAKFID ETTIQLG
RDBYUN S69584 A00121 28-Aug-1985 13-Mar-1997 05-Nov-1999
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) 14K protein complex III 14K protein cytochrome b-c1 complex 14K protein protein YDR529c yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Dietrich, F.S. submitted to the EMBL Data Library August1995 The sequence of S. cerevisiae cosmids 8166, 9787, 9717, and lambda 3073. S69584 DNA 1-127 EMBLU33057 NIDg927764 PIDNAAB64968.1 PIDg927796 GSPDBGN00004 MIPSYDR529c De Haan, M. Van Loon, A.P.G.M. Kreike, J. Vaessen, R.T.M.J. Grivell, L.A. Eur. J. Biochem. 1381984169-177 The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit. MUID84108379 A00121 DNA 1-91,'Q',93-127 EMBLX00256 NIDg3600 PIDNCAA25064.1 PIDg3601 strain FL100 SGDQCR7 SGDCRO1 SGDUCR7 SGDCOR4 MIPSYDR529c SGDS0002937 MIPSYDR529c 4R nuclear ubiquinol--cytochrome-c reductase 14K protein electron transfer membrane protein membrane-associated complex mitochondrial inner membrane mitochondrion oxidative phosphorylation oxidoreductase respiratory chain 127 complete MPQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTAL RRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDEL DNIEVSK
UYBO A00122 A61151 S14163 28-May-1986 28-May-1986 26-Feb-1999
ubiquinone-binding protein QP-C 14K protein ubiquinol-cytochrome c reductase chain VI bovine cattle Bos primigenius taurus Wakabayashi, S. Takao, T. Shimonishi, Y. Kuramitsu, S. Matsubara, H. Wang, T. Zhang, Z. King, T.E. J. Biol. Chem. 2601985337-343 Complete amino acid sequence of the ubiquinone binding protein (QP-C), a protein similar to the 14,000-dalton subunit of the yeast ubiquinol-cytochrome c reductase complex. MUID85080099 A00122 protein 1-110 Usui, S. Yu, L. Harmon, J. Yu, C.A. Arch. Biochem. Biophys. 2891991109-117 Immunochemical study of subunit VI (M-r 13,400) of mitochondrial ubiquinol-cytochrome c reductase. MUID91378519 A61151 protein 22-26;32-46;74-80 Cocco, T. Lorusso, M. Sardanelli, A.M. Minuto, M. Ronchi, S. Tedeschi, G. Papa, S. Eur. J. Biochem. 1951991731-734 Structural and functional characteristics of polypeptide subunits of the bovine heart ubiquinol - cytochrome-c reductase complex. MUID91153313 S14163 protein 1-32 This is one of the specific mitochondrial proteins that bind to ubiquinone and stabilize the ubisemiquinone radicals. ubiquinol--cytochrome-c reductase 14K protein acetylated amino end electron transfer mitochondrion oxidative phosphorylation respiratory chain modified-site acetylated amino end (Ala) 1 experimental 110 complete AGRPAVSASSRWLEGIRKWYYNAAGFNKLGLMRDDTIHENDDVKEAIRRLPENLYDDRVF RIKRALDLSMRQQILPKEQWTKYEEDKSYLEPYLKEVIRERKEREEWAKK
CCBO17 A00123 18-Apr-1984 18-Apr-1984 14-Sep-1994
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) 7K protein bovine cattle Bos primigenius taurus Schagger, H. von Jagow, G. Borchart, U. Machleidt, W. Hoppe-Seyler's Z. Physiol. Chem. 3641983307-311 Amino-acid sequence of the smallest protein of the cytochrome c-1 subcomplex from beef heart mitochondria. MUID83236204 A00123 protein 1-62 This is one of the nonheme components of the cytochrome c1 complex, which is located in the inner membrane of the mitochondrion and functions as electron donor to cytochrome c in the mitochondrial respiratory chain. cytochrome c1 nonheme 7K protein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain 62 complete VAPTLTARLYSLLFRRTSTFALTIVVGALFFERAFDQGADAIYEHINEGKLWKHIKHKYE NK
A38325 A38325 B38325 S64497 S64501 10-Sep-1999 10-Sep-1999 21-Jul-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) chain 9 protein G7164 protein YGR183c yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Phillips, J.D. Schmitt, M.E. Brown, T.A. Beckmann, J.D. Trumpower, B.L. J. Biol. Chem. 265199020813-20821 Isolation and characterization of QCR9, a nuclear gene encoding the 7.3-kDa subunit 9 of the Saccharomyces cerevisiae ubiquinol-cytochrome c oxidoreductase complex. An intron-containing gene with a conserved sequence occurring in the intron of COX4. MUID91065877 A38325 DNA 1-66 GBM59797 GBM37790 NIDg172311 PIDNAAA63575.1 PIDg172312 B38325 protein 2-11 Hebling, U. Hofmann, B. Delius, H. submitted to the Protein Sequence Database May1996 S64497 DNA 1-66 EMBLZ72968 NIDg1323323 PIDNCAA97209.1 PIDg1323324 GSPDBGN00007 MIPSYGR183c strain S288C Arroyo, J. Garcia-Gonzalez, M. Garcia-Saez, M.I. Sanchez-Perez, M. Nombela, C. submitted to the Protein Sequence Database May1996 S64501 DNA 1-66 EMBLZ72968 NIDg1323323 PIDNCAA97209.1 PIDg1323324 GSPDBGN00007 MIPSYGR183c strain S288C SGDQCR9 SGDUCR9 MIPSYGR183c SGDS0003415 MIPSYGR183c 7R nuclear 1/3 cytochrome c1 nonheme 7K protein membrane-associated complex mitochondrion oxidative phosphorylation oxidoreductase respiratory chain product ubiquinol--cytochrome-c reductase chain 9 2-66 experimental 66 complete MSFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAAGD GDDDDE
CCDV3 A24799 A00124 D32427 24-Apr-1984 17-Feb-1994 03-Mar-2000
cytochrome c3 precursor Desulfovibrio vulgaris (strain Hildenborough) Desulfovibrio vulgaris Voordouw, G. Brenner, S. Eur. J. Biochem. 1591986347-351 Cloning and sequencing of the gene encoding cytochrome c3 from Desulfovibrio vulgaris (Hildenborough). MUID87004646 A24799 DNA 1-129 GBX04304 NIDg40820 PIDNCAA27847.1 PIDg40821 Trousil, E.B. Campbell, L.L. J. Biol. Chem. 2491974386-393 Amino acid sequence of cytochrome c-3 from Desulfovibrio vulgaris. MUID74070664 A00124 protein 23-129 strain Hildenborough, NCIB 8303 Loutfi, M. Guerlesquin, F. Bianco, P. Haladjian, J. Bruschi, M. Biochem. Biophys. Res. Commun. 1591989670-676 Comparative studies of polyhemic cytochromes c isolated from Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio desulfuricans (Norway). MUID89193654 D32427 protein 23-44 cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein sulfate respiration domain signal sequence 1-22 predicted product cytochrome c3 23-129 experimental domain cytochrome c3 homology 42-128 binding-site heme iron (His) (axial ligands) 44,56 predicted binding-site heme iron (His) (axial ligands) 47,105 predicted binding-site heme (Cys) (covalent) 52,55 predicted binding-site heme iron (His) (axial ligands) 57,74 predicted binding-site heme (Cys) (covalent) 68,73 predicted binding-site heme iron (His) (axial ligands) 92,128 predicted binding-site heme (Cys) (covalent) 101,104 predicted binding-site heme (Cys) (covalent) 122,127 predicted 129 complete MRKLFFCGVLALAVAFALPVVAAPKAPADGLKMEATKQPVVFNHSTHKSVKCGDCHHPVN GKEDYRKCGTAGCHDSMDKKDKSAKGYYHVMHDKNTKFKSCVGCHVEVAGADAAKKKDLT GCKKSKCHE
CCDV3M S33874 A00125 31-Oct-1980 10-Oct-1997 15-Sep-2000
cytochrome c3 precursor [validated] Desulfovibrio vulgaris (strain Miyazaki) Desulfovibrio vulgaris Kitamura, M. Ozawa, K. Kojima, S. Kumagai, I. Akutsu, H. Miura, K. Protein Seq. Data Anal. 51993193-196 The primary structure of pre-cytochrome c(3) from Desulfovibrio vulgaris (Miyazaki F) as determined by nucleotide sequencing of its gene and partial amino acid sequencing. S33874 DNA 1-130 DDBJD31702 NIDg496361 PIDNBAA06511.1 PIDg496362 Shinkai, W. Hase, T. Yagi, T. Matsubara, H. J. Biochem. 8719801747-1756 Amino acid sequence of cytochrome c-3 from Desulfovibrio vulgaris, Miyazaki. MUID80249474 A00125 protein 24-64,'N',66-130 Higuchi, Y. Kusunoki, M. Matsuura, Y. Yasuoka, N. Kakudo, M. J. Mol. Biol. 1721984109-139 Refined structure of cytochrome c-3 at 1.8 angstrom resolution. MUID84114880 annotation X-ray crystallography, 1.8 angstroms Higuchi, Y. Kusunoki, M. Matsuura, Y. Yasuoka, N. Kakudo, M. submitted to the Brookhaven Protein Data Bank November1983 PDB2CDV annotation X-ray crystallography, 1.8 angstroms, residues 24-64,'N',66-130 accepts electrons from cytochrome-c3 hydrogenase (EC 1.12.2.1) and transfers them to ferredoxin sulfate respiration cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein sulfate respiration product cytochrome c3 24-130 experimental domain cytochrome c3 homology 43-129 binding-site heme iron (His) (axial ligands) 45,57 experimental binding-site heme iron (His) (axial ligands) 48,106 experimental binding-site heme (Cys) (covalent) 53,56 experimental binding-site heme iron (His) (axial ligands) 58,75 experimental binding-site heme (Cys) (covalent) 69,74 experimental binding-site heme iron (His) (axial ligands) 93,129 experimental binding-site heme (Cys) (covalent) 102,105 experimental binding-site heme (Cys) (covalent) 123,128 experimental 130 complete MKKMFLTGVLALAVAIAMPALAAAPKAPADGLKMDKTKQPVVFNHSTHKAVKCGDCHHPV NGKEDYQKCATAGCHDNMDKKDKSAKGYYHAMHDKGTKFKSCVGCHLETAGADAAKKKEL TGCKGSKCHS
CCDV3G A00126 07-May-1981 07-May-1981 31-Mar-2000
cytochrome c3 Desulfovibrio gigas Desulfovibrio gigas Ambler, R.P. Bruschi, M. Le Gall, J. FEBS Lett. 51969115-117 The structure of cytochrome c'-3 from Desulfovibrio gigas (NCIB 9332). A00126 protein 1-111 NCIB 9332 one of the four residues at positions 34, 35, 39, and 42 is amidated cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein sulfate respiration domain cytochrome c3 homology 23-109 binding-site heme iron (His) (axial ligands) 25,37 predicted binding-site heme iron (His) (axial ligands) 28,86 predicted binding-site heme (Cys) (covalent) 33,36 predicted binding-site heme iron (His) (axial ligands) 38,54 predicted binding-site heme (Cys) (covalent) 48,53 predicted binding-site heme iron (His) (axial ligands) 72,109 predicted binding-site heme (Cys) (covalent) 82,85 predicted binding-site heme (Cys) (covalent) 103,108 predicted 111 complete tentative VDVPADGAKIDFIAGGEKNL(V.V.F)NH(S.T.H)KDVKCBBCHHZPGBKQYAGCTTDG CHNILDKADKSVNSWYKVVHDAKGGAKPTCISCHKDKAGDDKELKKKLTGCKGSACHPS
CCDV3D A00127 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c3 Desulfovibrio desulfuricans Desulfovibrio desulfuricans Ambler, R.P. Bruschi, M. Le Gall, J. FEBS Lett. 181971347-350 The amino acid sequence of cytochrome c-3 from Desulfovibrio desulfuricans (strain El Agheila Z, NCIB 8380). A00127 protein 1-102 strain El Agheila Z, NCIB 8380 cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein sulfate respiration domain cytochrome c3 homology 24-99 binding-site heme iron (His) (axial ligands) 26,38 predicted binding-site heme iron (His) (axial ligands) 29,85 predicted binding-site heme (Cys) (covalent) 34,37 predicted binding-site heme iron (His) (axial ligands) 39,56 predicted binding-site heme (Cys) (covalent) 50,55 predicted binding-site heme iron (His) (axial ligands) 73,99 predicted binding-site heme (Cys) (covalent) 81,84 predicted binding-site heme (Cys) (covalent) 95,98 predicted 102 complete VDAPADMVIKAPAGAKVTKAPVAFSHKGHASMDCKTCHHKWDGAGAIQPCQASGCHANTE SKKGDDSFYMAFHERKSEKSCVGCHKSMKKGPTKCTECHPKN
CCDV3S A00128 A38898 31-Aug-1980 31-Aug-1980 31-Mar-2000
cytochrome c3 Desulfovibrio salexigens Desulfovibrio salexigens Ambler, R.P. Bruschi, M. Le Gall, J. unpublished results, cited by Haser, R., Pierrot, M., Frey, M., Payan, F., Astier, J.P., Bruschi, M., and Le Gall, J., Nature 282, 806-810 1979 Structure and sequence of the multihaem cytochrome c-3. A00128 protein 1-106 Ambler, R.P. Bruschi, M. Le Gall, J. unpublished results, cited by Ambler, R.P., Syst. Zool. 22, 554-565 1973 Bacterial cytochromes C and molecular evolution. A38898 protein 1-4,'G',6-106 cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein sulfate respiration domain cytochrome c3 homology 24-102 binding-site heme iron (His) (axial ligands) 26,38 predicted binding-site heme iron (His) (axial ligands) 29,86 predicted binding-site heme (Cys) (covalent) 34,37 predicted binding-site heme iron (His) (axial ligands) 39,56 predicted binding-site heme (Cys) (covalent) 50,55 predicted binding-site heme iron (His) (axial ligands) 75,102 predicted binding-site heme (Cys) (covalent) 82,85 predicted binding-site heme (Cys) (covalent) 98,101 predicted 106 complete tentative VDAPADMVLKAPAGAKMTKAPVDFSHKGHAALDCTKCHHKWDGKAEVKKCSAEGCHV(B, T,S)K(K,G,K,K,S,T,P,K)FYSAFHSKSDISCVGCHKALKKATGPTKCGDCHPKKK
CCDV3N A00129 A32427 31-Aug-1980 17-Oct-1997 15-Sep-2000
cytochrome c3, tetraheme [validated] cytochrome c3 M(r) 13,000 Desulfovibrio desulfuricans (strain Norway 4) Desulfovibrio desulfuricans Bruschi, M. Biochim. Biophys. Acta 6711981219-226 The primary structure of the tetrahaem cytochrome C-3 from Desulfovibrio desulfuricans (strain Norway 4). A00129 protein 1-85,'S',87-96,'ALK',100-118 this sequence has been corrected in reference S43400 Bruschi, M. Leroy, G. Guerlesquin, F. Bonicel, J. Biochim. Biophys. Acta 12051994123-131 Amino-acid sequence of the cytochrome c(3) (M(r) 26000) from Desulfovibrio desulfuricans Norway and a comparison with those of the other polyhemic cytochromes from Desulfovibrio. MUID94191018 annotation sequence correction peptides for sequence A00129 were redetermined and corrected Loutfi, M. Guerlesquin, F. Bianco, P. Haladjian, J. Bruschi, M. Biochem. Biophys. Res. Commun. 1591989670-676 Comparative studies of polyhemic cytochromes c isolated from Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio desulfuricans (Norway). MUID89193654 A32427 protein 1-36 Czjzek, M. Payan, F. Guerlesquin, F. Bruschi, M. Haser, R. J. Mol. Biol. 2431994653-667 Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 Angstroms resolution. MUID95055708 annotation X-ray crystallography, 1.7 angstroms the corrected sequence is shown Czjzek, M. Payan, F. Haser, R. submitted to the Brookhaven Protein Data Bank July1994 PDB2CY3 annotation X-ray crystallography, 1.7 angstroms, residues 1-118 Pierrot, M. Haser, R. Frey, M. Payan, F. Astier, J.P. J. Biol. Chem. 257198214341-14348 Crystal structure and electron transfer properties of cytochrome c-3. MUID83056976 annotation X-ray crystallography, 2.5 angstroms Haser, R. Pierrot, M. Frey, M. Payan, F. Astier, J.P. Bruschi, M. Le Gall, J. Nature 2821979806-810 Structure and sequence of the multihaem cytochrome c-3. MUID80078137 annotation X-ray crystallography, 2.5 angstroms monomer accepts electrons from cytochrome-c3 hydrogenase (EC 1.12.2.1) and transfers them to ferredoxin II sulfate respiration this protein is also active in the phosphoroclastic reaction cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein monomer phosphoroclastic reaction sulfate respiration domain cytochrome c3 homology 34-115 binding-site heme iron (His) (axial ligands) 36,48 experimental binding-site heme iron (His) (axial ligands) 39,96 experimental binding-site heme (Cys) (covalent) 44,47 experimental binding-site heme iron (His) (axial ligands) 49,67 experimental binding-site heme (Cys) (covalent) 61,66 experimental binding-site heme iron (His) (axial ligands) 89,115 experimental binding-site heme (Cys) (covalent) 92,95 experimental binding-site heme (Cys) (covalent) 111,114 experimental 118 complete ADAPGDDYVISAPEGMKAKPKGDKPGALQKTVPFPHTKHATVECVQCHHTLEADGGAVKK CTTSGCHDSLEFRDKANAKDIKLVENAFHTQCIDCHKALKKDKKPTGPTACGKCHTTN
S43400 S43400 B32427 20-Oct-1994 03-Aug-1995 15-Sep-2000
cytochrome c3, octaheme [validated] cytochrome c3 M(r) 26,000 Desulfovibrio desulfuricans (strain Norway 4) Desulfovibrio desulfuricans strain Norway Bruschi, M. Leroy, G. Guerlesquin, F. Bonicel, J. Biochim. Biophys. Acta 12051994123-131 Amino-acid sequence of the cytochrome c(3) (M(r) 26000) from Desulfovibrio desulfuricans Norway and a comparison with those of the other polyhemic cytochromes from Desulfovibrio. MUID94191018 S43400 protein 1-111 strain Norway, NCIB 8310 Loutfi, M. Guerlesquin, F. Bianco, P. Haladjian, J. Bruschi, M. Biochem. Biophys. Res. Commun. 1591989670-676 Comparative studies of polyhemic cytochromes c isolated from Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio desulfuricans (Norway). MUID89193654 B32427 protein 1-30 strain Norway 4, NCIB 8310 Czjzek, M. Haser, R. submitted to the Brookhaven Protein Data Bank January1996 PDB1CZJ annotation X-ray crystallography, 2.16 angstroms, residues 2-111 homodimer cytochrome c3 cytochrome c3 homology chromoprotein heme homodimer iron metalloprotein sulfate respiration domain cytochrome c3 homology 28-109 binding-site heme iron (His) (axial ligands) 30,42 experimental binding-site heme iron (His) (axial ligands) 33,90 experimental binding-site heme (Cys) (covalent) 38,41 experimental binding-site heme iron (His) (axial ligands) 43,60 experimental binding-site heme (Cys) (covalent) 54,59 experimental binding-site heme iron (His) (axial ligands) 77,109 experimental binding-site heme (Cys) (covalent) 86,89 experimental binding-site heme (Cys) (covalent) 105,108 experimental 111 complete ETFEIPESVTMSPKQFEGYTPKKGDVTFNHASHMDIACQQCHHTVPDTYTIESCMTEGCH DNIKERTEISSVYRTFHTTKDSEKSCVGCHRELKRQGPSDAPLACNSCHVQ
CCDS7 A00130 13-Jul-1981 13-Jul-1981 03-Mar-2000
cytochrome c7 (c551.5) Desulfuromonas acetoxidans Desulfuromonas acetoxidans Ambler, R.P. FEBS Lett. 181971351-353 The amino acid sequence of cytochrome c551.5 (cytochrome c-7) from the green photosynthetic bacterium Chloropseudomonas ethylica. A00130 protein 1-68 Olson, J.M. Int. J. Syst. Bacteriol. 281978128-129 annotation taxonomy This c3-type cytochrome, although homologous with cytochrome c3 and similar in redox potential, has only three hemes and a shorter polypeptide chain. This cytochrome was isolated from a culture originally called Chloropseudomonas ethylica, which has been found to be a mixture of Prosthecochloris aestuarii, a photosynthetic green sulfur bacterium, and Desulfuromonas acetoxidans, a colorless motile heterotroph. cytochrome c3 cytochrome c3 homology chromoprotein electron transfer heme iron metalloprotein domain cytochrome c3 homology 15-66 binding-site heme iron (His) (axial ligands) 17,30 predicted binding-site heme iron (His) (axial ligands) 20,53 predicted binding-site heme (Cys) (covalent) 26,29 predicted binding-site heme iron (His) (axial ligands) 45,66 predicted binding-site heme (Cys) (covalent) 49,52 predicted binding-site heme (Cys) (covalent) 62,65 predicted 68 complete ADVVTYENKKGNVTFDHKAHAEKLGCDACHEGTPAKIAIDKKSAHKDACKTCHKSNNGPT KCGGCHIK
A37129 A37129 B69597 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome c550 cccA Bacillus subtilis Bacillus subtilis von Wachenfeldt, C. Hederstedt, L. J. Biol. Chem. 265199013939-13948 Bacillus subtilis 13-kilodalton cytochrome c-550 encoded by cccA consists of a membrane-anchor and a heme domain. MUID90338015 A37129 preliminary DNA 1-120 GBJ05569 NIDg142651 PIDNAAA22294.1 PIDg142652 Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 B69597 nucleic acid sequence not shown translation not shown DNA 1-120 GBZ99116 GBAL009126 NIDg2634723 PIDNCAB14449.1 PIDg2634952 strain 168 cccA Bacillus cytochrome c550 cccA cytochrome c6 homology chromoprotein electron transfer heme iron metalloprotein transmembrane protein domain cytochrome c6 homology 50-116 binding-site heme (Cys) (covalent) 60,63 predicted binding-site heme iron (His, Met) (axial ligands) 64,99 predicted 120 complete MKWNPLIPFLLIAVLGIGLTFFLSVKGLDDSREIASGGESKSAEKKDANASPEEIYKANC IACHGENYEGVSGPSLKGVGDKKDVAEIKTKIEKGGNGMPSGLVPADKLDDMAEWVSKIK
S43726 S43726 S77898 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome c551 precursor thermophilic bacterium PS-3 thermophilic bacterium PS-3 Fujiwara, Y. Oka, M. Hamamoto, T. Sone, N. Biochim. Biophys. Acta 11441993213-219 Cytochrome c-551 of the thermophilic bacterium PS3, DNA sequence and analysis of the mature cytochrome. MUID93379042 S43726 DNA 1-111 EMBLX63125 NIDg402788 PIDNCAA44835.1 PIDg402789 S77898 protein 48-50,'X',52-53,'X',55-67;75-82;91-97,'Q',99-108,110-111 Bacillus cytochrome c550 cccA cytochrome c6 homology blocked amino end chromoprotein electron transfer heme iron metalloprotein domain signal sequence 1-18 predicted product cytochrome c551 19-111 predicted domain cytochrome c6 homology 41-107 binding-site heme (Cys) (covalent) 51,54 predicted binding-site heme iron (His, Met) (axial ligands) 55,90 predicted 111 complete MKWKLAAMFLGVSLALAACGGGGDNAGEKNGGSNGGGDTAAAAEQIFKQNCASCHGQDLS GGVGPNLQKVGSKYSKDEIKNIIANGRGAMPAGIIKGEDADKVAEWLAAKK
A39193 A39193 B39193 A40605 C32427 18-Jun-1999 18-Jun-1999 01-Dec-2000
cytochrome cc3 precursor high-molecular-weight cytochrome c (HMW) Desulfovibrio vulgaris (strain Hildenborough) Desulfovibrio vulgaris Pollock, W.B.R. Loutfi, M. Bruschi, M. Rapp-Giles, B.J. Wall, J.D. Voordouw, G. J. Bacteriol. 1731991220-228 Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough. MUID91100286 A39193 DNA 1-545 GBM34607 NIDg145080 strain Hildenborough B39193 protein 32-150;151-161;162-185;200-211;212-216;231-251;262-274;282-301;302-353;375-388;389-500;513-545 strain Hildenborough Rossi, M. Pollock, W.B.R. Reij, M.W. Keon, R.G. Fu, R. Voordouw, G. J. Bacteriol. 17519934699-4711 The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex. MUID93328674 A40605 preliminary DNA 524-545 GBL16784 NIDg290377 strain Hildenborough cytochrome cc3 has 16 covalently bound hemes the second axial ligand of heme 12 may be a methionine Loutfi, M. Guerlesquin, F. Bianco, P. Haladjian, J. Bruschi, M. Biochem. Biophys. Res. Commun. 1591989670-676 Comparative studies of polyhemic cytochromes c isolated from Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio desulfuricans (Norway). MUID89193654 C32427 preliminary protein 32-66 strain Hildenborough hmc cytochrome cc3 cytochrome c3 homology chromoprotein heme iron metalloprotein domain signal sequence 1-31 predicted product cytochrome cc3 32-545 experimental domain cytochrome c3 homology 64-139 domain cytochrome c3 homology 157-248 domain cytochrome c3 homology 296-366 domain cytochrome c3 homology 447-540 binding-site heme iron (His) (axial ligands) 66,84 predicted binding-site heme iron (His) (axial ligands) 69,118 predicted binding-site heme (Cys) (covalent) 80,83 predicted binding-site heme iron (His) (axial ligands) 111,139 predicted binding-site heme (Cys) (covalent) 114,117 predicted binding-site heme (Cys) (covalent) 135,138 predicted binding-site heme iron (His) (axial ligands) 159,182 predicted binding-site heme iron (His) (axial ligands) 162,229 predicted binding-site heme (Cys) (covalent) 178,181 predicted binding-site heme iron (His) (axial ligands) 183,206 predicted binding-site heme (Cys) (covalent) 202,205 predicted binding-site heme iron (His) (axial ligands) 222,248 predicted binding-site heme (Cys) (covalent) 225,228 predicted binding-site heme (Cys) (covalent) 244,247 predicted binding-site heme iron (His) (axial ligands) 298,312 predicted binding-site heme iron (His) (axial ligands) 301,353 predicted binding-site heme (Cys) (covalent) 308,311 predicted binding-site heme iron (His) (axial ligands) 313,323 predicted binding-site heme (Cys) (covalent) 319,322 predicted binding-site heme iron (His) (axial ligands) 341,366 predicted binding-site heme (Cys) (covalent) 349,352 predicted binding-site heme (Cys) (covalent) 362,365 predicted binding-site heme (Cys) (covalent) 378,381 predicted binding-site heme iron (His) (axial ligand) 382 predicted binding-site heme iron (His) (axial ligands) 449,481 predicted binding-site heme iron (His) (axial ligands) 470,523 predicted binding-site heme (Cys) (covalent) 477,480 predicted binding-site heme iron (His) (axial ligands) 482,497 predicted binding-site heme (Cys) (covalent) 493,496 predicted binding-site heme iron (His) (axial ligands) 516,540 predicted binding-site heme (Cys) (covalent) 519,522 predicted binding-site heme (Cys) (covalent) 536,539 predicted 545 complete MRNGRTLLRWAGVLAATAIIGVGGFWSQGTTKALPEGPGEKRADLIEIGAMERFGKLDLP KVAFRHDQHTTAVTGMGKDCAACHKSKDGKMSLKFMRLDDNSAAELKEIYHANCIGCHTD LAKAGKKTGPQDAECRSCHNPKPSAASSWKEIGFDKSLHYRHVASKAIKPVGDPQKNCGA CHHVYDEASKKLVWGKNKEDSCRACHGEKPVDKRPALDTAAHTACISCHMDVAKTKAETG PVNCAGCHAPEAQAKFKVVREVPRLDRGQPDAALILPVPGKDAPREMKGTMKPVAFDHKA HEAKANDCRTCHHVRIDTCTACHTVNGTADSKFVQLEKAMHQPDSMRSCVGCHNTRVQQP TCAGCHGFIKPTKSDAQCGVCHVAAPGFDAKQVEAGALLNLKAEQRSQVAASMLSARPQP KGTFDLNDIPEKVVIGSIAKEYQPSEFPHRKIVKTLIAGIGEDKLAATFHIEKGTLCQGC HHNSPASLTPPKCASCHGKPFDADRGDRPGLKAAYHQQCMGCHDRMKIEKPANTACVDCH KERAK
CCALC A00131 13-Jul-1981 10-Oct-1997 15-Sep-2000
cytochrome c' [validated] Alcaligenes sp. Alcaligenes sp. Ambler, R.P. Biochem. J. 1351973751-758 The amino acid sequence of cytochrome c' from Alcaligenes sp. N.C.I.B. 11015. MUID74100155 A00131 protein 'Z',2-127 NCIB 11015 this organism was previously identified as Pseudomonas denitrificans Dobbs, A.J. Faber, H.R. Anderson, B.F. Baker, E.N. submitted to the Brookhaven Protein Data Bank May1995 PDB1CGO annotation X-ray crystallography, 1.8 angstroms, residues 1-51,'T',53-125 Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin heme proteins; the heme has no sixth ligand. However, they are confined in their reactivity with potential ligands to carbon monoxide and nitric oxide. homodimer cytochrome c' chromoprotein electron transfer heme homodimer iron metalloprotein pyroglutamic acid modified-site pyrrolidone carboxylic acid (Gln) 1 experimental binding-site heme (Cys) (covalent) 116,119 experimental binding-site heme iron (His) (axial ligand) 120 experimental 127 complete QFAKPEDAVKYRQSALTLMASHFGRMTPVVKGQAPYDAAQIKANVEVLKTLSALPWAAFG PGTEGGDARPEIWSDAASFKQKQQAFQDNIVKLSAAADAGDLDKLRAAFGDVGASCKACH DAYRKKK
CCAGB6 A00132 22-May-1981 22-May-1981 03-Mar-2000
cytochrome c556 Agrobacterium tumefaciens (strain B2a) Agrobacterium tumefaciens Van Beeumen, J. Tempst, P. Stevens, P. Bral, D. Van Damme, J. De Ley, J. Protides of the Biological Fluids, Proc. 28th Colloq., Peeters, H., ed., pp.69-74, Pergamon Press, Oxford 1980 Cytochromes c of two different sequence classes in Agrobacterium tumefaciens. A00132 protein 1-122 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme iron (Met, His) (axial ligands) 11,115 predicted binding-site heme (Cys) (covalent) 111,114 predicted 122 complete AGEVEKREGMMKQIGGAMGSLAAISKGEKPFDADTVKAAVTTIGTNAKAFPEQFPAGTET GSAAAPAIWENFEDFKAKAAKLGTDADIVLANLPGDQAGVATAMKTLGADCGTCHQTYRL KK
CCAGC6 A00133 22-May-1981 22-May-1981 03-Mar-2000
cytochrome c556 Agrobacterium tumefaciens (strain II Chrys) Agrobacterium tumefaciens Van Beeumen, J. Tempst, P. Stevens, P. Bral, D. Van Damme, J. De Ley, J. Protides of the Biological Fluids, Proc. 28th Colloq., Peeters, H., ed., pp.69-74, Pergamon Press, Oxford 1980 Cytochromes c of two different sequence classes in Agrobacterium tumefaciens. A00133 protein 1-122 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme iron (Met, His) (axial ligands) 11,115 predicted binding-site heme (Cys) (covalent) 111,114 predicted 122 complete AGEVEKREGMMKQIGGSMGALAAISKGQKPYDAEAVKAAVTTISTNAKAFPDQFPPGSET GSAAAPAIWENFDDFKSKAAKLGADADKVLASLPADQAGVTAAMQTLGADCGACHQTYRL KK
CCAGA6 A00134 19-Feb-1984 19-Feb-1984 03-Mar-2000
cytochrome c556 Agrobacterium tumefaciens (strain Apple 185) Agrobacterium tumefaciens Tempst, P. van Beeumen, J. Eur. J. Biochem. 1351983321-330 The amino acid sequence of cytochrome c-556 from Agrobacterium tumefaciens strain Apple 185. MUID83287429 A00134 protein 1-125 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme iron (Met, His) (axial ligands) 13,117 predicted binding-site heme (Cys) (covalent) 113,116 predicted 125 complete ADGGTHDARIALMKKIGGATGALGAIAKGEKPYDAEIVKASLTTIAETAKAFPDQFNPKD STDAEVNPKIWDNLDDFKAKAAKLSTDAETALAQLPADQAGVGNTLKTLGGNCGACHQAY RIKKD
CCRFCG A00135 31-May-1979 31-May-1979 03-Mar-2000
cytochrome c' Rhodocyclus gelatinosus Rhodocyclus gelatinosus Ambler, R.P. Meyer, T.E. Kamen, M.D. Nature 2781979661-662 Anomalies in amino acid sequences of small cytochromes c and cytochromes c' from two species of purple photosynthetic bacteria. MUID79199668 A00135 protein 1-129 Rhodopseudomonas is a genus of purple, nonsulfur, photosynthetic bacteria. cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 119,122 predicted binding-site heme iron (His) (axial ligand) 123 predicted 129 complete QFQKPGDAIEYRQSAFTLIANHFGRVAAMAQGKAPFDAKVAAENIALVSTLSKLPLTAFG PGTDKGHGTEAKPAVWSDAAGFKAAADKFAAAVDKLDAAGKTGDFAQIKAAVGETGGACK GCHDKFKEK
CCPCC8 A00136 S06910 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c' Paracoccus sp. Paracoccus sp. Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00136 protein 1-132 ATCC 12084 Ambler, R.P. Daniel, M. McLellan, L. Meyer, T.E. Cusanovich, M.A. Kamen, M.D. Biochem. J. 2481987365-371 Amino acid sequences of cytochrome c-554(548) and cytochrome c' from a halophilic denitrifying bacterium of the genus Paracoccus. MUID88133881 S06910 protein 1-132 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 122,125 predicted binding-site heme iron (His) (axial ligand) 126 predicted 132 complete AEPEDAIHYRQSALSVMGWQMGPMGAMAQGDIEYDADEFATRANNLAAVAHLPWEGFTEG TLQGDDHGVETDALADIGDDWEGFEERQETFKQEAATLAQMVDDGEEFSALRRQVGAVGK SCKGCHDDFRAE
CCQFCR A00137 07-May-1981 07-May-1981 03-Mar-2000
cytochrome c' Rhodospirillum rubrum Rhodospirillum rubrum Meyer, T.E. Ambler, R.P. Bartsch, R.G. Kamen, M.D. J. Biol. Chem. 25019758416-8421 Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1. MUID76069185 A00137 protein 1-126 strain S1, ATCC 11170 Yasui, M. Harada, S. Kai, Y. Kasai, N. Kusunoki, M. Matsuura, Y. J. Biochem. 1111992317-324 Three-dimensional structure of ferricytochrome c' from Rhodospirillum rubrum at 2.8 angstrom resolution. MUID92268030 annotation X-ray crystallography, 2.8 angstroms cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 116,119 experimental binding-site heme iron (His) (axial ligand) 120 experimental 126 complete ADPAAYVEYRKSVLSATSNYMKAIGITLKEDLAVPNQTADHAKAIASIMETLPAAFPEGT AGIAKTEAKAAIWKDFEAFKVASKKSQDAALELASAAETGDKAAIGAKLQALGGTCKACH KEFKAD
CCQFCP A00138 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c' Rhodospirillum photometricum Rhodospirillum photometricum Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00138 protein 1-125 strain SP113 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 116,119 predicted binding-site heme iron (His) (axial ligand) 120 predicted 125 complete ASPEAYVEYRKQALKASGDHMKALSAIVKGQLPLNAEAAKHAEAIAAIMESLPAAFPEGT AGIAKTEAKAVVWSKADEFKADAVKSADAAKALAQAATAGDTAQMGKALAALGGTCKGCH ETFRE
CCRFCX A00139 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c' Rhodopseudomonas sp. Rhodopseudomonas sp. Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00139 protein 1-128 strain TJ12 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 117,120 predicted binding-site heme iron (His) (axial ligand) 121 predicted 128 complete DGMETVKARQDYFKSLGGAMKALSGVAKNYDAEAAKAEAAKLEAILATDIKPLFAPGTSD ADFPGESEAKASIWENMEDFGAKGQAMHEAGMELIAAANTGEASAFGPALKKLGGTCKAC HDDYRAEH
CCRFPP A00140 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c' Rhodobacter capsulatus Rhodobacter capsulatus Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00140 protein 1-129 strain SP7 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 118,121 predicted binding-site heme iron (His) (axial ligand) 122 predicted 129 complete ADTKEVLEAREAYFKSLGKSMKAMTGVAKSFDAEAAKAEAAALEKILATDVAPLFPAGTS STDLPGQTEAKAAIWTNMADFGAKGKAMNDAGAEVIAAANAGDATAFGAALQKLGGTCKA CHDDYREED
CCRFCS A00141 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c' Rhodobacter sphaeroides Rhodobacter sphaeroides Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00141 protein 1-130 strain 2.4.1, ATCC 17023 Rhodopseudomonas is a genus of purple, nonsulfur, photosynthetic bacteria. cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 119,122 predicted binding-site heme iron (His) (axial ligand) 123 predicted 130 complete ADAEHVVEARKGYFSLVALEFGPLAAMAKGEMPYDAAAAKAHASDLVTLTKYDPSDLYAP GTSADDVKGTAAKAAIWQDADGFQAKGMAFFEAVAALEPAAGAGQKELAAAVGKVGTGCK SCHDDFRVKR
CCRFCP A00142 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c' Rhodopseudomonas palustris Rhodopseudomonas palustris Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00142 protein 1-125 strain 2.1.37 Rhodopseudomonas is a genus of purple, nonsulfur, photosynthetic bacteria. cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 113,116 experimental binding-site heme iron (His) (axial ligand) 117 predicted 125 complete QTDVIAQRKAILKQMGEATKPIAAMLKGEAKFDQAVVQKSLAAIADDSKKLPALFPADSK TGGDTAALPKIWEDKAKFDDLFAKLAAAATAAQGTIKDEASLKANIGGVLGNCKSCHDDF RAKKS
CCRF6P A00143 18-Dec-1981 18-Dec-1981 03-Mar-2000
cytochrome c556 Rhodopseudomonas palustris Rhodopseudomonas palustris Ambler, R.P. Bartsch, R.G. Daniel, M. Kamen, M.D. McLellan, L. Meyer, T.E. Van Beeumen, J. Proc. Natl. Acad. Sci. U.S.A. 7819816854-6857 Amino acid sequences of bacterial cytochromes c' and c-556. MUID82082545 A00143 protein 1-129 strain 2.1.37, ATCC 17007 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme iron (Met, His) (axial ligands) 12,121 predicted binding-site heme (Cys) (covalent) 117,120 predicted 129 complete QQDLVDKTQKLMKDNGRNMMVLGAIAKGEKPYDQAAVDAALKQFDETAKDLPKLFPDSVK GLKPFDSKYSSSPKIWAERAKFDTEIADFAKAVDGAKGKIKDVDTLKAAMQPIGKACGNC HENFRDKEG
CCQFCF A00144 30-Nov-1979 30-Nov-1979 03-Mar-2000
cytochrome c' Rhodospirillum fulvum Rhodospirillum fulvum Ambler, R.P. Abstr. E17 in Third Int. Symp. Photosynthetic Prokaryotes (Oxford), Nichols, J.M., ed., Univ. Liverpool 1979 A00144 protein 1-128 cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 118,121 predicted binding-site heme iron (His) (axial ligand) 122 predicted 128 complete QQSKPEELLKLRQGLMQTLKSQWAPIAGFAAGKADLPADAAQRAENMVLVAKLAPIGWAK GTEALPNSETKAEAFGAKSAQFMEGWKAMAAESTKLAAAAKAGPDALKAQAAATGKVCKA CHEEFKQD
CCQFCM A00145 30-Nov-1979 30-Nov-1979 15-Sep-2000
cytochrome c' [validated] Rhodospirillum molischianum Rhodospirillum molischianum Ambler, R.P. Abstr. E17 in Third Int. Symp. Photosynthetic Prokaryotes (Oxford), Nichols, J.M., ed., Univ. Liverpool 1979 A00145 protein 1-128 Finzel, B.C. Weber, P.C. Hardman, K.D. Salemme, F.R. submitted to the Brookhaven Protein Data Bank August1985 PDB2CCY annotation X-ray crystallography, 1.67 angstroms, residues 2-128 Finzel, B.C. Weber, P.C. Hardman, K.D. Salemme, F.R. J. Mol. Biol. 1861985627-643 Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67 Angstroms resolution. MUID86143817 annotation X-ray crystallography, 1.67 angstroms homodimer cytochrome c' chromoprotein electron transfer heme homodimer iron metalloprotein binding-site heme (Cys) (covalent) 118,121 experimental binding-site heme iron (His) (axial ligand) 122 experimental 128 complete QQSKPEDLLKLRQGLMQTLKSQWVPIAGFAAGKADLPADAAQRAENMAMVAKLAPIGWAK GTEALPNGETKPEAFGSKSAEFLEGWKALATESTKLAAAAKAGPDALKAQAAATGKVCKA CHEEFKQD
CCQFCT A00146 31-May-1979 31-May-1979 03-Mar-2000
cytochrome c' Rhodocyclus tenuis Rhodocyclus tenuis Ambler, R.P. Meyer, T.E. Kamen, M.D. Nature 2781979661-662 Anomalies in amino acid sequences of small cytochromes c and cytochromes c' from two species of purple photosynthetic bacteria. MUID79199668 A00146 protein 1-133 Rhodospirillum is a genus of purple, nonsulfur, photosynthetic bacteria. cytochrome c' chromoprotein electron transfer heme iron metalloprotein binding-site heme (Cys) (covalent) 122,125 experimental binding-site heme iron (His) (axial ligand) 126 predicted 133 complete EPAKSEDLIKWRQSAYQVLHWNMDRLKANIDSPQYNKDDGIKAANTIAAIANSGMGSLFA AGTETGKGWHPTSVKPAFFTDGKKVGEVAVAFNKEANELAKVAATGDAAAVKAQFGKVGQ TCKACHDDFRRKD
CCKRCV A00147 31-May-1979 31-May-1979 15-Sep-2000
cytochrome c' [validated] Chromatium vinosum Chromatium vinosum Ambler, R.P. Daniel, M. Meyer, T.E. Bartsch, R.G. Kamen, M.D. Biochem. J. 1771979819-823 The amino acid sequence of cytochrome c' from the purple sulphur bacterium Chromatium vinosum. MUID79187139 A00147 protein 1-131 strain D, ATCC 17899 Ren, Z. McRee, D.E. submitted to the Brookhaven Protein Data Bank May1992 PDB1BBH annotation X-ray crystallography, 1.8 angstroms, residues 1-131 Ren, Z. Meyer, T. Mcree, D.E. J. Mol. Biol. 2341993433-445 Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 angstroms resolution. MUID94047091 annotation X-ray crystallography, 1.8 angstroms homodimer cytochrome c' chromoprotein electron transfer heme homodimer iron metalloprotein binding-site heme (Cys) (covalent) 121,124 experimental binding-site heme iron (His) (axial ligand) 125 experimental 131 complete AGLSPEEQIETRQAGYEFMGWNMGKIKANLEGEYNAAQVEAAANVIAAIANSGMGALYGP GTDKNVGDVKTRVKPEFFQNMEDVGKIAREFVGAANTLAEVAATGEAEAVKTAFGDVGAA CKSCHEKYRAK
CFPM A00148 S19109 E48310 03-Aug-1984 03-Aug-1984 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor garden pea chloroplast garden pea chloroplast Pisum sativum Willey, D.L. Auffret, A.D. Gray, J.C. Cell 361984555-562 Structure and topology of cytochrome f in pea chloroplast membranes. MUID84106860 A00148 DNA 1-342 GBK01516 NIDg343020 PIDNAAA85363.1 PIDg552817 parts of this sequence, including the amino end of the mature protein, were determined by protein sequencing Nagano, Y. Matsuno, R. Sasaki, Y. Curr. Genet. 201991431-436 Sequence and transcriptional analysis of the gene cluster trnQ-zfpA-psaI-ORF231-petA in pea chloroplasts. MUID92224289 S19109 preliminary nucleic acid sequence not shown translation not shown DNA 1-191 EMBLX56315 the nucleotide sequence was submitted to the EMBL Data Library, August 1990 Willey, D.L. Gray, J.C. Curr. Genet. 151989213-220 Two small open reading frames are co-transcribed with the pea chloroplast genes for the polypeptides of cytochrome b-559. MUID89354671 E48310 DNA 330-342 GBX15767 NIDg12152 PIDNCAA33776.1 PIDg12157 Cytochrome f is a component of the cytochrome b/f complex, which transports protons across the thylakoid membrane and transfers electrons from photosystem II to photosystem I. It receives electrons from a Rieske iron-sulfur protein and passes them to plastocyanin; this function is very similar to that of mitochondrial cytochrome c1. petA chloroplast cytochrome f chloroplast chromoprotein electron transfer heme iron membrane protein metalloprotein oxidoreductase photosynthesis thylakoid domain transit peptide (thylakoid) 1-57 predicted product plastoquinol--plastocyanin reductase cytochrome f 58-342 experimental domain thylakoid lumenal 58-310 experimental domain transmembrane 311-327 predicted domain chloroplast stroma 328-342 experimental binding-site heme (Cys) (covalent) 78,81 predicted binding-site heme iron (His) (axial ligand) 82 predicted 342 complete MDRELSNLPNLIVEIFRIKDCTMQTRNAFSWIKKEITRSISVLLMIYIITRAPISNAYPI FAQQGYENPREATGRIVCANCHLANKPVDIEVPQAVLPDTVFEAVVRIPYDMQVKQVLAN GKKGALNVGAVLILPEGFELAPPHRLSPQIKEKIGNLSFQSYRPTKKNILVIGPVPGKKY SEITFPILSPDPATKRDVYFLKYPLYVGGNRGRGQIYPDGSKSNNNVSNATATGVVKQII RKEKGGYEITIVDASDGSEVIDIIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEI VLQDPLRVQGLLLFLASIILAQILLVLKKKQFEKVQLSEMNF
CFNT A00149 30-Jun-1987 30-Jun-1987 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor common tobacco chloroplast common tobacco chloroplast Nicotiana tabacum Sugiura, M. submitted to the EMBL Data Library August1986 A00149 DNA 1-320 cv. Bright Yellow 4 Shinozaki, K. Ohme, M. Tanaka, M. Wakasugi, T. Hayashida, N. Matsubayashi, T. Zaita, N. Chunwongse, J. Obokata, J. Yamaguchi-Shinozaki, K. Ohto, C. Torazawa, K. Meng, B.Y. Sugita, M. Deno, H. Kamogashira, T. Yamada, K. Kusuda, J. Takaiwa, F. Kato, A. Tohdoh, N. Shimada, H. Sugiura, M. EMBO J. 519862043-2049 The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. annotation gene organization, sites, features Cytochrome f is a component of the cytochrome b6-f complex, which translocates protons across the thylakoid membrane and transfers electrons from photosystem II to photosystem I. It receives electrons from the Rieske iron-sulfur protein and passes them to plastocyanin; this function is very similar to that of mitochondrial cytochrome c1. petA chloroplast cytochrome f chloroplast chromoprotein electron transfer heme iron membrane protein metalloprotein oxidoreductase photosynthesis thylakoid domain transit peptide (thylakoid) 1-35 predicted product plastoquinol--plastocyanin reductase cytochrome f 36-320 predicted domain transmembrane 283-307 predicted binding-site heme (Cys) (covalent) 56,59 predicted binding-site heme iron (His) (axial ligand) 60 predicted 320 complete MQTRNAFSWLKKQITRSISVSLMIYILTRTSISSAYPIFAQQGYENPREATGRIVCANCH LANKPVEIEVPQAVLPDTVFEAVVRIPYDMQLKQVLANGKRGGLNVGAVLILPEGFELAP PDRISPEMKEKIGNLSFQSYRPNKKNILVIGPVPGQKYSEITFPILSPDPATKKDVHFLK YPIYVGGNRGRGQIYPDGSKSNNTVYNATAAGIVSKIIRKEKGGYEITITDASDGRQVVD IIPPGPELLVSEGESIKFDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFLASVILAQ IFLVLKKKQFEKVQLAEMNF
CFRZ JQ0239 S05119 A29496 31-Mar-1990 31-Mar-1990 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0239 DNA 1-320 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05119 nucleic acid sequence not shown translation not shown DNA 1-320 EMBLX15901 NIDg11957 PIDNCAA33961.1 PIDg12000 cv. Nihonbare Wu, N.H. Cote, J.C. Wu, R. Gene 501986271-278 Nucleotide sequence of the rice cytochrome f gene and the presence of sequence variation near this gene. MUID87219885 A29496 DNA 1-13,'I',15-19,'D',21-320 GBM15955 NIDg343206 PIDNAAA84590.1 PIDg552858 cv. Labelle Cytochrome f is a component of the cytochrome b6-f complex, which translocates electrons from photosystem II to photosystem I. It receives electrons from the Rieske iron-sulfur protein and passes them to plastocyanin; this function is very similar to that of mitochondrial cytochrome c1. petA CP59601-60563 chloroplast cytochrome f chloroplast chromoprotein electron transfer heme iron membrane protein metalloprotein oxidoreductase photosynthesis thylakoid domain transit peptide (thylakoid) 1-35 predicted product cytochrome f 36-320 predicted domain transmembrane 289-305 predicted binding-site heme (Cys) (covalent) 56,59 predicted binding-site heme iron (His) (axial ligand) 60 predicted 320 complete MENRNTFSWVKEQMTRSISVSIMIYVITRTSISNAYPIFAQQGYENPREATGRIVCANCH LANKPVDIEVPQAVLPDTVFEAVLRIPYDMQLKQVLANGKKGGLNVGAVLILPEGFELAP PDRISPELKEKIGNLSFQSYRPNKKNILVIGPVPGKKYSEIVFPILSPDPAMKKDVHFLK YPIYVGGNRGRGQIYPDGSKSNNTVYNATSTGVVRKILRKEKGGYEISIVDASDGRQVID LIPPGPELLVSEGESIKLDQPLTSNPNVGGFGQGDAEIVLQDPLRVQGLLFFFASVILAQ VFLVLKKKQFEKVQLYEMNF
CFLV S01534 A00150 30-Jun-1987 30-Jun-1987 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome f precursor liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Fukuzawa, H. Kohchi, T. Sano, T. Shirai, H. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988333-351 Structure and organization of Marchantia polymorpha chloroplast genome. III. Gene organization of the large single copy region from rbcL to trnI(CAU). MUID89068687 S01534 DNA 1-320 EMBLX04465 NIDg11640 PIDNCAA28097.1 PIDg11685 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features petA chloroplast cytochrome f chloroplast chromoprotein electron transfer heme iron membrane protein metalloprotein oxidoreductase photosynthesis thylakoid domain transit peptide (thylakoid) 1-35 predicted product plastoquinol--plastocyanin reductase cytochrome f 36-320 predicted domain transmembrane 289-305 predicted binding-site heme (Cys) (covalent) 56,59 predicted binding-site heme iron (His) (axial ligand) 60 predicted 320 complete MQNRNFNNLIIKWAIRLISIMIIINTIFWSSISEAFPIYAQQGYENPREATGRIVCANCH LAKKPVDIEVPQSVLPNTVFEAVVKIPYDMQIKQVLANGKKGSLNVGAVLILPEGFELAP SDRIPPEMKEKIGNLFFQPYSNDKKNILVIGPVPGKKYSEMVFPILSPDPATNKEAHFLK YPIYVGGNRGRGQIYPDGSKSNNTVYNASITGKVSKIFRKEKGGYEITIDDISDGHKVVD ISAAGPELIISEGELVKVDQPLTNNPNVGGFGQGDAEVVLQDPLRIQGLLLFFGSVILAQ IFLVLKKKQFEKVQLAEMNF
CBEC62 S19544 S25107 S56462 A33153 A00195 G65235 24-Apr-1984 02-Jul-1996 23-Mar-2001
cytochrome b562 precursor [validated] Escherichia coli Escherichia coli Nikkila, H. Gennis, R.B. Sligar, S.G. Eur. J. Biochem. 2021991309-313 Cloning and expression of the gene encoding the soluble cytochrome b(562) of Escherichia coli. MUID92104149 S19544 DNA 1-128 EMBLS74736 NIDg241592 PIDNAAB20782.1 PIDg241593 Trower, M.K. submitted to the EMBL Data Library July1992 S25107 DNA 1-128 EMBLX67290 NIDg41194 PIDNCAA47706.1 PIDg41195 ssp. B strain OP7 Burland, V. Plunkett III, G. Sofia, H.J. Daniels, D.L. Blattner, F.R. Nucleic Acids Res. 2319952105-2119 Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. MUID95334362 S56462 nucleic acid sequence not shown translation not shown DNA 29-38,'V',40-121,'S',123-124,'K',126-128 EMBLU14003 NIDg1263172 PIDNAAA97133.1 PIDg537078 the nucleotide sequence was submitted to the EMBL Data Library, August 1994 Lederer, F. Glatigny, A. Bethge, P.H. Bellamy, H.D. Mathews, F.S. J. Mol. Biol. 1481981427-448 Improvement of the 2.5 angstrom resolution model of cytochrome b-562 by redetermining the primary structure and using molecular graphics. MUID82078041 A33153 protein 23-128 sequence revision X-ray crystallography, 2.5 angstroms Itagaki, E. Hager, L.P. Biochem. Biophys. Res. Commun. 3219681013-1019 The amino acid sequence of cytochrome b562 of Escherichia coli. MUID69077911 A00195 protein 23-27,'D',29,'Q',31-42,'BBZKAND',45-49,'L',54-60,'N',62-64,'K',65-75,'N',77,'QP',80-92,'E',94-112,'EA',115-123,'K',124-128 Hamada, K. Bethge, P.H. Mathews, F.S. submitted to the Brookhaven Protein Data Bank January1990 PDB256B annotation X-ray crystallography, 1.4 angstroms, residues 23-128 Mathews, F.S. Bethge, P.H. Czerwinski, E.W. J. Biol. Chem. 25419791699-1706 The structure of cytochrome b562 from Escherichia coli at 2.5A resolution. MUID79109778 annotation X-ray crystallography, 2.5 angstroms Wand, A.J. Feng, Y. Sligar, S.G. submitted to the Brookhaven Protein Data Bank October1993 PDB1APC annotation conformation by (1)H-NMR, residues 23-128 Feng, Y. Sligar, S.G. Wand, A.J. Nat. Struct. Biol. 1199430-35 Solution structure of apocytochrome b562. MUID95384751 annotation conformation by (1)H-NMR, apo form Feng, Y. Wand, A.J. Sligar, S.G. Biochemistry 3019917711-7717 (1)H and (15)N NMR resonance assignments and preliminary structural characterization of Escherichia coli apocytochrome b562. MUID91329334 annotation conformation by (1)H-NMR Blattner, F.R. Plunkett III, G. Bloch, C.A. Perna, N.T. Burland, V. Riley, M. Collado-Vides, J. Glasner, J.D. Rode, C.K. Mayhew, G.F. Gregor, J. Davis, N.W. Kirkpatrick, H.A. Goeden, M.A. Rose, D.J. Mau, B. Shao, Y. Science 27719971453-1462 The complete genome sequence of Escherichia coli K-12. MUID97426617 G65235 nucleic acid sequence not shown translation not shown DNA 29-38,'V',40-121,'S',123-124,'K',126-128 GBAE000495 GBU00096 NIDg2367361 PIDNAAC77193.1 PIDg1790684 UWGPb4236 strain K-12, substrain MG1655 This periplasmic electron transfer protein appears to be nonessential. cybC cytochrome b562 chromoprotein electron transfer heme iron metalloprotein monomer periplasmic space domain signal sequence 1-22 predicted product cytochrome b562 23-128 experimental binding-site heme iron (Met, His) (axial ligands) 29,124 experimental 128 complete MRKSLLAILAVSSLVFSSASFAADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAAL DAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTR NAYHQKYR
CBHU A00151 I57452 22-May-1981 23-Oct-1981 31-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b human mitochondrion man mitochondrion Homo sapiens Anderson, S. Bankier, A.T. Barrell, B.G. de Bruijn, M.H.L. Coulson, A.R. Drouin, J. Eperon, I.C. Nierlich, D.P. Roe, B.A. Sanger, F. Schreier, P.H. Smith, A.J.H. Staden, R. Young, I.G. Nature 2901981457-465 Sequence and organization of the human mitochondrial genome. MUID81173052 A00151 DNA 1-380 EMBLV00662 NIDg13003 PIDNCAA24038.1 PIDg13016 GSPDBGN00100 Spurr, N.K. Bodmer, W.F. Mol. Biol. Med. 21984239-249 Serendipitous cloning of a mitochondrial cDNA and its polymorphism. MUID86064879 I57452 preliminary translated from GB/EMBL/DDBJ mRNA 269-380 GBM28016 NIDg337203 PIDNAAA31851.1 PIDg552606 GDBMTCYB GDB118906 MTH14747-15887 mitochondrion SGC1 the transmembrane complex includes cytochrome b, cytochrome c1 (see PIR:S00680), Rieske iron-sulfur protein, and other accessory proteins the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 380 complete MTPMRKINPLMKLINHSFIDLPTPSNISAWWNFGSLLGACLILQITTGLFLAMHYSPDAS TAFSSIAHITRDVNYGWIIRYLHANGASMFFICLFLHIGRGLYYGSFLYSETWNIGIILL LATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGYSVDSPTLTRFFT FHFILPFIIAALATLHLLFLHETGSNNPLGITSHSDKITFHPYYTIKDALGLLLFLLSLM TLTLFSPDLLGDPDNYTLANPLNTPPHIKPEWYFLFAYTILRSVPNKLGGVLALLLSILI LAMIPILHMSKQQSMMFRPLSQSLYWLLAADLLILTWIGGQPVSYPFTIIGQVASVLYFT TILILMPTISLIENKMLKWA
CBBO A00152 S27097 A49734 18-Aug-1982 18-Aug-1982 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b cytochrome bc1 complex cytochrome b component mitrochondrial complex III cytochrome b subunit ubiquinol-cytochrome-c oxidoreductase cytochrome b bovine mitochondrion cattle mitochondrion Bos primigenius taurus Anderson, S. de Bruijn, M.H.L. Coulson, A.R. Eperon, I.C. Sanger, F. Young, I.G. J. Mol. Biol. 1561982683-717 Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome. MUID83010260 A00152 DNA 1-379 GBJ01394 NIDg336430 PIDNAAB59280.1 PIDg336443 EMBLV00654 NIDg12800 PIDg12813 Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S27097 DNA 1-379 this sequence and translation are not annotated in GenBank release 111.0, but do represent a separate determination He, D.Y. Yu, L. Yu, C.A. J. Biol. Chem. 26919942292-2298 Ubiquinone binding domains in bovine heart mitochondrial cytochrome b. MUID94124591 A49734 protein 142-146;327-332 Xia, D. Yu, C.A. Kim, H. Xia, J.Z. Kachurin, A.M. Zhang, L. Yu, L. Deisenhofer, J. Science 277199760-66 Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria. MUID97349328 annotation X-ray crystallography, 2.9 angstroms mitochondrion SGC1 the transmembrane complex includes cytochrome b, cytochrome c1 (see PIR:CCBO1), Rieske iron-sulfur protein (see PIR:A34660), and other accessory proteins (see PIR:CCBO11, PIR:CCBO17, PIR:A24864, PIR:ZPBOC1, and PIR:ZPBOC2) the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 experimental binding-site heme iron (His) (axial ligands) (high potential) 97,196 experimental 379 complete MTNIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILL LTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFILPFIIMAIAMVHLLFLHETGSNNPTGISSDVDKIPFHPYYTIKDILGALLLILALM LLVLFAPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAFSILI LALIPLLHTSKQRSMMFRPLSQCLFWALVADLLTLTWIGGQPVEHPYITIGQLASVLYFL LILVLMPTAGTIENKLLKW
CBMS A00153 02-Apr-1982 02-Apr-1982 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b mouse mitochondrion house mouse mitochondrion Mus musculus Bibb, M.J. Van Etten, R.A. Wright, C.T. Walberg, M.W. Clayton, D.A. Cell 261981167-180 Sequence and gene organization of mouse mitochondrial DNA. MUID82137051 A00153 DNA 1-381 GBJ01420 NIDg342520 PIDNAAB48656.1 PIDg896302 EMBLV00711 NIDg13838 PIDg13851 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 381 complete MTNMRKTHPLFKIINHSFIDLPAPSNISSWWNFGSLLGVCLMVQIITGLFLAMHYTSDTM TAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTFMETWNIGVLLL FAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIIAALAIVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDILGILIMFLILM TLVLFFPDMLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILI LALMPFLHTSKQRSLMFRPITQILYWILVANLLILTWIGGQPVEHPFIIIGQLASISYFS IILILMPISGIIEDKMLKLYP
CBRT A00154 S04759 14-Nov-1983 14-Nov-1983 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b rat mitochondrion Norway rat mitochondrion Rattus norvegicus Koike, K. Kobayashi, M. Yaginuma, K. Taira, M. Yoshida, E. Imai, M. Gene 201982177-185 Nucleotide sequence and evolution of the rat mitochondrial cytochrome b gene containing the ochre termination codon. MUID83158755 A00154 DNA 1-380 GBJ01436 NIDg343168 PIDNAAA99907.1 PIDg829020 the authors translated the codon ATA for residue 42 as Ile, CAC for residue 54 as Asn, ATA for residue 89 as Ile, ATT for residue 284 as Leu, ATC for residue 295 as Ala, and TTA for residue 296 as Phe. In another figure, the amino acids at all these positions except position 89, which was shown as Leu, agreed with the nucleic acid translation. In addition, the sequence differed from the translation in having 11-Glu Gadaleta, G. Pepe, G. De Candia, G. Quagliariello, C. Sbisa, E. Saccone, C. J. Mol. Evol. 281989497-516 The complete nucleotide sequence of the Rattus norvegicus mitochondrial genome: cryptic signals revealed by comparative analysis between vertebrates. MUID89362487 S04759 DNA 1-82,'Q',84-152,'I',154-380 EMBLX14848 NIDg854269 PIDNCAA32966.1 PIDg639986 cob 87-94 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 380 complete MTNIRKSHPLFKIINHSFIDLPAPSNISSWWNFGSLLGVCLMVQILTGLFLAMHYTSDTM TAFSSVTHICRDVNYGWLIRYLHANGASMFFICLFLHVGRGLYYGSYTFLETWNIGIILL FAVMATAFMGYVLPWGQMSFWGATVITNLLSATPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIIAALAIVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDLLGVFMLLLFLM TLVLFFPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVVALILSILI LAFLPFLHTSKQRSLTFRPITQILYWILVANLLVLTWIGGQPVEHPFIIIGQLASISYFS IILILMPISGIVEDKMLKWN
S17408 S17408 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b black rhinoceros mitochondrion black rhinoceros mitochondrion Diceros bicornis Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17408 translation not shown DNA 1-379 EMBLX56283 NIDg12903 PIDNCAA39730.1 PIDg578698 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLIKIINHSFIDLPTPSNISAWWNFGSLLGICLILQILTGLFLAMHYTPDTT TAFSSVAHICREVNYGWIIRYLHANGASMFFICLFIHMGRGLYYGSYTFLKTWNIGVILL LTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIISALAITHLLFLHETGSNNPSGIPSNMDKIPFHPYYTIKDILGILLLILTLL TLVLFSPHHLGDPDNYTPATPLNTPPHIKPEWYFLFAYAILRSVPNKLGGVLALALSILI LALIPILHTSKQRSMMFRPLSQCMFWLLVADLLTLTWIGGQPVEHPFIIIGQLASILYFS LILVLMPLAGIIENNLLKW
S17410 S17410 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Grevy's zebra mitochondrion Grevy's zebra mitochondrion Equus grevyi Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17410 translation not shown DNA 1-379 EMBLX56282 NIDg12948 PIDNCAA39729.1 PIDg578705 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLIKIINHSFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLFIHVGRGLYYGSYTFLETWNIGIILL LTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIITALVIVHLLFLHETGSNNPSGIPSDMDKIPFHPYYTIKDILGLLLLILLLL TLVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILI LALIPTLHTSKQRSMMFRPLSQCVFWLLVADLLTLTWIGGQPVEHPYMIIGQLASILYFS LILIFMPLASTIENNLLKW
S17419 S17419 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Balabac chevrotain mitochondrion Balabac chevrotain mitochondrion Tragulus napu Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17419 translation not shown DNA 1-379 EMBLX56288 NIDg13836 PIDNCAA39735.1 PIDg578830 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MINIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTS TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFLETWNIGVILL LTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTELVEWIWGGFSVDKATLTRFFA FHFILPFVITALALVHLLFLHETGSNNPTGIPSDADKIPFHPYYTIKDVLGALVLMLVLL LLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALIASILI LQLMPLLHTSKQRSMMFRPISQCLFWLLAADLLTLTWIGGQPVEHPYVVIGQLASILYFS IILVLMPVAGVIENKMLKW
S17405 S17405 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b pronghorn mitochondrion pronghorn mitochondrion Antilocapra americana Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17405 translation not shown DNA 1-379 EMBLX56286 NIDg12624 PIDNCAA39733.1 PIDg578675 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MINIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTADTT TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYMFLETWNIGVILL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFILPFIIAALAMVHLLFLHETGSNNPTGIPSDADKIPFHPYYTIKDILGALLMILALM MLVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LIFMPLLHTSKQRSMMFRPFSQCLFWILVADLLTLTWIGGQPVEHPFIIIGQLASIMYFL IILVLMPVTSTIENNLLKW
S43267 S43267 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Caperea marginata mitochondrion mitochondrion Caperea marginata Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43267 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75586 NIDg457773 PIDNCAA53262.1 PIDg578663 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINNAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWVIRYLHANGASMFFICIYAHMGRGLYYGSHAFRETWNIGVILL FTTMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAAVHLLFLHETGSNNPTGIPSNMDKIPFHPYYTIKDILGVLLLILTLL MLTLFTPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILI LALIPMLHTSKQRSMMFRPFSQFLFWVLVADLLTLTWIGGQPVEHPYVMVGQLASILYFF LILILMPVTSLIENKLMKW
S43265 S43265 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Balaena glacialis mitochondrion mitochondrion Balaena glacialis Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43265 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75587 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPVMKIINDAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTT TAFSSITHICRDVNYGWIIRYLHANGASMFFICLYAHMGRGLYYGSYAFQETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGNTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAIVHLLFLHETGSNNPTGIPSNMDKIPFHPYYTIKDILGALLLILTLL MLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LAFIPMLHTSKQRSMMFRPFSQFLFWVLVADLLTLTWIGGQPVEHPYMIVGQFASILYFL LILVLMPTASLIENKLMKW
S17409 S17409 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b fallow deer mitochondrion fallow deer mitochondrion Dama dama Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17409 translation not shown DNA 1-379 EMBLX56290 NIDg12907 PIDNCAA39737.1 PIDg578699 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MINIRKSHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTM TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYMFLETWNIGVILL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFILPFIIAALAMVHLLFLHETGSNNPTGIPSDADKIPFHPYYTIKDILGALLMILVLM MLVLFSPDVLGDPDNYTPANPLNTPPLIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LIFMPLLHTSKQRSMMFRPFSQCLFWILVADLLTLTWIGGQPVEHPFIIIGQLASILYFL IILVLMPATSTIQNNLLKW
S43266 S43266 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Balaena mysticetus mitochondrion mitochondrion Balaena mysticetus Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43266 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75588 NIDg457770 PIDNCAA53264.1 PIDg578577 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINDAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTT TAFSSITHICRDVNYGWIIRYLHANGASMFFICLYAHMGRGLYYGSHAFQETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYVGNTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAIVHLLFLHETGSNNPTGIPSDMDKIPFHPYYTIKDILGALLLILALL MLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LAFIPMLHTSKQRSMMFRPFSQFLFWMLVADLLTLTWIGGQPVEHPYVIVGQFASILYFL LILVLMPVASLIENKLMKW
S17411 S17411 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b giraffe mitochondrion giraffe mitochondrion Giraffa camelopardalis Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17411 translation not shown DNA 1-379 EMBLX56287 NIDg12951 PIDNCAA39734.1 PIDg578707 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MINIRKSHPLMKIVNNALIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILL FTVMATAFMEYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFILPFIIMALTMVHLLFLHETGSNNPMGIPSDMDKIPFHPYYTIKDILGALLLILVLM LLVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LIFMPLLHTSKQRSMMFRPFSQCLFWILVADLLTLTWIGGQPVEHPFIIIGQLASIMYFL IILVLMPVTSAIQNNLLKW
S43268 S43268 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b California gray whale mitochondrion California gray whale mitochondrion Eschrichtius robustus, Eschrichtius gibbosus Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43268 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75585 NIDg457777 PIDNCAA53261.1 PIDg578673 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINDAFVDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTT TAFSSITHICRDVNYGWIIRYLHANGASMFFICLYAHMGRGLYYGSHAFRETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWVWGGFSVDKATLTRFFA FHFILPFIILALAIVHLIFLHETGSNNPTGIPSNMDNIPFHPYYTIKDMLGALLLILTLL MLTLFAPDLLGDPDNYTPANPLSTPTHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LAFIPMLHTSKQRSMMFRPFSQFLFWVLVADLLTLTWIGGQPVEHPYMIVGQFASILYFL LILVLMPVASLIENKLMKW
S17414 S17414 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b mule deer mitochondrion mule deer mitochondrion Odocoileus hemionus Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17414 translation not shown DNA 1-379 EMBLX56291 NIDg13198 PIDNCAA39738.1 PIDg578739 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTM TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFILPFIIAALAMVHLLFLHETGSNNPTGIPSDADKIPFHPYYTIKDILGALLLTLFLM LLVLFAPDLLGDPDNYTPANPLNTPPHIKPECYFLFAYAILRSIPNKLGGVLALVLSILI LVLMPLLHTSKQRSMMFRPFSQCLFWILVAHLLTLTWIGGQPVEHPFIIIGQLASILYFL IILVLMPVTSTIENNLLKW
S17407 S17407 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b goat mitochondrion domestic goat mitochondrion Capra aegagrus hircus Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17407 translation not shown DNA 1-379 EMBLX56289 NIDg12871 PIDNCAA39736.1 PIDg578696 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIVNNAFIDLPTPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTM TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHIGRGLYYGSYTFLETWNIGVILL LATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFILPFIITALAMVHLLFLHETGSNNPTGIPSDTDKIPFHPYYTIKDILGAMLLILVLM LLVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LVLVPFLHTSKQRSMMFRPISQCMFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFL IILVMMPVASTIENNLLKW
S43269 S43269 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b humpback whale mitochondrion humpback whale mitochondrion Megaptera novaeangliae Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43269 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75584 NIDg457794 PIDNCAA53260.1 PIDg578841 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINDTFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYAHMGRGLYYGSYAFRETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIITALAIVHLIFLHETGSNNPTGIPSNMDKIPFHPYYTIKDTLGALLLILTLL MLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LAFIPMLHTSKQRSMMFRPFSQFLFWMLVADLLALTWIGGQPVEHPYMIVGQLASILYFL LILVLMPMTSLIENKLMKW
S17413 S17413 S55933 T11062 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b sheep mitochondrion domestic sheep mitochondrion Ovis orientalis aries, Ovis ammon aries Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17413 translation not shown DNA 1-379 EMBLX56284 NIDg13156 PIDNCAA39731.1 PIDg578735 Zardoya, R. Villalta, M. Lopez-Perez, M.J. Garrido-Pertierra, A. Montoya, J. Bautista, J.M. Curr. Genet. 28199594-96 Nucleotide sequence of the sheep mitochondrial DNA D-loop and its flanking tRNA genes. MUID96022431 S55933 nucleic acid sequence not shown translation not shown DNA 204-237,'T',239-294,'I',296-303,'I',305-379 EMBLL29055 NIDg456705 the nucleotide sequence was submitted to the EMBL Data Library, March 1994 this ORF is not annotated in GenBank entry SHPMTDLOOP, release 111.0 Hiendleder, S. Lewalski, H. Wassmuth, R. Janke, A. J. Mol. Evol. 471998441-448 The complete mitochondrial DNA sequence of the domestic sheep (Ovis aries) and comparison with the other major ovine haplotype. MUID98440761 T11062 preliminary translated from GB/EMBL/DDBJ DNA 1-294,'I',296-379 EMBLAF010406 NIDg3445513 PIDg3445516 PIDNAAD10107.1 strain Merinolandschaf; liver cytb mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MINIRKTHPLMKIVNNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLFMHVGRGLYYGSYTFLETWNIGVILL FATMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTNLVEWIWGGFSVDKATLTRFFA FHFIFPFIIAALAMVHLLFLHETGSNNPTGIPSDTDKIPFHPYYTIKDILGAILLILILM LLVLFTPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILV LVIMPLLHTSKQRSMMFRPISQCMFWILVADLLTLTWIGGQPVEHPYIIIGQLASIMYFL IILVMMPVASIIENNLLKW
S17418 T10984 T11882 S17418 S58080 S58021 S58059 S58058 S58060 S58079 29-Jan-1993 23-Jul-1999 16-Jun-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b pig mitochondrion domestic pig mitochondrion Sus scrofa domestica Lin, C.S. Liu, C.Y. Sun, Y.L. Chang, L.C. Cheng, I.C. Yang, P.C. Mao, S.J.T. Huang, M.C. submitted to the EMBL Data Library November1997 Complete nucleotide sequence of the porcine mitochondrial genome. T10984 preliminary translated from GB/EMBL/DDBJ DNA 1-379 EMBLAF034253 NIDg4958951 PIDg4958964 PIDNAAD34197.1 Ursing, B.M. submitted to the EMBL Data Library February1999 The complete mitochondrial DNA sequence of the pig (Sus scrofa). T11882 preliminary translated from GB/EMBL/DDBJ DNA 1-313,'G',315-379 EMBLAJ002189 PIDNCAA05239.1 Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17418 translation not shown DNA 1-197,'M',199-313,'G',315-379 EMBLX56295 NIDg13678 PIDNCAA39742.1 PIDg578827 Randi, E. Lucchini, V. Diong, C. submitted to the EMBL Data Library July1995 Evolutionary genetics of the suiformes. S58080 DNA 1-379 EMBLZ50087 NIDg902692 PIDNCAA90418.1 PIDg902693 subspecies leucomystax S58021 DNA 1-379 EMBLZ50079 NIDg902354 PIDNCAA90410.1 PIDg902355 Asian domestic pig S58059 DNA 1-313,'G',315-379 EMBLZ50088 NIDg902696 PIDNCAA90419.1 PIDg902697 subspecies majori S58058 DNA 1-313,'G',315-379 EMBLZ50085 NIDg902688 PIDNCAA90416.1 PIDg902689 subspecies lybicus, isolate Bulgarian (1) S58060 DNA 1-313,'G',315-367,'V',369-379 EMBLZ50089 NIDg902694 PIDNCAA90420.1 PIDg902695 subspecies meridionalis (Sardinian wild boar) S58079 DNA 1-294,'M',296-313,'G',315-379 EMBLZ50086 NIDg902690 PIDNCAA90417.1 PIDg902691 subspecies lybicus, isolate Bulgarian (2) cytb mitochondrion SGC1 cytb the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLMKIINNAFIDLPAPSNISSWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSVTHICRDVNYGWVIRYLHANGASMFFICLFIHVGRGLYYGSYMFLETWNIGVVLL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFA FHFILPFIITALAAVHLLFLHETGSNNPTGISSDMDKIPFHPYYTIKDILGALFMMLILL ILVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVASILI LILMPMLHTSKQRSMMFRPLSQCLFWMLVADLITLTWIGGQPVEHPFIIIGQLASILYFL IILVLMPITSIIENNLLKW
S17415 S17415 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b bridled dolphin mitochondrion bridled dolphin mitochondrion Stenella attenuata Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17415 translation not shown DNA 1-379 EMBLX56294 NIDg13495 PIDNCAA39741.1 PIDg578785 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKILNDAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTS TAFSSVAHICRDVNYGWFIRYLHANGASMFFICLYAHIGRGLYYGSYMFQETWNIGVLLL LTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIITALAAVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGGLLLILTLL ALTLFTPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLAGVLALLLSILV LIFIPMLQTSKQRSMMFRPFSQLLFWTLIADLLTLTWIGGQPVEHPYIIVGQLASILYFL LILVLMPTAGLIENKLLKW
S43263 S43263 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b sei whale mitochondrion sei whale mitochondrion Balaenoptera borealis Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43263 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75582 NIDg457763 PIDNCAA53258.1 PIDg578574 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIVNDTFVDLPTPSNISSWWNFGSLLGLCLITQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYAHMGRGLYYGSYAFRETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAMVHLIFLHETGSNNPTGIPSDMDKIPFHPYYTVKDILGALLLILTLL MLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LALIPMLHTSKQRSMMFRPFSQFLFWVLVADLLTLTWIGGQPVEHPYVIVGQFASILYFL LILVLMPATSLIENKLMKW
S43262 S43262 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Balaenoptera bonaerensis mitochondrion mitochondrion Balaenoptera bonaerensis Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43262 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75581 NIDg457762 PIDNCAA53257.1 PIDg578573 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINDAFVDLPTPSNISSWWNFGSLLGLCLIVQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYAHMGRGLYYGTHAFRETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAIVHLIFLRETGSNNPTGIPSDMDKIPFHPYYTIKDILGALLLILTLL TLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LAFIPMLHTSKQRSMMFRPFSQFLFWVLVADLLTLTWIGGQPVEHPYMIVGQLASILYFL LILVLMPVASLIENKLMKW
S17417 S17417 S17416 29-Jan-1993 20-Aug-1994 17-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b, isolate 1B pantropical spinner dolphin mitochondrion pantropical spinner dolphin mitochondrion Stenella longirostris Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17417 translation not shown DNA 1-379 EMBLX56293 NIDg13628 PIDNCAA39740.1 PIDg578804 isolate 1B S17416 translation not shown DNA 1-59,'T',61-97,'M',99-265,'P',267-299,'I',301-326,'V',328-379 EMBLX56292 NIDg13626 PIDNCAA39739.1 PIDg578803 isolate 1A mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKILNDAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTS TAFSSVAHICRDVNYGWFIRYLHANGASMFFICLYAHIGRGLYYGSYMFQETWNIGVLLL LTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIITALAAVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGGLLLILTLL ALTLFTPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILV LIFIPMLQTSKQRSMMFRPFSQLLFWTLIADLLTLTWIGGQPVEHPYIIVGQLASILYFL LILVLMPTAGLIENKLLKW
S43261 S43261 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b minke whale mitochondrion minke whale, lesser rorqual mitochondrion Balaenoptera acutorostrata Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43261 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75753 NIDg457761 PIDNCAA53381.1 PIDg578572 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINDAFIDLPTPSNISSWWNFGSLLGLCLIVQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYAHMGAGLYYGSHAFRETWNIGVILL FTIMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAIVHLIFLHETGSNNPTGIPSDMDKIPFHPYYTIKDILGALLLILTLL ALTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LAFIPMLHTSKQRSMMFRPFSQSLFWVLVADLLTLTWIGGQPVEHPYMIVGQLASILYFL LILVLMPVASLIENKLMKW
S41832 S41832 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b blue whale mitochondrion blue whale mitochondrion Balaenoptera musculus Arnason, U. Gullberg, A. J. Mol. Evol. 371993312-322 Comparison between the complete mtDNA sequences of the blue and the fin whale, two species that can hybridize in nature. MUID94141932 S41832 DNA 1-379 EMBLX72204 NIDg414126 PIDNCAA51007.1 PIDg575318 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINDAFIDLPTPSNISSWWNFGSLLGLCLIVQILTGLFLAMHYTPDTM TAFSSVTHICRDVNYGWVIRYLHANGASMFFICLYAHMGRGLYYGSHAFRETWNIGVILL FTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIIMALAIVHLIFLHETGSNNPTGIPSDMDKIPFHPYYTIKDILGALLLILTLL MLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILV LALIPMLHTSKQRSMMFRPFSQFLFWVLVADLLTLTWIGGQPVEHPYVIVGQLASILYFL LILVLMPVTSLIENKLMKW
S43264 S43264 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Bryde's whale mitochondrion Bryde's whale mitochondrion Balaenoptera edeni Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43264 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75583 NIDg457766 PIDNCAA53259.1 PIDg578575 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIVNDAFVDLPTPSNISSWWNFGSLLGLCLITQILTGLFLAMHYTPDTT TAFSSVAHICRDVNYGWVIRYLHANGASMFFICLYAHMGRGLYYGSYAFRETWNIGVILL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALAMVHLIFLHETGSNNPTGIPSNMDKIPFHPYYTTKDILGALLLILTLL MLTLFVPDLLGDPDNYTPANPLSTPTHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILI LALIPMLHTSKQRSMMFRPFSQFLFWVLIADLLTLTWIGGQPVEHPYVIVGQFASILYFL LILVLMPVTSLIENKLMKW
S43270 S43270 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Physeter macrocephalus mitochondrion mitochondrion Physeter macrocephalus Arnason, U. Gullberg, A. Nature 3671994726-728 Relationship of baleen whales established by cytochrome b gene sequence comparison. MUID94150700 S43270 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX75589 NIDg457797 PIDNCAA53265.1 PIDg578930 the nucleotide sequence was submitted to the EMBL Data Library, November 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLMKIINNAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTT TAFSSITHICRDVNYGWTIRYLHANGASMFFICLYTHMGRGWYYGSYIFQETWNVGMMLL ITVMATAFVGYVLPWGQMSFWAATVITNLLSAIPYIGTTLVEWVWGGFSVDKATLTRFFT LHFILPFITLTLTMVHLLFLHETGSNNPTGIPSNMDKIPFHPYHTIKDTMGALLLILSLL TLTLFAPDLLGDPDNYTPANPLNTPTHIKPEWYFLFAYAILRSVPNKLGGVLALLLSILI LVFIPMLHTAKQRSMMFRPFSQFLFWTLIMDLLTLTWIGGQPVEHPYVTVGQLASILYFL LILILMPTASLIENKLLKW
S17420 S17420 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b collared peccary mitochondrion collared peccary mitochondrion Tayassu tajacu Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17420 translation not shown DNA 1-379 EMBLX56296 NIDg13874 PIDNCAA39743.1 PIDg578835 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLMKIINNTFIDLPTPSNISSWWNFGSLLGICLLLQILTGLFLAMHYTPDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLFIHVGRGLYYGSYLFLETWNIGVILL LTVMATAFMGYVLPWGQMSFWAATVITNLLSAIPYIGTDLVEWIWGGFSVDKATLTRFFA FHFILPFIITALVIVHLLFLHETGSNNPTGIPSNMDKIPFHPYYTIKDILGATLMILILL LLVLFSPDLLGDPDNYTPANPLNTPSHIKPEWYFLFAYAILRSIPNKLGGVLALALSILI LALVPALHTSKQRSMMFRPLSQLLFWMLVADFLTLTWIGSQPVEHPFIIIGQLASILYFL IILVLMPVANIIENNLLKW
S26163 S26163 S58453 03-Feb-1994 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b harbor seal mitochondrion harbor seal mitochondrion Phoca vitulina Arnason, U. Johnsson, E. J. Mol. Evol. 341992493-505 The complete mitochondrial DNA sequence of the harbor seal, Phoca vitulina. MUID92277666 S26163 DNA 1-379 EMBLX63726 NIDg13431 PIDNCAA45269.1 PIDg578776 Arnason, U. Bodin, K. Gullberg, A. Ledje, C. Mouchaty, S. J. Mol. Evol. 40199578-85 A molecular view of pinniped relationships with particular emphasis on the true seals. MUID95230701 S58453 preliminary nucleic acid sequence not shown translation not shown DNA 1-14,'D',16-189,'S',191-192,'A',194-213,'N',215-258,'A',260-299,'I',301-303,'V',305-349,'I',351-359,'M',361-379 EMBLX82306 NIDg693981 PIDNCAA57749.1 PIDg693982 the nucleotide sequence was submitted to the EMBL Data Library, October 1994 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINNSFIDLPTPSNISAWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYMHVGRGLYYGSYTFTETWNIGIILL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYVGTDLVQWIWGGFSVDKATLTRFFA FHFILPFVVLALDAVHLLFLHETGSNNPSGIMSDSDKIPFHPYYTIKDILGALLLILVLT LLVLFSPDLLGDPDNYIPPNPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILV LAIMPLLHTSKQRGMMFRPISQCLFWFLVADLLTLTWIGGQPVEHPYITVGQLASILYFT ILLVLMPIASIIENNILKW
S41847 S41847 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b gray seal mitochondrion gray seal mitochondrion Halichoerus grypus Arnason, U. Gullberg, A. Johnsson, E. Ledje, C. J. Mol. Evol. 371993323-330 The nucleotide sequence of the mitochondrial DNA molecule of the grey seal, Halichoerus grypus, and a comparison with mitochondrial sequences of other true seals. MUID94141933 S41847 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX72004 NIDg414757 PIDNCAA50889.1 PIDg578709 the nucleotide sequence was submitted to the EMBL Data Library, May 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLMKIINNSFIDLPTPSNISAWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSVTHICRDVNYGWIIRYLHANGASMFFICLYMHVGRGLYYGSYTFTETWNIGIILL FTIMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTGFFA FHFILPFVVLALAAVHLLFLHETGSNNPSGIMPDSDKIPFHPYYTIKDILGALLLILVLT LLVLFSPDLLGDPDNYIPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LAIVPLLHTSKQRGMMFRPISQCLFWLLVADLLTLTWIGGQPVEHPYITIGQLASILYFM ILLVLMPIASIIENNILKW
S41833 S41833 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Weddell seal mitochondrion Weddell seal mitochondrion Leptonychotes weddelli Arnason, U. Gullberg, A. Johnsson, E. Ledje, C. J. Mol. Evol. 371993323-330 The nucleotide sequence of the mitochondrial DNA molecule of the grey seal, Halichoerus grypus, and a comparison with mitochondrial sequences of other true seals. MUID94141933 S41833 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX72005 NIDg414771 PIDNCAA50890.1 PIDg578717 the nucleotide sequence was submitted to the EMBL Data Library, May 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLAKIINNSFIDLPTPSNISAWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSVTHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFTETWNIGIILL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFA FHFILPFVVSALAAVHLLFLHETGSNNPSGIPSDSDKIPFHPYYTIKDILGALLLILTLM LLVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALALSILI LAIIPLLHTSKQRGMMFRPISQCLFWLLVADLLTLTWIGGQPVEHPYITIGQLASILYFT ILLVLMPITSIIENNILKW
S41834 S41834 10-Sep-1999 10-Sep-1999 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Monachus schauinslandi mitochondrion mitochondrion Monachus schauinslandi Arnason, U. Gullberg, A. Johnsson, E. Ledje, C. J. Mol. Evol. 371993323-330 The nucleotide sequence of the mitochondrial DNA molecule of the grey seal, Halichoerus grypus, and a comparison with mitochondrial sequences of other true seals. MUID94141933 S41834 nucleic acid sequence not shown translation not shown DNA 1-379 EMBLX72209 NIDg414773 PIDNCAA51008.1 PIDg578719 the nucleotide sequence was submitted to the EMBL Data Library, May 1993 mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKTHPLAKIINNSLIDLPAPSNISMWWNFGSLLGICLILQILTGLFLAMHYTSDTT TAFSSITHICRDVNYGWIIRYMHANGASMFFICLYMHVGRGLYYGSYTFTETWNIGIILL LTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTDLVQWIWGGFSVDKATLTRFFA FHFIMPFMVLALAAVHLLFLHETGSNNPSGIPSNSDKIPFHPYYTIKDILGALLLILILM LLVLFSPDLLGDPDNYIPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LAIIPLLHTSKQRGMTFRPMSQCLFWLLAADLITLTWIGGQPVEYPYTTIGQLASILYFT IPLVLMPITSIIENNILKW
S22931 S22931 H33285 S21611 S70405 S70404 S21612 S21613 S21614 S21615 S21616 S21617 S21618 S21619 S21620 S21621 S21622 S21623 S21624 S21625 29-Jan-1993 26-Jul-1996 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b gray-crowned babbler mitochondrion gray-crowned babbler mitochondrion Pomatostomus temporalis Edwards, S.V. Arctander, P. Wilson, A.C. Proc. R. Soc. Lond. B Biol. Sci. 243199199-107 Mitochondrial resolution of a deep branch in the genealogical tree for perching birds. MUID91288587 S22931 translation not shown DNA 1-308 EMBLX60936 NIDg13395 PIDNCAA43271.1 PIDg13396 Kocher, T.D. Thomas, W.K. Meyer, A. Edwards, S.V. Paeaebo, S. Villablanca, F.X. Wilson, A.C. Proc. Natl. Acad. Sci. U.S.A. 8619896196-6200 Dynamics of mitochondrial DNA evolution in animals: amplification and sequencing with conserved primers. MUID89345630 H33285 translation not shown DNA 15,'A',17-94 GBM25688 NIDg343668 PIDNAAA32139.1 PIDg343669 Edwards, S.V. Wilson, A.C. submitted to the EMBL Data Library October1990 Phylogenetically informative length polymorphism and sequence variability in mitochondrial DNA of Australian songbirds (Pomatostomus). S21611 DNA 5-98 EMBLX54900 EMBLX54901 EMBLX54902 EMBLX54903 EMBLX54904 EMBLX54905 EMBLX54899 EMBLX54898 EMBLX54897 EMBLX54896 EMBLX54895 EMBLX54894 EMBLX54893 EMBLX54892 EMBLX54891 Edwards, S.V. Wilson, A.C. Genetics 1261990695-711 Phylogenetically informative length polymorphism and sequence variability in mitochondrial DNA of Australian songbirds (Pomatostomus). MUID91065505 S70405 DNA 5-98 EMBLX54891 EMBLX54906 EMBLX54892 EMBLX54893 EMBLX54894 EMBLX54895 EMBLX54896 EMBLX54897 EMBLX54898 EMBLX54899 EMBLX54900 EMBLX54901 EMBLX54902 EMBLX54903 EMBLX54904 EMBLX54905 S70404 translation not shown DNA 5-13,'I',15-98 EMBLX54885 NIDg13329 PIDNCAA38658.1 PIDg13330 EMBLX54914 NIDg13331 PIDg13332 individual 23C cyb mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology (fragment) 1-307 domain cytochrome b6 homology (fragment) 1-98 domain transmembrane 4-20 predicted domain transmembrane 49-67 predicted domain transmembrane 85-101 predicted domain transmembrane 146-168 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 189-307 domain transmembrane 197-213 predicted domain transmembrane 256-272 predicted binding-site heme iron (His) (axial ligands) (low potential) 51,150 predicted binding-site heme iron (His) (axial ligands) (high potential) 65,164 predicted 308 fragment /FGLLLGICLIVQIVTGLLLAAHYTADTSLAFASVAHMCRNVQFGWLIRNLHANGASFFF ICIYLHIGRGLYYGSYLNKETWNIGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFS AIPYIGQTLVEWAWGGFSVDNPTLTRFFALHFLLPFVIAGLTLVHLTFLHETGSNNPLGI PSDCDKIPFHPYYSTKDMLGFALMLIPLITLALFSPNLLGDPENFTPANPLATPPHIKPE WYFLFAYAILRSIPNKLGGVLALAASVLVLFLIPLLHTSKARSMTFRPLSQILFWTLVAN LLVLTWVGS/
S17406 S17406 29-Jan-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Arabian camel mitochondrion Arabian camel mitochondrion Camelus dromedarius Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17406 translation not shown DNA 1-379 EMBLX56281 NIDg12854 PIDNCAA39728.1 PIDg578693 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLLKIMNDAFIDLPAPSNISSWWNFGSLLGVCLIMQILTGLFLAMHYTSDTT TAFSSVAHICRDVNYGWIIRYLHANGASMFFICLYIHVGRGLYYGSYTFSETWNVGMVLL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFILPFIITALVAVHLLFLHETGSNNPTGISSDMDKIPFHPYYTIKDILGALLLMLALL ILVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSILI LAFIPALHTSKQRSMTFRPISQCLFWVLVADLLTLTWIGGQPVEPPFIMIGQVASILYFS LILILMPVAGIIENRILKW
S33572 S33572 03-Feb-1994 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b southern African porcupine mitochondrion southern African porcupine mitochondrion Hystrix africaeaustralis Ma, D.P. Zharkikh, A. Graur, D. VandeBerg, J.L. Li, W.H. J. Mol. Evol. 361993327-334 Structure and evolution of opossum, guinea pig, and porcupine cytochrome b genes. MUID93301932 S33572 DNA 1-379 EMBLX70674 NIDg14012 PIDNCAA50010.1 PIDg602073 residue 1 and the corresponding nucleotide sequence are not shown cob mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 379 complete MTNIRKSHPLLKIINHSFIDLPTPSNISTWWNFGSLLGACLIIQILTGLFLAMHYTAYTT TAFSSVAHICRDVNYGWLIRYLHANGASMFFICLYLHVGRGLYYGSYMFTETWNIGILLL FTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA FHFSLPFIITALVLVHLLFLHETGSNNPSGIDSNSDKIPFHPYYTIKDILGLLLMLTALL ILVLFSPDLLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALIFSILI LAIIPLLHTSKQRSMLFRPFSQCLFWILAANLLILTWIGGQPVEHPYITIGQLASISYFS ILLIIMPLTSIMENKLLKW
S33573 S33573 03-Feb-1994 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b short-tailed opossum (Monodelphis domestica) mitochondrion mitochondrion Monodelphis domestica Ma, D.P. Zharkikh, A. Graur, D. VandeBerg, J.L. Li, W.H. J. Mol. Evol. 361993327-334 Structure and evolution of opossum, guinea pig, and porcupine cytochrome b genes. MUID93301932 S33573 DNA 1-382 EMBLX70673 NIDg14019 PIDNCAA50009.1 PIDg14020 residue 1 and the corresponding nucleotide sequence are not shown cob mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 382 complete MTNLRKNYPLMKIINHSFIDLPAPSNISAWWNFGSLLGMCLIIQILTGLFLAMHYTSDTL TAFSSVAHICRDVNYGWLIRNLHANGASMFFMCLFLHVGRGIYYGSYLYKETWNIGVILM LTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGNTLVEWIWGGFSVDKATLTRFFA FHFILPFIILALVIVHLLFLHETGSNNPTGINPNSDKIPFHPYYTIKDALGLILMLLILM SLAMFSPDMLGNPDNFTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLASLLI LLIIPLLHTSKQRSLMFRPISQIMFWLLVANLLTLTWIGGQPVEQPFIIIGQLASTLYFS LIIIFMPLAGMYEDHLLEPKFP
S10198 S10198 31-Dec-1990 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b chicken mitochondrion chicken mitochondrion Gallus gallus Desjardins, P. Morais, R. J. Mol. Biol. 2121990599-634 Sequence and gene organization of the chicken mitochondrial genome. A novel gene order in higher vertebrates. MUID90230301 S10198 DNA 1-380 EMBLX52392 NIDg12960 PIDNCAA36636.1 PIDg12972 cytB mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 12-340 domain cytochrome b6 homology 12-210 domain transmembrane 37-53 predicted domain transmembrane 82-100 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 84,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 98,197 predicted 380 complete MAPNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVCLMTQILTGLLLAMHYTADT SLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVIL LLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTLVEWAWGGFSVDNPTLTRFF ALHFLLPFAIAGITIIHLTFLHESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPF LTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVL ILFLIPFLHKSKQRTMTFRPLSQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYF TILLILFPTIGTLENKMLNY
S17412 T45562 S17412 29-Jan-1993 03-Mar-2000 09-Jun-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b [similarity] African elephant mitochondrion African elephant mitochondrion Loxodonta africana Hauf, J. Waddell, P.J. Chalwatzis, N. Joger, U. Zimmermann, F.K. submitted to the EMBL Data Library February1998 The complete mitochondrial genome sequence of the African elephant (Loxodonta africana), phylogenetic relationships of Proboscidea to other mammals and D-loop heteroplasmy. T45562 translated from GB/EMBL/DDBJ DNA 1-378 EMBLAJ224821 PIDNCAA12150.1 cell type: whole blood cells Irwin, D.M. Kocher, T.D. Wilson, A.C. J. Mol. Evol. 321991128-144 Evolution of the cytochrome b gene of mammals. MUID91178817 S17412 translation not shown DNA 1-2,'D',4-26,'M',28-149,'L',151-248,'H',250-256,'TL',259,'N',261-263,'N',265,'P',267-321,'LCAYC',326-378 EMBLX56285 NIDg13070 PIDNCAA39732.1 PIDg13071 cytb mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 378 complete MTHIRKSHPLLKIINKSFIDLPTPSNISTWWNFGSLLGACLITQILTGLFLAMHYTPDTM TAFSSMSHICRDVNYGWIIRQLHSNGASIFFLCLYTHIGRNIYYGSYLYSETWNTGIMLL LITMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGTNLVEWIWGGFSVDKATLNRFFA LHFILPFTMIALAGVHLTFLHETGSNNPLGLTSDSDKIPFHPYYTIKDFLGLLILILLLL LLALLSPDMLGDPDNYMPADPLNTPLHIKPEWYFLFAYAILRSVPNKLGGVLALLLSILI LGLMPLLHTSKHRSMMLRPLSQVLFWTLTMDLLTLTWIGSQPVEYPYIIIGQMASILYFS IILAFLPIAGVIENYLIK
CBXL A23955 A00155 28-Feb-1986 09-Sep-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b African clawed frog mitochondrion African clawed frog mitochondrion Xenopus laevis Dunon-Bluteau, D. Volovitch, M. Brun, G. Gene 36198565-78 Nucleotide sequence of a Xenopus laevis mitochondrial DNA fragment containing the D-loop, flanking tRNA genes and the apocytochrome b gene. MUID86056961 A23955 DNA 1-380 GBM10188 the authors state that this sequence corrects that which was reported in reference A00155 Roe, B.A. Ma, D.P. Wilson, R.K. Wong, J.F.H. J. Biol. Chem. 26019859759-9774 The complete nucleotide sequence of the Xenopus laevis mitochondrial genome. MUID85261388 A00155 DNA 1-71,'F',73-77,'L',79-87,'L',89-153,'K',155-164,'SL',167-284,'M',287-333,'L',335-380 GBM10217 GBX02890 NIDg343717 PIDNAAA66470.1 PIDg807694 cob mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 12-340 domain cytochrome b6 homology 12-210 domain transmembrane 37-53 predicted domain transmembrane 82-100 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 84,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 98,197 predicted 380 complete MAPNIRKSHPLIKIINNSFIDLPTPSNISSLWNFGSLLGVCLIAQIITGLFLAMHYTADT SMAFSSVAHICRDVNYGWLIRNLHANGASFFFICIYLHIGRGLYYGSFLYKETWNIGVIL LFLVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGNVLVQWIWGGFSVDNATLTRFF AFHFLLPFIIAGASILHLLFLHETGSTNPTGLNSDPDKVPFHPYFSYKDLLGFLIMLTAL TLLAMFSPNLLGDPDNFTPANPLITPPHIKPEWYFLFAYAILRSIPNKLGGVLALVLSIL ILALMPLLHTSKQRSLMFRPFTQIMFWALVADTVILTWIGGQPVEDPYTMIGQLASVIYF SIFIIMFPLMGWVENKLLNW
S36011 S36011 E44651 31-Dec-1993 24-Jul-1998 23-Mar-2001
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b common carp mitochondrion common carp mitochondrion Cyprinus carpio Chang, Y.S. Huang, F.L. submitted to the EMBL Data Library July1991 The cDNA and primary structure of pregrowth hormones of three species of Cyprinadae: silver carp, bighead carp and grass carp. S36011 DNA 1-380,'C' EMBLX61010 NIDg436882 GenBank entry MICCCG PID:g436884 terminates with a UGC Cys codon Chang, Y.S. Huang, F.L. Lo, T.B. J. Mol. Evol. 381994138-155 The complete nucleotide sequence and gene organization of carp (Cyprinus carpio) mitochondrial genome. MUID94223691 E44651 nucleic acid sequence not shown not compared with conceptual translation DNA 1-301,'I',303-380 EMBLX61010 NIDg436882 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 380 complete MASLRKTHPLIKIANDALVDLPTPSNISAWWNFGSLLGLCLITQILTGLFLAMHYTSDIS TAFSSVTHICRDVNYGWLIRNVHANGASFFFICIYMHIARGLYYGSYLYKETWNIGVVLL LLVMMTAFVGYVLPWGQMSFWGATVITNLLSAVPYMGDMLVQWIWGGFSVDNATLTRFFA FHFLLPFVIAAATIIHLLFLHETGSNNPIGLNSDADKVSFHPYFSYKDLLGFVIMLLALT LLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILV LMVVPLLHTSKQRGLTFRPITQFLFWTLVADMIILTWIGGMPVEHPFIIIGQIASVLYFA LFLIFMPLAGWLENKALKWA
S35473 S35473 S60283 03-Feb-1994 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b hillstream loach (Crossostoma lacustre) mitochondrion mitochondrion Crossostoma lacustre Tzeng, C.S. Hui, C.F. Shen, S.C. Huang, P.C. Nucleic Acids Res. 2019924853-4858 The complete nucleotide sequence of the Crossostoma lacustre mitochondrial genome: conservation and variations among vertebrates. MUID93027205 S35473 nucleic acid sequence not shown translation not shown DNA 1-398 EMBLM91245 the nucleotide sequence was submitted to the EMBL Data Library, November 1992 Tzeng, C.S. Shen, S.C. Huang, P.C. Bull. Inst. Zool. Acad. Sin. 29199011-19 Mitochondrial DNA identity of Crossostoma (Homalopteridae, Pisces) from two river systems of the same geographical origin. S60283 nucleic acid sequence not shown translation not shown DNA 1-380 GBM91245 NIDg1381122 PIDNAAB96823.1 PIDg336716 mitochondrion SGC1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 398 complete MASLRKTHPLIKIANDALVDLPAPSNISVWWNFGSLLGLCLITQILTGLFLAMHYTSDIS TAFSSVAHICRDVNYGWLIRNIHANGASFFFICLYLHIARGLYYGSYLYKETWNIGVVLF LLVMMTAFVGYVLPWGQMSFWGATVITNLLSAVPYVGDMLVQWIWGGFSVDNATLTRFFA FHFLFPFIVAAVTILHLLFLHETGSNNPAGLNSDADKISFHPYFSYKDLLGFVVMLLGLT TLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILV LMVVPVLHTSKQRGLTFRPATQFLFWTLVADMIILTWIGGMPVEHPYIIIGQIASILYFA LFLILIPLAGWLENKALEWVCPSSLVWKHRSCNPKIGG
S04840 S04840 20-Apr-2000 20-Apr-2000 20-Apr-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b [similarity] white sturgeon mitochondrion white sturgeon mitochondrion Acipenser transmontanus Brown, J.R. Gilbert, T.L. Kowbel, D.J. O'Hara, P.J. Buroker, N.E. Beckenbach, A.T. Smith, M.J. Nucleic Acids Res. 1719894389 Nucleotide sequence of the apocytochrome B gene in white sturgeon mitochondrial DNA. MUID89296501 S04840 DNA 1-380 EMBLX14944 NIDg12749 PIDNCAA33076.1 PIDg12750 the termination resulting from transcript polyadenylation is shown mitochondrion SGC1 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 11-339 domain cytochrome b6 homology 11-209 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 117-133 predicted domain transmembrane 178-200 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 221-339 domain transmembrane 229-245 predicted domain transmembrane 288-304 predicted domain transmembrane 323-343 predicted domain transmembrane 353-369 predicted binding-site heme iron (His) (axial ligands) (low potential) 83,182 predicted binding-site heme iron (His) (axial ligands) (high potential) 97,196 predicted 380 complete MANIRKTHPLLKIINGAFIDLPTPSNISVWWNFGSLLGLCLITQILTGLFLAMHYTADIS TAFSSVAHICRDVNYGWLIRNIHANGASFFFICLYLHVARGMYYGSYLQKETWNIGVILL LLTMMTAFVGYVLPWGQMSFWGATVITNLLSAFPDIGDTLVQWIWGGFSVDNATLTRFFA FHFLLPFVIAGASMIHLLFLHQTGSNNPTGLNSDADKVTFHPYFSYKDLFGFTLMLVGLT SVALFSPNLLGDPDNFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALLFSILV LMLVPMLHTSKQRGNTFRPLSQILFWALVADMLVLTWIGGQPVEHPFVLIGQVASTVYFA LFLIALPLTGWLENKALNWN
S01190 S01190 S01742 28-Feb-1990 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b fruit fly (Drosophila melanogaster) mitochondrion mitochondrion Drosophila melanogaster Garesse, R. Genetics 1181988649-663 Drosophila melanogaster mitochondrial DNA: gene organization and evolutionary considerations. MUID88212147 S01190 DNA 1-378 GBM37275 EMBLY00610 NIDg336819 PIDNAAA69714.1 PIDg552530 Garesse, R. submitted to the EMBL Data Library February1988 S01742 DNA 1-257,'YSANSFSNT',267-378 EMBLY00610 FlyBasemt:Cyt-b FlyBaseFBgn0013678 mitochondrion SGC4 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 12-340 domain cytochrome b6 homology 12-210 domain transmembrane 37-53 predicted domain transmembrane 82-100 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 84,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 98,197 predicted 378 complete MNKPLRNSHPLFKIANNALVDLPAPINISSWWNFGSLLGLCLIIQILTGLFLAMHYTADI NLAFYSVNHICRDVNYGWLLRTLHANGASFFFICIYLHVGRGIYYGSYKFTPTWLIGVII LFLVMGTAFMGYVLPWGQMSFWVATVITNLLYAIPYLGMDLVQWLWGGFAVDNATLTRFF TFHFILPFIVLAMTMIHLLFLHQTGSNNPIGLNSNIDKIPFHPYFTFKDIVGFIVMIFIL ISLVLISPNLLGDPDNFIPATPLVTPAHIQPEWYFLFAYAILRSIPNKLGGVIALVLSIA ILMILPFYNLSKFRGIQFYPINQVMFWSMLVTVILLTWIGARPVEEPYVLIGQILTVVYF LYYLVNPLITKWWDNLLN
C30020 C30020 L25797 05-Jun-1987 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b fruit fly (Drosophila yakuba) mitochondrion mitochondrion Drosophila yakuba Clary, D.O. Wolstenholme, D.R. J. Mol. Evol. 221985252-271 The mitochondrial DNA molecule of Drosophila yakuba: nucleotide sequence, gene organization, and genetic code. MUID86089137 C30020 DNA 1-378 GBX03240 NIDg12923 PIDNCAA26996.1 PIDg12935 FlyBaseDyak/mt:Cyt-b FlyBaseFBgn0013182 mitochondrion SGC4 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 12-340 domain cytochrome b6 homology 12-210 domain transmembrane 37-53 predicted domain transmembrane 82-100 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 84,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 98,197 predicted 378 complete MHKPLRNSHPLFKIANNALVDLPAPINISSWWNFGSLLGLCLIIQILTGLFLAMHYTADV NLAFYSVNHICRDVNYGWLLRTLHANGASFFFICIYLHIGRGIYYGSYLFTPTWLVGVII LFLVMGTAFMGYVLPWGQMSFWGATVITNLLSAIPYLGMDLVQWLWGGFAVDNATLTRFF TFHFILPFIVLAMTMIHLLFLHQTGSNNPIGLNSNIDKIPFHPYFTFKDIVGFIVMIFIL ISLVLISPNLLGDPDNFIPANPLVTPAHIQPEWYFLFAYAILRSIPNKLGGVIALVLSIA ILMILPFYNLSKFRGIQFYPINQILFWSMLVTVILLTWIGARPVEEPYVLIGQILTIIYF LYYLINPLVTKWWDNLLN
D34285 D34285 H26510 06-Jul-1990 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b sea urchin (Paracentrotus lividus) mitochondrion common urchin mitochondrion Paracentrotus lividus Cantatore, P. Roberti, M. Rainaldi, G. Gadaleta, M.N. Saccone, C. J. Biol. Chem. 264198910965-10975 The complete nucleotide sequence, gene organization, and genetic code of the mitochondrial genome of Paracentrotus lividus. MUID89291831 D34285 DNA 1-380 GBJ04815 NIDg342913 PIDNAAA68145.1 PIDg854698 Cantatore, P. Roberti, M. Morisco, P. Rainaldi, G. Gadaleta, M.N. Saccone, C. Gene 53198741-54 A novel gene order in the Paracentrotus lividus mitochondrial genome. MUID87248108 H26510 preliminary not compared with conceptual translation DNA 81,'K',83-85,'K',87-98,'M',100-106;'CDEV',112-114,'K',116-124,'M',126-129,'M',131-137,'Q',139-147,'T',149-151,'S',153,'I',155,'YY',158-182;352-353,'M',355-363,'M',365-374,'K',376-377,'M',379-380 mitochondrion SGC8 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 12-340 domain cytochrome b6 homology 12-210 domain transmembrane 37-53 predicted domain transmembrane 82-100 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 84,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 98,202 predicted 380 complete MLGPLRKEHPIFRILNSTFVDLPLPSNLSIWWNFGSLLGLCLITQILTGLFLAMHYTADI SLAFSSASHICRDVNYGWLLRNVHANGASLFFICMYCHIGRGLYYGGSNKIETWNVGVIL FLVTVLTAFVGYVLVWGRMSFWAATVIANLVTAVPCVGTTIVQWLWGGFSVDNATLTRFF AFHFLFPFIIAALAIIDLVFLHNSGANNPVGLNSNYDKAPFHIYYTTKDTVGFIALIAAL FVLALLFPCALNDPENFIPANPLSHPPHIQPEWYFLFAYAILRSIPNKLGGVIALVAAIL VLFLMPLLNTSKNESNSFRPLSQATFWILVATFFVLTWIGSQPVEQPFVLIGQIASLLYF SLFIFGFPLVSSLENKMIFS
S01511 S01511 01-Dec-1989 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b sea urchin (Strongylocentrotus purpuratus) mitochondrion purple urchin mitochondrion Strongylocentrotus purpuratus Jacobs, H.T. Elliott, D.J. Math, V.B. Farquharson, A. J. Mol. Biol. 2021988185-217 Nucleotide sequence and gene organization of sea urchin mitochondrial DNA. MUID89011951 S01511 DNA 1-385 EMBLX12631 cytb mitochondrion SGC8 ATA the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 17-345 domain cytochrome b6 homology 17-215 domain transmembrane 42-58 predicted domain transmembrane 87-105 predicted domain transmembrane 123-139 predicted domain transmembrane 184-206 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 227-345 domain transmembrane 235-251 predicted domain transmembrane 294-310 predicted domain transmembrane 329-349 predicted domain transmembrane 359-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 89,188 predicted binding-site heme iron (His) (axial ligands) (high potential) 103,202 predicted 385 complete MSINIMAAPLRKEHPIFRILNSTFVDLPLPSNLSIWWNSGSLLGLCLVVQILTGIFLAMH YTADITLAFSSVMHILRDVNYGWFLRYVHANGVSLFFICMYCHIGRGLYYGSYNKIETWN VGVILFLVTILTAFMGYVLVWGQMSFWAATVITNLVSAIPYIGTIIVQWLWGGFSVDNAT LTRFFPFHFLFPFIIAALAVIHLVFLHNSGANNPFAFNSNYDKAPFHIYFTTKDTVGFIL LVAALFSLALLFPGALNDPENFIPANPLVTPPHIQPEWYFLFAYAILRSIPNKLGGVIAL VAAILVLFLMPLLNTSKNESNSFRPLSQAAFWLLVAHLFILTWIGSQPVEYPYVLLGQVA SVLYFSLFIFGFPIVSSIENKIIFS
S26031 S26031 S25804 12-Feb-1993 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Caenorhabditis elegans mitochondrion mitochondrion Caenorhabditis elegans Okimoto, R. Macfarlane, J.L. Clary, D.O. Wolstenholme, D.R. Genetics 1301992471-498 The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum. MUID92201635 S26031 DNA 1-370 EMBLX54252 NIDg13988 PIDNCAA38156.1 PIDg559501 the authors translated the initiation codon TTG for residue 1 as Leu Okimoto, R. Macfarlane, J.L. Wolstenholme, D.R. Nucleic Acids Res. 1819906113-6118 Evidence for the frequent use of TTG as the translation initiation codon of mitochondrial protein genes in the nematodes, Ascaris suum and Caenorhabditis elegans. MUID91045077 S25804 DNA 1-25 EMBLX54252 the authors translated the initiation codon TTG for residue 1 as Leu cytB mitochondrion SGC4 TTG the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane protein metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain domain cytochrome b homology 8-332 domain cytochrome b6 homology 8-206 domain plastoquinol--plastocyanin reductase 17K protein homology 218-332 binding-site heme iron (His) (axial ligands) (low potential) 80,179 predicted binding-site heme iron (His) (axial ligands) (high potential) 94,198 predicted 370 complete MKINNSLLNFVNGMLVTLPSSKTLTLSWNFGSMLGMVLIFQILTGTFLAFYYTPDSLMAF STVQYIMYEVNFGWVFRIFHFNGASLFFIFLYLHIFKGLFFMSYRLKKVWMSGLTIYLLV MMEAFMGYVLVWAQMSFWAAVVITSLLSVIPIWGPTIVTWIWSGFGVTGATLKFFFVLHF LLPWAILVIVLGHLIFLHSTGSTSSLYCHGDYDKVCFSPEYLGKDAYNIVIWLLFIVLSL IYPFNLGDAEMFIEADPMMSPVHIVPEWYFLFAYAILRAIPNKVLGVIALLMSIVTFYFF ALVNNYTSCLTKLNKFLVFMFIISSTILSWLGQCTVEDPFTILSPLFSFIYFGLAYLMLF IFMSSKLLFK
S26019 S26019 S25792 12-Feb-1993 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b pig roundworm mitochondrion pig roundworm mitochondrion Ascaris suum Okimoto, R. Macfarlane, J.L. Clary, D.O. Wolstenholme, D.R. Genetics 1301992471-498 The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum. MUID92201635 S26019 DNA 1-365 EMBLX54253 NIDg13971 PIDNCAA38168.1 PIDg559493 the authors translated the initiation codon ATT for residue 1 as Ile Okimoto, R. Macfarlane, J.L. Wolstenholme, D.R. Nucleic Acids Res. 1819906113-6118 Evidence for the frequent use of TTG as the translation initiation codon of mitochondrial protein genes in the nematodes, Ascaris suum and Caenorhabditis elegans. MUID91045077 S25792 DNA 1-20 EMBLX54253 the authors translated the initiation codon ATT for residue 1 as Ile cytB mitochondrion SGC4 ATT the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane protein metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain domain cytochrome b homology 3-327 domain cytochrome b6 homology 3-201 domain plastoquinol--plastocyanin reductase 17K protein homology 213-327 binding-site heme iron (His) (axial ligands) (low potential) 75,174 predicted binding-site heme iron (His) (axial ligands) (high potential) 89,188 predicted 365 complete MKLDFVNSMVVSLPSSKVLTYGWNFGSMLGMVLGFQILTGTFLAFYYSNDGALAFLSVQY IMYEVNFGWIFRVLHFNGASLFFIFLYLHLFKGLFFMSYRLKKVWVSGIVILLLVMMEAF MGYVLVWAQMSFWASVVITSLLSVIPVWGFAIVTWIWSGFTVSSATLKFFFVLHFLVPWG LLLLVLLHLVFLHETGSTSKLYCHGDYDKVCFYPEYWVKDFLNVVVWFVFIFFSLGYPFL LGDPEMFIESDPMMSPVHIVPEWYFLFAYAILRAIPNKVLGVVSLFASILVLVVFVLVNN YVSVMSKLNKFLVFVFIFVLVVLSWLGQCLVEDPFVFLSMVFSFLYFFVIFLLFLVYYFA GRVFM
CBZM A00156 04-Dec-1986 30-Jun-1992 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b maize mitochondrion maize mitochondrion Zea mays Dawson, A.J. Jones, V.P. Leaver, C.J. EMBO J. 319842107-2113 The apocytochrome b gene in maize mitochondria does not contain introns and is preceded by a potential ribosome binding site. A00156 DNA 1-388 EMBLX00789 NIDg13904 PIDNCAA25367.1 PIDg13905 the authors translated the codon CGG for residue 239 as Trp, assuming a special genetic code for plant mitochondria cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 16-346 domain cytochrome b6 homology 16-216 domain transmembrane 41-57 predicted domain transmembrane 86-104 predicted domain transmembrane 124-140 predicted domain transmembrane 185-207 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 228-346 domain transmembrane 236-252 predicted domain transmembrane 295-311 predicted domain transmembrane 330-350 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 88,189 predicted binding-site heme iron (His) (axial ligands) (high potential) 102,203 predicted 388 complete MTIRNQRFSLLKQPIYSTLNQHLIDYPTPSNLSYWWGFGCLAGICLVIQIVTGVFLAMHY TPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFLIVVHLHIFRGLYHASYSSPREFVW CLGVVIFLLMIVTAFIGYVPPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNA TLNRFFSLHHLLPLILAGASLLHLAALHQYGSNNPLGVHSEMDKIASYPYFYVKDLVGRV ASAIFFSIWIFFAPNVLGHPDNYIPANPMPTPPHIVPEWYFLPIHAILRSIPDKAGGVAA IAPVFISLLALPFFKEMYVRSSSFRPIHQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQI SSFFFFLFFAITPIPGRVGRGIPKYYTE
CBRZ JQ0164 S20659 S07874 30-Jun-1992 30-Jun-1992 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b rice mitochondrion rice mitochondrion Oryza sativa Kaleikau, E.K. Andre, C.P. Doshi, B. Walbot, V. Nucleic Acids Res. 181990372 Sequence of the rice mitochondrial gene for apocytochrome b. MUID90221830 JQ0164 DNA 1-397 EMBLX17064 NIDg13214 PIDNCAA34910.1 PIDg13215 strain IR36 Koh-ichi, K. submitted to the EMBL Data Library June1990 S20659 DNA 1-27,'T',29-30,'N',32-58,'H',60-395,'V',397 EMBLX53710 NIDg13202 PIDNCAA37747.1 PIDg13203 cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 16-346 domain cytochrome b6 homology 16-216 domain transmembrane 41-57 predicted domain transmembrane 86-104 predicted domain transmembrane 124-140 predicted domain transmembrane 185-207 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 228-346 domain transmembrane 236-252 predicted domain transmembrane 295-311 predicted domain transmembrane 330-350 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 88,189 predicted binding-site heme iron (His) (axial ligands) (high potential) 102,203 predicted 397 complete MTIRNQRFSLLKQPIYSTLNQHLIDYPLPSILSYWWGFGSLAGICLVIQIVTGVFLAMNH TPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFLIVVHLHIFRGLYHASYSSPREFVW CLGVVIFLLMIVTAFIGYVPPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNA TLNRFFSLHHLLPLILVGASLLHLAALHQYGSNNPLGVHSEMDKIASYPYFYVKDLVGRV ASAIFFSIWIFFAPNVLGHPDNYIPANPMPTPPHIVPEWYFLPIHAILRSIPDKAGGVAA IAPVFISLLALPFFKEMYVRSSSFRPIHQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQI PSFFFFLFFAITPIPGRVGRGIPKYYTDETHRTGSFS
A22931 A22931 S36920 20-Aug-1987 24-Feb-1995 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b wheat mitochondrion common wheat mitochondrion Triticum aestivum Boer, P.H. McIntosh, J.E. Gray, M.W. Bonen, L. Nucleic Acids Res. 1319852281-2292 The wheat mitochondrial gene for apocytochrome b: absence of a prokaryotic ribosome binding site. MUID85215614 A22931 DNA 1-59,'H',61-95,'L',97-99,'H',101-108,'H',110-119,'R',121-139,'P',141-189,'H',191-193,'L',195-226,'S',228-238,'R',240-241,'S',243-269,'P',271-284,'H',286-302,'P',304-327,'H',329-360,'P',362-374,'P',376-398 EMBLX02352 NIDg13699 PIDNCAA26207.1 PIDg13700 the authors translated the codon CGG for residue 239 as Trp, assuming a special genetic code for plant mitochondria the differences between the sequences from reference A22931 and S36919 at positions 60, 96, 100, 109, 120, 140, 190, 194, 227, 239, 242, 270, 285, 303, 328, 361, and 375 are due to RNA editing Zanlungo, S. Begu, D. Quinones, V. Araya, A. Jordana, X. Curr. Genet. 241993344-348 RNA editing of apocytochrome b (cob) transcripts in mitochondria from two genera of plants. MUID94073991 S36920 not compared with conceptual translation mRNA 13-23;55-65;92-112;115-125;135-145;184-199;223-245;266-274;280-289;299-306,'C';323-333;357-366;370-380;382-398 cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain RNA editing transmembrane protein domain cytochrome b homology 16-346 domain cytochrome b6 homology 16-216 domain transmembrane 41-57 predicted domain transmembrane 86-104 predicted domain transmembrane 124-140 predicted domain transmembrane 185-207 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 228-346 domain transmembrane 236-252 predicted domain transmembrane 295-311 predicted domain transmembrane 330-350 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 88,189 predicted binding-site heme iron (His) (axial ligands) (high potential) 102,203 predicted 398 complete MTIRNQRFSLLKQPIYSTLNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHY TPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHIFRGLYYASYSSPREFVW CLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNA TLNRFFSLHYLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDKIAFYPYFYVKDLVGWV AFAIFFSIWIFFAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKAGGVAA IALVFISLLALPFFKEMYVRSSSFRPIYQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQI SSVFFFLFFAITPILGRVGRGIPKYYTDETHRTGSFWP
CBOBE S20141 S20142 S03156 30-Jun-1992 31-Dec-1992 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b evening primrose mitochondrion evening primrose mitochondrion Oenothera villaricae Schuster, W. Ternes, R. Knoop, V. Hiesel, R. Wissinger, B. Brennicke, A. Curr. Genet. 201991397-404 Distribution of RNA editing sites in Oenothera mitochondrial mRNAs and rRNAs. MUID92224283 S20141 mRNA 1-394 the authors translated the codon TTC for residue 97 as Tyr S20142 not compared with conceptual translation DNA 1-18,'T',20-96,'L',98-100,'H',102-103,'I',105-107,'H',109-120,'R',122-136,'T',138-189,'H',191-285,'H',287-303,'P',305-328,'H',330-361,'P',363-394 Schuster, W. Brennicke, A. Curr. Genet. 91985157-163 TGA-Termination codon in the apocytochrome b gene from Oenothera mitochondria. S03156 DNA 1-18,'T',20-96,'L',98-100,'H',102-103,'I',105-107,'H',109-136,'T',138-189,'H',191-285,'H',287-303,'P',305-328,'H',330-361,'P',363-394 EMBLX07126 the authors translated the codon ATA for residue 292 as His the authors translated the codon CGG for residue 121 as Trp, assuming a special genetic code for plant mitochondria cob cytB mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain RNA editing transmembrane protein domain cytochrome b homology 17-347 domain cytochrome b6 homology 17-217 domain transmembrane 42-58 predicted domain transmembrane 87-105 predicted domain transmembrane 125-141 predicted domain transmembrane 186-208 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 229-347 domain transmembrane 237-253 predicted domain transmembrane 296-312 predicted domain transmembrane 331-351 predicted domain transmembrane 361-376 predicted binding-site heme iron (His) (axial ligands) (low potential) 89,191 predicted binding-site heme iron (His) (axial ligands) (high potential) 103,204 predicted 394 complete MATIRNQRFSLLKQPISSILNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMH YTPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHTFRGLYYASYSSPREFV WCLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDN ATLNRFFSLYHLLPFILVGASLLHLAALHQYGSSNPLGVHSEMDKISFYPYFYVKDLVGW VAFAIFFSIWIFYAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKAGGVA AIALVFICLLALPFFKDMYVRSSSFRPIYQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQ ISSIVFFLFFAITPILGRVGRGIPNSYTDETDHT
S38960 S38960 S36912 10-Mar-1994 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Arabidopsis thaliana mitochondrion mouse-ear cress mitochondrion Arabidopsis thaliana Brandt, P. Unseld, M. Eckert-Ossenkopp, U. Brennicke, A. Curr. Genet. 241993330-336 An rps14 pseudogene is transcribed and edited in Arabidopsis mitochondria. MUID94073989 S38960 not compared with conceptual translation mRNA 1-393 S36912 DNA 1-95,'L',97-108,'H',110-189,'H',191-284,'H',286-302,'P',304-327,'H',329-361,'P',363-393 EMBLX67736 NIDg402960 PIDNCAA47966.1 PIDg402962 differences from the sequence translated from mRNA are due to RNA editing cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain RNA editing transmembrane protein domain cytochrome b homology 16-346 domain cytochrome b6 homology 16-216 domain transmembrane 41-57 predicted domain transmembrane 86-104 predicted domain transmembrane 124-140 predicted domain transmembrane 185-207 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 228-346 domain transmembrane 236-252 predicted domain transmembrane 295-311 predicted domain transmembrane 330-350 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 88,189 predicted binding-site heme iron (His) (axial ligands) (high potential) 102,203 predicted 393 complete MTIRNQRFSLLKQPISSTLNQHLVDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHY TPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHIFRGLYYASYSSPREFVW CLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNA TLNRFFSLHYLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDKIAFYPYFYVKDLVGWV AFAIFFSIWIFYAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKAGGVAA IALVFICLLALPFFKSMYVRSSSFRPIYQGMFWLLLADCLLLGWIGCQPVEAPFVTIGQI SSLVFFLFFAITPILGRVGRGIPNSYTDETDHT
CBPOM S17427 S36919 S28874 31-Dec-1992 24-Feb-1995 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b potato mitochondrion potato mitochondrion Solanum tuberosum Zanlungo, S. Litvak, S. Jordana, X. Plant Mol. Biol. 171991527-530 Isolation and nucleotide sequence of the potato mitochondrial gene for apocytochrome b. MUID91355947 S17427 DNA 1-17,'T',19-99,'H',101-108,'H',110-119,'R',121-189,'H',191-226,'S',228-284,'H',286-302,'P',304-327,'H',329-361,'P',363-393 EMBLX58437 NIDg12877 PIDNCAA41343.1 PIDg12878 cv. Bintje differences between the sequences from references S17427 and S36919 are due to RNA editing Zanlungo, S. Begu, D. Quinones, V. Araya, A. Jordana, X. Curr. Genet. 241993344-348 RNA editing of apocytochrome b (cob) transcripts in mitochondria from two genera of plants. MUID94073991 S36919 not compared with conceptual translation mRNA 13-23;55-65;92-112;115-125;135-145;184-199;223-245;266-274;280-289;299-307;323-333;357-366;370-380;382-393 cv. Bintje Braun, H.P. Schmitz, U.K. FEBS Lett. 3161993128-132 Purification and sequencing of cytochrome b from potato reveals methionine cleavage of a mitochondrially encoded protein. MUID93131029 S28874 protein 2-16 cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain RNA editing transmembrane protein product ubiquinol--cytochrome-c reductase cytochrome b 2-393 experimental domain cytochrome b homology 16-346 domain cytochrome b6 homology 16-216 domain transmembrane 41-57 predicted domain transmembrane 86-104 predicted domain transmembrane 124-140 predicted domain transmembrane 185-207 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 228-346 domain transmembrane 236-252 predicted domain transmembrane 295-311 predicted domain transmembrane 330-350 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 88,189 predicted binding-site heme iron (His) (axial ligands) (high potential) 102,203 predicted 393 complete MTIRNQRLSLLKQPISSILNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHY TPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFFIVVYLHIFRGLYYASYSSPREFVW CLGVVIFLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNA TLNRFFSLHYLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDKIAFYPYFYVKDLVGWV AFAIFFSIWIFYAPNVLGHPDNYIPANPMSTPPHIVPEWYFLPIYAILRSIPDKVGGVAA IALVFICLLALPFFKSMYVRSSSFRPIYQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQI SSLVFFLFFAITPILGRVGRGIPNSYTDETDHT
CBVF S01221 30-Jun-1992 30-Jun-1992 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b fava bean mitochondrion fava bean mitochondrion Vicia faba Wahleithner, J.A. Wolstenholme, D.R. Nucleic Acids Res. 1619886897-6913 Ribosomal protein S14 genes in broad bean mitochondrial DNA. MUID88303319 S01221 DNA 1-392 EMBLX07237 NIDg13880 PIDNCAA30226.1 PIDg13882 the authors translated the codon GGA for residue 137 as Phe the authors translated the codon CGG for residue 120 as Trp, assuming a special genetic code for plant mitochondria cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 16-346 domain cytochrome b6 homology 16-216 domain transmembrane 41-57 predicted domain transmembrane 86-104 predicted domain transmembrane 124-140 predicted domain transmembrane 185-207 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 228-346 domain transmembrane 236-252 predicted domain transmembrane 296-311 predicted domain transmembrane 330-350 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 88,189 predicted binding-site heme iron (His) (axial ligands) (high potential) 102,203 predicted 392 complete MTIRNQRLSLLKQPISSTLNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHY TPHVDLAFNSVEHVMRDVEGGWLLRYMHANGASMFLIVVHLHIFRGLYHASYSSPREFVR CLGVVIFLLMIVTAFTGYVPPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNA TLNRFFSLHHLLPFILVGASLLHLAALHQYGSNNPLGVHSEMDQISFYPYFYVKDLVGWV AFAIFFSIWIFYAPNVLGHPDNYIPANPMPTPPHIVPEWYFLPIHAILRSIPDKSGGVAA IAPVFICLLALPFFKSMYVRSSSFRPIHQGIFWLLLADRLLLGWIGCQPVEAPFVTIGQI PPFVFFLFFAITPIPGRVGRGIPNSYTDETDQ
S25953 S25953 07-May-1993 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b liverwort (Marchantia polymorpha) mitochondrion mitochondrion Marchantia polymorpha Oda, K. Yamato, K. Ohta, E. Nakamura, Y. Takemura, M. Nozato, N. Akashi, K. Kanegae, T. Ogura, Y. Kohchi, T. Ohyama, K. J. Mol. Biol. 22319921-7 Gene organization deduced from the complete sequence of liverwort Marchantia polymorpha mitochondrial DNA. A primitive form of plant mitochondrial genome. MUID92114051 S25953 nucleic acid sequence not shown translation not shown DNA 1-404 EMBLM68929 NIDg786182 PIDNAAC09441.1 PIDg786227 the nucleotide sequence was submitted to the EMBL Data Library, February 1992 cob mitochondrion 124/3; 261/3; 275/2 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 13-343 domain cytochrome b6 homology 13-213 domain transmembrane 38-54 predicted domain transmembrane 83-101 predicted domain transmembrane 121-137 predicted domain transmembrane 182-204 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 225-343 domain transmembrane 233-249 predicted domain transmembrane 292-308 predicted domain transmembrane 327-347 predicted domain transmembrane 357-372 predicted binding-site heme iron (His) (axial ligands) (low potential) 85,186 predicted binding-site heme iron (His) (axial ligands) (high potential) 99,200 predicted 404 complete MARRLSILKQPIFSTFNNHLIDYPTPSNISYWWGFGSLAGLCLVIQILTGVFLAMHYTPH VDLAFLSVEHIMRDVKGGWLLRYMHANGASMFFIVVYLHFFRGLYYGSYASPRELVWCLG VVILLLMIVTAFIGYVLPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNATLN RFFSLHYLLPFIIAGASILHLAALHQYGSNNPLGINSSVDKIAFYPYIYVKDLVGWVAFA IFFSIFVFYAPNVLGHPDNYIPANPMSTPAHIVPEWYFLPVYAILRSIPNKLGGVAAIGL VFVSLLALPFINTSYVRSSSFRPIHQKFFWLLVADCLLLGWIGCQPVEAPYVTIGQIASV GFFFYFAITPILGKCEARLIKNSNACEARSVLASFLTSIGLLWW
A53224 A53224 S11966 S12016 PQ0039 S33471 12-May-1994 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Chlamydomonas reinhardtii mitochondrion mitochondrion Chlamydomonas reinhardtii Bennoun, P. Delosme, M. Kueck, U. Genetics 1271991335-343 Mitochondrial genetics of Chlamydomonas reinhardtii: resistance mutations marking the cytochrome b gene. MUID91169284 A53224 DNA 1-381 GBX59471 NIDg13747 PIDNCAA42076.1 PIDg13748 Ma, D.P. Yang, Y.W. King, T.Y. Hasnain, S.E. Plant Mol. Biol. 151990357-359 The mitochondrial apocytochrome b gene from Chlamydomonas reinhardtii. MUID91355882 S11966 DNA 1-187,'F',189-231,'VLCSWL',238,'CSAF',243-381 EMBLX52168 NIDg311947 PIDNCAA36421.1 PIDg311948 Michaelis, G. Vahrenholz, C. Pratje, E. Mol. Gen. Genet. 2231990211-216 Mitochondrial DNA of Chlamydomonas reinhardtii: the gene for apocytochrome b and the complete functional map of the 15.8 kb DNA. MUID91066832 S12016 DNA 1-187,'F',189-381 GBX66484 GBM37212 GBX01442 GBX16537 GBX62284 NIDg12510 PIDNCAA47111.1 PIDg12511 Ma, D.P. Yang, Y.W. King, Y.T. Hasnain, S.E. Gene 851989363-370 Nucleotide sequence of cloned nad4 (urf4) gene from Chlamydomonas reinhardtii mitochondrial DNA. MUID90185210 PQ0039 DNA 1-65 the gene encoding this protein is located downstream from gene nad4 cob mitochondrion the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-337 domain cytochrome b6 homology 10-210 domain transmembrane 36-52 predicted domain transmembrane 81-99 predicted domain transmembrane 119-135 predicted domain transmembrane 180-202 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-337 domain transmembrane 231-247 predicted domain transmembrane 290-306 predicted domain transmembrane 325-345 predicted domain transmembrane 355-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,197 predicted 381 complete MRMHNKIQLLSVLNTHLVAYPTPMNLNYSWNGGSLAGMMLASQMLTGILLAMHYVGHVDY AFASVQHLMTDVPSGMILRYAHANGASLFFIVVYLHVLRGMYYGSGAQPREIVWISGVVI LLVMIITAFIGYVLPWGQMSFWGATVITSLATAIPVVGKHIMYWLWGGFSVDNPTLNRFY SFHYTLPLILAGLSVFHIAALHQYGSTNPLGVNSQSSLISFGSYFGAKDLVGALFLALVF SILVFFYPDLLGHPDNLIPANPYSTPQHIVPEWYFLWVYAILRSIPNKAMGVLAIGLVFA SLFAMPFIGLGGGKFRIITEWLYWTFLADVLLLTWLGGNEITPITSFVGQCCTAYLFFYL LVCQPLVGYLETQFAHGTQTN
CBASN A00157 02-Apr-1982 02-Apr-1982 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Emericella nidulans mitochondrion mitochondrion Emericella nidulans, Aspergillus nidulans Waring, R.B. Davies, R.W. Lee, S. Grisi, E. Berks, M.M. Scazzocchio, C. Cell 2719814-11 The mosaic organization of the apocytochrome b gene of Aspergillus nidulans revealed by DNA sequencing. MUID82115341 A00157 DNA 1-387 GBJ01389 GBV00651 GBV00652 NIDg336901 PIDNAAA31737.1 PIDg336903 imperfect stage cobA mitochondrion SGC3 169/2 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-341 domain cytochrome b6 homology 10-211 domain transmembrane 35-51 predicted domain transmembrane 80-98 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 223-341 domain transmembrane 231-247 predicted domain transmembrane 290-306 predicted domain transmembrane 325-345 predicted domain transmembrane 355-371 predicted binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,197 predicted 387 complete MRILKSHPLLKIVNSYIIDSPQPANLSYLWNFGSLLALCLGIQIVTGVTLAMHYTPSVSE AFNSVEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGLYYGSYKTPRTLTWAIGTVI LIVMMATAFLGYVLPYGQMSLWGATVITNLMSAIPWIGQDIVEFIWGGFSVNNATLNRFF ALHFLLPFVLAALALMHLIAMHDTVGSGNPLGISANYDRLPFAPYFIFKDLITIFIFFIV LSIFVFFMPNALGDSENYVMANPMQTPPAIVPEWYLLPFYAILRSIPNKLLGVIAMFAAI LALMVMPITDLSKLRGVQFRPLSKVVFYIFVANFLILMQIGAKHVETPFIEFGQISTIIY FAYFFVIVPVVSLIENTLVELGTKKNF
CBNC A00158 S03128 B28755 15-Nov-1984 15-Nov-1984 16-Jun-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Neurospora crassa mitochondrion mitochondrion Neurospora crassa Citterich, M.H. Morelli, G. Macino, G. EMBO J. 219831235-1242 Nucleotide sequence and intron structure of the apocytochrome b gene of Neurospora crassa mitochondria. A00158 DNA 1-385 GBM37324 NIDg342695 in GenBank entry NEUMTCYTAB, release 113.0, PID:g497778, PIDN:AAA31961.1, although it is stated otherwise, apparently GenBank translation table 5 (PIR SGC4) was used rather than the correct translation table 4 (PIR SGC3) the translation with SGC3 matching the author's translation in Fig. 2 is shown here Collins, R.A. Reynolds, C.A. Olive, J. Nucleic Acids Res. 1619881125-1134 The self-splicing intron in the Neurospora apocytochrome b gene contains a long reading frame in frame with the upstream exon. MUID88143984 S03128 DNA 1-163 EMBLX06884 NIDg13115 PIDNCAA30001.1 PIDg13117 PIDg1334408 Burke, J.M. Breitenberger, C. Heckman, J.E. Dujon, B. RajBhandary, U.L. J. Biol. Chem. 2591984504-511 Cytochrome b gene of Neurospora crassa mitochondria. MUID84161957 B28755 DNA 132-163,'FIW',167-182,'H',184-186,'P',188-190,'AA',193-196,'H',198-199,'A',201,'H',203,'TA',206,'S',208-212,'VS',215-220,'T',222-279,'Y',281-360,'F',362-385 GBK01181 NIDg342694 this ORF is not translated in GenBank entry NEUMTCYB, release 106.0 See PIR:A28755 for a hypothetical gene cob intron 2 encoded protein. cob mitochondrion SGC3 131/3; 164/1 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-341 domain cytochrome b6 homology 10-211 domain transmembrane 35-51 predicted domain transmembrane 80-98 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 223-341 domain transmembrane 231-247 predicted domain transmembrane 290-306 predicted domain transmembrane 325-345 predicted domain transmembrane 355-371 predicted binding-site heme iron (His, Tyr) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His, Tyr) (axial ligands) (high potential) 96,197 predicted 385 complete MRLLKSHPLLKLVNSYLIDASQPSNISYLWNFGSLLACCLIIQIVTGVTLAMHYSPNVLE AFNSIEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGMYYGSYRAPRTLVWAIGTVI LILMMATAFLGYVLPYGQMSLWGATVITNLISAIPWIGQDIVELHLGGFSVNNATLNRFF ALYFVLLFILVVLVLMYLIVLYDIVGLSNPLGALGNYDRIIFAPYYLFKDLITIFIFIYV LSSFVFFMPNVLGDSENYIMANPMQTPPAIVPEWYLLPFDAILRSIPNKLLGVIAMFSAI LAIMLLPITDLGRSKGLQFRPLSKFAFWAFVVNFLILMKLGACHVESPFIELGQFSTIFY LSYFIFIVPVLSLIENTLVDLNYLK
A48326 A48326 04-Feb-1994 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Podospora anserina mitochondrion mitochondrion Podospora anserina Cummings, D.J. Michel, F. McNally, K.L. Curr. Genet. 161989407-418 DNA sequence analysis of the apocytochrome b gene of Podospora anserina: a new family of intronic open reading frame. MUID90124723 A48326 DNA 1-387 GBX55026 NIDg14030 PIDNCAA38772.1 PIDg14038 mitochondrion SGC3 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-341 domain cytochrome b6 homology 10-211 domain transmembrane 35-51 predicted domain transmembrane 80-98 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 223-341 domain transmembrane 231-247 predicted domain transmembrane 290-306 predicted domain transmembrane 325-345 predicted domain transmembrane 355-371 predicted binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,197 predicted 387 complete MRILKSHPLLKLVNSYLIDASQPSNISYLWNFGSLLLLCLIIQIITGVTLAMHYSPNVLE AFNSIEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGMYYGSYRAPRTLVWAIGTVI LIVMIVTAFLGYVLPYGQMSLWGATVITNLVSAIPWIGQDIVEFIWGGFSVNNATLNRFF ALHYLLPFILVALVLMHLIALHDTAGSSNPLGISGNYDRITFAPYYLFKDLITIFIFIFV LSSFVFFMSNVLGDSENYIMANPMQTPAAIVPEWYLLPFYAILRSIPNKLLGVIAMFAAI LAIMLLPITDLGRSKGLQFRPLSKFAFWVFVVNFLILMKLGACHVETPFIELGQLSTALY FGHFIIIVPIISLIENTLVDLNTMSKG
CBBY A00159 A38011 A38012 S56165 S68973 31-Dec-1980 19-Feb-1984 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b yeast (Saccharomyces cerevisiae) mitochondrion mitochondrion Saccharomyces cerevisiae Nobrega, F.G. Tzagoloff, A. J. Biol. Chem. 25519809828-9837 Assembly of the mitochondrial membrane system. DNA sequence and organization of the cytochrome b gene in Saccharomyces cerevisiae D273-10B. MUID81046788 A00159 DNA 1-385 EMBLV00696 strain D273-10B/A21 the coding region was identified by homology with mammalian cytochromes b the amino acids at the intron junctions are uncertain residue 253 may be Gln or His and residue 270 may be Asp or Val the authors translated the codon ATA for residue 69 according to the standard code Lazowska, J. Jacq, C. Slonimski, P.P. Cell 221980333-348 Sequence of introns and flanking exons in wild-type and box3 mutants of cytochrome b reveals an interlaced splicing protein coded by an intron. MUID81088336 A38011 DNA 20-121,'T',123-138 EMBLV00686 strain 777-3A the authors translated the codon ATA for residue 69 according to the standard code Lazowska, J. Jacq, C. Slonimski, P.P. Cell 27198112-14 Splice points of the third intron in the yeast mitochondrial cytochrome b gene. MUID82115326 A38012 DNA 144-169 strain 777-3A Jacq, C. submitted to the EMBL Data Library January1995 S56165 DNA 1-121,'T',123-252,'H',254-269,'V',271-385 EMBLX84042 NIDg643020 PIDNCAA58861.1 PIDg643021 strain WR200 Claros, M.G. Perea, J. Shu, Y. Samatey, F.A. Popot, J.L. Jacq, C. Eur. J. Biochem. 2281995762-771 Limitations to in vivo import of hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b. MUID95255283 S68973 DNA 1-121,'T',123-252,'H',254-269,'V',271-385 EMBLX84042 NIDg643020 PIDNCAA58861.1 PIDg643021 cytb cob 71.6-76.2 mitochondrion SGC2 253/3; 270/3 strain D273-10B/A21 cytb cob mitochondrion SGC2 139/1; 143/2; 169/2; 253/3; 270/3 strain 777-3A the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrial inner membrane mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-340 domain cytochrome b6 homology 10-210 domain transmembrane 35-51 predicted domain transmembrane 80-98 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,197 predicted 385 complete MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGQPDNYIPGNPLVTPASIDPEWYLLPFYAILRSIPDKLLGVITMFAAIL VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK
S15157 S15157 12-Feb-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b yeast (Saccharomyces sp.) mitochondrion (strain 4707-22D) mitochondrion Saccharomyces sp. Tian, G.L. Michel, F. Macadre, C. Slonimski, P.P. Lazowska, J. J. Mol. Biol. 2181991747-760 Incipient mitochondrial evolution in yeasts. II. The complete sequence of the gene coding for cytochrome b in Saccharomyces douglasii reveals the presence of both new and conserved introns and discloses major differences in the fixation of mutations in evolution. MUID91218158 S15157 not compared with conceptual translation DNA 1-385 the source is designated as Saccharomyces douglasii cob mitochondrion SGC2 131/3; 139/1; 143/3; 169/2 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-340 domain cytochrome b6 homology 10-210 domain transmembrane 35-51 predicted domain transmembrane 80-98 predicted domain transmembrane 118-136 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-342 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,197 predicted 385 complete MAFRKSNVYLSLVNSYTIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL AFSSVEHIMRDVHSGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK
S12352 S12352 S09405 12-Feb-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b yeast (Kluyveromyces marxianus var. lactis) mitochondrion mitochondrion Kluyveromyces marxianus var. lactis, Candida sphaerica Brunner, A. Coria, R. Yeast 51989209-218 Cloning and sequencing of the gene for apocytochrome b of the yeast Kluyveromyces lactis strains WM27 (NRRL Y-17066) and WM37 (NRRL Y-1140). MUID89284741 S12352 not compared with conceptual translation DNA 1-386 mitochondrion SGC2 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 10-340 domain cytochrome b6 homology 10-210 domain transmembrane 35-51 predicted domain transmembrane 80-98 predicted domain transmembrane 118-134 predicted domain transmembrane 179-201 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 222-340 domain transmembrane 230-246 predicted domain transmembrane 289-305 predicted domain transmembrane 324-344 predicted domain transmembrane 354-370 predicted binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,197 predicted 386 complete MSFRKSNIYLNLLNSYMIDSPQPSSINYWWNLGSLLGLCLVIQICTGIFLAMHYSSNIEL AFSAVEHIMRDVQGGWFIRYAHANGASFFFICMYIHIGKGLYYGSYRAPRTLVWNVGVII FVLTMAAAFLGYCCVYGQMSHWGATVITNLFSAIPFIGNDIVSWLWGGFSVSNPTIQRFF AFHYLVPFIIAAFVIMHFMALHTHGSSNPLGVTGNLDRLPMHGYFIFKDLITVFVFLFFF SLFVFFSPNTMGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSVPDKLLGVLAMFGAIL ILLVLPITDRSVIRGNAFKVFSKFFFFLFIANFVLLGHLGECHVEPPFVVMGQIATVIYF AYFLVIVPVVSTIENVLFYVGRKNTK
CBUTB A00160 18-Apr-1984 18-Apr-1984 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Trypanosoma brucei mitochondrion mitochondrion Trypanosoma brucei Benne, R. De Vries, B.F. Van den Burg, J. Klaver, B. Nucleic Acids Res. 1119836925-6941 The nucleotide sequence of a segment of Trypanosoma brucei mitochondrial maxi-circle DNA that contains the gene for apocytochrome b and some unusual unassigned reading frames. MUID84041494 A00160 DNA 1-363 GBX00017 NIDg13737 PIDNCAA24915.1 PIDg578828 the authors translated the initiation codon ATT for residue 1 as Ile The cytochrome b gene was isolated from a 20-kb maxicircle. mitochondrion SGC6 ATT the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane protein metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain domain cytochrome b homology 2-334 domain cytochrome b6 homology 2-202 domain plastoquinol--plastocyanin reductase 17K protein homology 216-334 binding-site heme iron (His) (axial ligands) (low potential) 74,175 predicted binding-site heme iron (His) (axial ligands) (high potential) 88,189 predicted 363 complete MLYKSGEKRKGLLMSGCLYRIYGVGFSLGFFIALQIICGVCLAWLFFSCFICSNWYFVLF LWDFDLGFVIRSVHICFTSLLYLLLYIHIFKSITLIILFDTHILVWFIGFILFVFIIIIA FIGYVLPCTMMSYWGLTVFSNIIATVPILGIWLCYWIWGSEFINDFTLLKLHVLHVLLPF ILLIILILHLFCLHYFMSSDAFCDRFAFYCERLSFCMWFYLRDMFLAFSILLCMMYVIFI NWYFVFHEESWVIVDTLKTSDKILPEWFFLYLFGFLKAIPDKFMGLFLMVILLFSLFLFI LNCILWFVYCRSSLLWLTYSLILFYSIWMSGFLALYVVLAYPIWMELQYWVLLLFLLIVC RLD
H22848 H22848 A28118 30-Jun-1989 26-Jul-1996 20-Apr-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b [validated] Leishmania tarentolae mitochondrion mitochondrion Leishmania tarentolae de la Cruz, V.F. Neckelmann, N. Simpson, L. J. Biol. Chem. 259198415136-15147 Sequences of six genes and several open reading frames in the kinetoplast maxicircle DNA of Leishmania tarentolae. MUID85079995 H22848 DNA 'IIIKAERKEKA',21-371 GBM10126 NIDg1256945 this translation is not annotated in GenBank entry LEIKPMAX, release 113.0 it is produced from codons 5393-6481 Feagin, J.E. Shaw, J.M. Simpson, L. Stuart, K. Proc. Natl. Acad. Sci. U.S.A. 851988539-543 Creation of AUG initiation codons by addition of uridines within cytochrome b transcripts of kinetoplastids. MUID88124876 A28118 mRNA 1-48 GBM10126 NIDg1256945 Horvath, A. Berry, E.A. Maslov, D.A. Science 28720001639-1640 Translation of the edited mRNA for cytochrome b in trypanosome mitochondria. MUID20165033 annotation amino acid sequencing the blocking group was removed part of this sequence, including the unblocked amino end of the mature protein, was determined by protein sequencing mitochondrion SGC6 membrane-associated monomer; membrane-associated homopolymer; substoichiometric association with ubiquinol--cytochrome-c reductase complex the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology blocked amino end chromoprotein electron transfer heme iron membrane protein metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain RNA editing domain cytochrome b homology 10-342 domain cytochrome b6 homology 10-210 domain plastoquinol--plastocyanin reductase 17K protein homology 224-342 modified-site blocked amino end (Met) (probably formylated) 1 experimental binding-site heme iron (His) (axial ligands) (low potential) 82,183 predicted binding-site heme iron (His) (axial ligands) (high potential) 96,202 predicted 371 complete MFFRVRFLLFFLLFRNLCCLLTSGCLLRVYGVGFSLGFFICMQIICGVCLAWLFFSCFIC TNWYFVLFLWDFDLGFVIRSTHICFTSLLFFLLYVHIFKCIVLIILFDTHILVWAVGFII YIFIVVIGFIGYVLPCTMMSYWGLTVFSNILATVPVIGTWLCYWIWGSEYINDFTLLKLH VLHVLLPFVLILVIFMHLFCLHYFMSSDGFCDRFAFYCERLCFCMWFYLRDMFLAFLILF YVVYFIFINWYFVFHEESWVIVDTLKTSDKILPEWFFLFLFGFLKAVPDKFTGLLLMVIL LFSLFLFILNCILWFVYCRSSLLWFTYSLILFYSIFMSGFLALYVILAYPIWMELQFWVL LLFMLVVCRLD
A32566 A32566 07-Sep-1990 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Plasmodium gallinaceum mitochondrion mitochondrion Plasmodium gallinaceum Aldritt, S.M. Joseph, J.T. Wirth, D.F. Mol. Cell. Biol. 919893614-3620 Sequence identification of cytochrome b in Plasmodium gallinaceum. MUID89384587 A32566 not compared with conceptual translation mRNA 1-300 The location of the second heme iron ligand for each of the two supposed heme groups is uncertain. mitochondrion SGC6 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 6-280 atypical domain cytochrome b6 homology 6-182 atypical domain transmembrane 34-50 predicted domain transmembrane 112-128 predicted domain transmembrane 168-185 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 183-280 atypical domain transmembrane 228-244 predicted domain transmembrane 283-299 predicted binding-site heme iron (His) (axial ligand) (low potential) 63 predicted binding-site heme iron (His) (axial ligand) (high potential) 78 predicted 300 complete MNYYSINLAKAHLLHYPCPLNINFLWNYGFLLGIVFFIQILKGVLLALVILQKLSYAYYS VQHILRAIMDGWCFRYMHATGASFVFILTYLHILRGLNYSYSYLPLSWISGLMIFLISIV TAFYGYVLPWGQMSFWNTTVITNLLYLFRTCFMDCGGYLVSDPTLKRFFVFIYFPFIALC QSLFGILPLSHPDNAITVDRYATPLHIVPEWYFLPFYAMLKTIPNKTAGLLVMLASLQIL FLLAEQRNLTTLIHFKFAFGAREYSVPTICYMSSMLIWIGCQLPQILHFIWSFIYYIILF
S28664 S28664 10-Sep-1999 10-Sep-1999 21-Jul-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Plasmodium falciparum mitochondrion mitochondrion Plasmodium falciparum Feagin, J.E. Werner, E. Gardner, M.J. Williamson, D.H. Wilson, R.J.M. Nucleic Acids Res. 201992879-887 Homologies between the contiguous and fragmented rRNAs of the two Plasmodium falciparum extrachromosomal DNAs are limited to core sequences. MUID92178987 S28664 nucleic acid sequence not shown translation not shown DNA 1-376 EMBLM76611 NIDg1311631 PIDNAAC63391.1 PIDg3721518 mitochondrion SGC6 this protein originates from a 6K extrachromosomal linear element cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 6-329 atypical domain cytochrome b6 homology 6-200 domain transmembrane 34-50 predicted domain transmembrane 112-128 predicted domain transmembrane 169-236 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 211-329 atypical domain transmembrane 279-295 predicted domain transmembrane 336-352 predicted binding-site heme iron (His) (axial ligands) (low potential) 78,173 predicted binding-site heme iron (His) (axial ligands) (high potential) 92,187 predicted 376 complete MNFYSINLVKAHLINYPCPLNINFLWNYGFLLGIIFFIQIITGVFLASRYTPDVSYAYYS IQHILRELWSGWCFRYMHATGASLVFLLTYLHILRGLNYSYMYLPLSWISGLILFMIFIV TAFVGYVLPWGQMSYWGATVITNLLSSIPVAVIWICGGYTVSDPTIKRFFVLHFILPFIG LCIVFIHIFFLHLHGSTNPLGYDTALKIPFYPNLLSLDVKGFNNVIILFLIQSLFGIIPL SHPDNAIVVNTYVTPSQIVPEWYFLPFYAMLKTVPSKPAGLVIVLLSLQLLFLLAEQRSL TTIIQFKMIFGARDYSVPIIWFMCAFYALLWIGCQLPQDIFILYGRLFIVLFFCSGLFVL VHYRRTHYDYSSQANI
CBQFR S12257 A38814 31-Dec-1991 31-Dec-1991 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Rhodospirillum rubrum Rhodospirillum rubrum Majewski, C. Trebst, A. Mol. Gen. Genet. 2241990373-382 The pet genes of Rhodospirillum rubrum: cloning and sequencing of the genes for the cytochrome bc(1)-complex. MUID91094774 S12257 DNA 1-405 EMBLX55387 NIDg46382 PIDNCAA39059.1 PIDg46385 the authors translated the codon AAT for residue 161 as Leu and CTG for residue 162 as Asn A38814 protein 1-26,'E' petB cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase respiratory chain transmembrane protein product cytochrome b 1-405 experimental domain cytochrome b homology 22-354 domain cytochrome b6 homology 22-222 domain transmembrane 47-63 predicted domain transmembrane 92-110 predicted domain transmembrane 130-146 predicted domain transmembrane 191-213 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 236-354 domain transmembrane 244-260 predicted domain transmembrane 303-319 predicted domain transmembrane 338-356 predicted domain transmembrane 368-384 predicted binding-site heme iron (His) (axial ligands) (low potential) 94,195 predicted binding-site heme iron (His) (axial ligands) (high potential) 108,209 predicted 405 complete MYTPPRWNNKALKWFDERLPVLTVAHKELVVYPAPRNLNYFWNFGSLAGIAMIIMIATGI FLAMSYTAHVDHAFDSVERIMRDVNYGWLMRYMHANGASMFFIVVYVHMFRGLYYGSYKP PREVLWWLGLVILLLMMATAFMGYVLPWGQMSFWGATVITNLFSAIPVVGDDIVTLLWGG FSVDNPTLNRFFSLHYLFPMLLFAVVFLHMWALHVKKSNNPLGIDAKGPFDTIPFHPYYT VKDAFGLGIFLMVFCFFVFFAPNFFGEPDNYIPANPMVTPTHIVPEWYFLPFYAILRAVP DKLGGVLAMFGAILILFVLPWLDTSKVRSATFRPVFKGFFWVFLADCLLLGYLGAMPAEE PYVTITQLATIYYFLHFLVITPLVGWFEKPKPLPVSISSPVTTQA
B29336 B29336 B25405 S09373 31-Dec-1988 22-Jul-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Rhodobacter capsulatus Rhodobacter capsulatus Davidson, E. Daldal, F. J. Mol. Biol. 195198713-24 Primary structure of the bc-1 complex of Rhodopseudomonas capsulata. Nucleotide sequence of the pet operon encoding the Rieske, cytochrome b, and cytochrome c-1 apoproteins. MUID88011223 B29336 DNA 1-437 EMBLX05630 NIDg46093 PIDNCAA29117.1 PIDg46095 Gabellini, N. Sebald, W. Eur. J. Biochem. 1541986569-579 Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c-1. MUID86136096 source is designated as Rhodopseudomonas sphaeroides B25405 DNA 1-66,'ID',69-280,'I',282-437 EMBLX03476 NIDg46007 PIDNCAA27195.1 PIDg46009 fbcB petB cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 26-381 domain cytochrome b6 homology 26-225 domain transmembrane 51-67 predicted domain transmembrane 96-114 predicted domain transmembrane 134-150 predicted domain periplasmic 146-193 predicted domain transmembrane 195-217 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 245-381 domain transmembrane 253-269 predicted domain periplasmic 270-329 predicted domain transmembrane 330-346 predicted domain transmembrane 365-383 predicted domain transmembrane 395-411 predicted binding-site heme iron (His) (axial ligands) (low potential) 97,198 predicted binding-site heme iron (His) (axial ligands) (high potential) 111,212 predicted 437 complete MSGIPHDHYEPKTGIEKWLHDRLPIVGLVYDTIMIPTPKNLNWWWIWGIVLAFTLVLQIV TGIVLAMHYTPHVDLAFASVEHIMRDVNGGWAMRYIHANGASLFFLAVYIHIFRGLYYGS YKAPREITWIVGMVIYLLMMGTAFMGYVLPWGQMSFWGATVITGLFGAIPGIGPSIQAWL LGGPAVDNATLNRFFSLHYLLPFVIAALVAIHIWAFHTTGNNNPTGVEVRRTSKADAEKD TLPFWPYFVIKDLFALALVLLGFFAVVAYMPNYLGHPDNYVQANPLSTPAHIVPEWYFLP FYAILRAFAADVWVVILVDGLTFGIVDAKFFGVIAMFGAIAVMALAPWLDTSKVRSGAYR PKFRMWFWFLVLDFVVLTWVGAMPTEYPYDWISLIASTYWFAYFLVILPLLGATEKPEPI PASIEEDFNSHYGNPAE
B29413 B29413 31-Mar-1989 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b bc1 complex complex III Paracoccus denitrificans Paracoccus denitrificans Kurowski, B. Ludwig, B. J. Biol. Chem. 262198713805-13811 The genes of the Paracoccus denitrificans bc-1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits. MUID88007612 B29413 DNA 1-440 GBM17522 NIDg150569 PIDNAAA25572.1 PIDg150571 cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome b homology 26-381 domain cytochrome b6 homology 26-225 domain transmembrane 51-67 predicted domain transmembrane 96-114 predicted domain transmembrane 134-150 predicted domain transmembrane 195-217 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 245-381 domain transmembrane 253-269 predicted domain transmembrane 330-346 predicted domain transmembrane 365-383 predicted domain transmembrane 395-411 predicted binding-site heme iron (His) (axial ligands) (low potential) 97,198 predicted binding-site heme iron (His) (axial ligands) (high potential) 111,212 predicted 440 complete MAGIPHDHYEPKTGFERWLHRRLPIVSLVYDTLMIPTPKNLNWWWIWGIVLAFCLVLQIA TGIVLVMHYTPHVDLAFASVEHIMRDVNGGYMLRYLHANGASLFFLAVYIHIFRGLYYGS YKAPREVTWIVGMLIYLMMMGTAFMGYVLPWGQMSFWGATVITGLFGAIPGVGEAIQTWL LGGPAVDNPTLNRFFSLHYLLPFVIAALVVVHIWAFHTTGNNNPTGVEVRRGSKEEAKKD TLPFWPYFVIKDLFALAVVLVVFFAIVGFMPNYLGHPDNYIEANPLVTPAHIVPEWYFLP FYAILRAFTADVWVVMLVNWLSFGIIDAKFFGVIAMFGAILVMALVPWLDTSRVRSGQYR PLFKWWFWLLAVDFVVLMWVGAMPAEGIYPYIALAGSAYWFAYFLIILPLLGIIEKPDAM PQTIEEDFNAHYGPETHPAE
S13869 S13869 A34591 31-Dec-1988 22-Jul-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Rhodobacter sphaeroides Rhodobacter sphaeroides Yun, C.H. Beci, R. Crofts, A.R. Kaplan, S. Gennis, R.B. Eur. J. Biochem. 1941990399-411 Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc(1) complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant. MUID91099313 S13869 DNA 1-445 EMBLX56157 NIDg46425 PIDNCAA39624.1 PIDg46427 the sequence from Fig. 5 is inconsistent with that from Fig. 2 in having 179-Glu, 277-Leu, and 316-Cys Andrews, K.M. Crofts, A.R. Gennis, R.B. Biochemistry 2919902645-2651 Large-scale purification and characterization of a highly active four-subunit cytochrome bc-1 complex from Rhodobacter sphaeroides. MUID90268011 A34591 protein 2-6,'X',8-9,'Z',11-15,'XX',18-19 fbcB cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis respiratory chain transmembrane protein product cytochrome b 2-445 experimental domain cytochrome b homology 26-381 domain cytochrome b6 homology 26-225 domain transmembrane 43-67 predicted domain transmembrane 95-113 predicted domain transmembrane 127-149 predicted domain periplasmic 150-193 predicted domain transmembrane 194-216 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 245-381 domain transmembrane 253-270 predicted domain periplasmic 271-329 predicted domain transmembrane 330-349 predicted domain transmembrane 365-382 predicted domain transmembrane 394-413 predicted binding-site heme iron (His) (axial ligands) (low potential) 97,198 predicted binding-site heme iron (His) (axial ligands) (high potential) 111,212 predicted 445 complete MSGIPHDHYEPRTGIEKWLHSRLPIVALAYDTIMIPTPRNLNWMWIWGVVLAFCLVLQIV TGIVLAMHYTPHVDLAFASVEHIMRNVNGGFMLRYLHANGASLFFIAVYLHIFRGLYYGS YKAPREVTWIVGMLIYLAMMATAFMGYVLPWGQMSFWGATVITGLFGAIPGIGHSIQTWL LGGPAVDNATLNRFFSLHYLLPFVIAALVAIHIWAFHSTGNNNPTGVEVRRTSKAEAQKD TVPFWPYFIIKDVFALAVVLLVFFAIVGFMPNYLGHPDNYIEANPLSTPAHIVPEWYFLP FYAILRAFTADVWVVQIANFISFGIIDAKFFGVLAMFGAILVMALVPWLDTSPVRSGRYR PMFKIYFWLLAADFVILTWVGAQQTTFPYDWISLIASAYWFAYFLVILPILGAIEKPVAP PATIEEDFNAHYSPATGGTKTVVAE
JQ0346 JQ0346 07-Sep-1990 02-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Rhodopseudomonas viridis Rhodopseudomonas viridis Verbist, J. Lang, F. Gabellini, N. Oesterhelt, D. Mol. Gen. Genet. 2191989445-452 Cloning and sequencing of the fbcF, B and C genes encoding the cytochrome b/c1 complex from Rhodopseudomonas viridis. MUID90158506 JQ0346 DNA 1-419 strain 133 This protein is one of the three subunits of the ubiquinol-cytochrome C2 oxidoreductase complex, which is coupled with another membrane-protein complex at the reaction center in a cyclic electron-transport system that catalyzes the synthesis of ATP. fbcB cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome b homology 24-356 domain cytochrome b6 homology 24-224 domain transmembrane 49-65 predicted domain transmembrane 94-112 predicted domain transmembrane 132-148 predicted domain transmembrane 193-215 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 238-356 domain transmembrane 246-262 predicted domain transmembrane 305-321 predicted domain transmembrane 340-360 predicted domain transmembrane 370-386 predicted binding-site heme iron (His) (axial ligands) (low potential) 96,197 predicted binding-site heme iron (His) (axial ligands) (high potential) 110,211 predicted 419 complete MSGHSSYQPSTGIERWLDTRLPIVRMMYDQFVAFPVPKNINYAYAFGAILAVFLIIQIVS GVVLAMHYVAQDTLAFASIEHIMRDVNYGWLIRYIHMNGASFFFFAVYAHTFRGMYYGSY KEPREVLWILGVIIIILMMATAFMGYVLPWGQMSFWGATVITNLFSAIPYIGDPIVTWLW GGYSVGNPTLTRFYSLHYLLPFVIVGVVMLHVWALHVTGQTNPTGVEVKSEKDTVRFTPF ALTKDAVALGVCFIAFAWFVFFVPNYLGHADNYIPANPGVTPAHIVPEWYLLPFYAILRA VPDKLGGVIAMFGALVVLLFLPWLDGSKVRSAAYRPLYRIFFWLFVADCIFLGWLGAMPA EGIYPTLSQVGTVWYFAHFLVIVPALGYFEKPKPLPESISAAVLEAHSRPSLLARLINR
S41691 S41691 S40156 31-Dec-1993 20-Aug-1994 03-Mar-2000
ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b Theileria parva mitochondrion mitochondrion Theileria parva Kairo, A. Fairlamb, A.H. Gobright, E. Nene, V. EMBO J. 131994898-905 A 7.1 kb linear DNA molecule of Theileria parva has scrambled rDNA sequences and open reading frames for mitochondrially encoded proteins. MUID94155854 S41691 DNA 1-386 EMBLZ23263 NIDg437862 PIDNCAA80800.1 PIDg437865 mitochondrion SGC6 the net reaction catalyzed by the ubiquinol--cytochrome-c reductase complex (complex III) is the oxidation of one molecule of ubiquinol to ubiquinone by two molecules of cytochrome c, with two hydrogen ions taken up from the mitochondrial matrix and four hydrogen ions released into the intermembrane space oxidative phosphorylation respiratory chain cytochrome b cytochrome b homology cytochrome b6 homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein domain cytochrome b homology 24-347 domain cytochrome b6 homology 24-218 domain transmembrane 49-65 predicted domain transmembrane 94-112 predicted domain transmembrane 130-146 predicted domain transmembrane 187-209 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 230-347 domain transmembrane 238-254 predicted domain transmembrane 299-316 predicted domain transmembrane 339-356 predicted domain transmembrane 360-375 predicted binding-site heme iron (His) (axial ligands) (low potential) 96,191 predicted binding-site heme iron (His) (axial ligands) (high potential) 110,205 predicted 386 complete MFYKKVIKIKLGNRALTYKLTFIMNMFNAHIPSYLVPKNLNSNWNVGFILGILLILQILS GLLLTFFYVPCKEGAFESLSRLVTETQFGWFVRLYHSVGVSFYFFFMFIHIIKGMWYSSK YMPWSWYSGIVILILSIVIAFTGYVLPDGQMSFWGATVISNLLEWFGKAKVITFGGFTVG PETLKRFFILHFVLPAVVLVIVLLHLYFLHREGSSNPLTLAEAVALLKFYQLILFSDVKF LVIISMFIGPQVGYGIWTLFQADNDNSILSSSENTPAHIIPEWYLLLFYATLKVFPTKVS GLVAMVVVLKLLIILVESRSKSQAVSTAHHHRVWTTTSVPLVPALFLLGCIGRMVINLDL IIIGIYGVLLSTTFVQKLLDSSRVRA
B32382 B32382 A39715 12-Oct-1989 20-Aug-1994 03-Mar-2000
fcbH bifunctional protein ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome b ubiquinol--cytochrome-c reductase (EC 1.10.2.2) cytochrome c1 Bradyrhizobium japonicum Bradyrhizobium japonicum Thoeny-Meyer, L. Stax, D. Hennecke, H. Cell 571989683-697 An unusual gene cluster for the cytochrome bc-1 complex in Bradyrhizobium japonicum and its requirement for effective root nodule symbiosis. MUID89249332 B32382 DNA 1-687 GBJ03176 NIDg152082 PIDNAAA26200.1 PIDg152084 Thoeny-Meyer, L. James, P. Hennecke, H. Proc. Natl. Acad. Sci. U.S.A. 8819915001-5005 From one gene to two proteins: the biogenesis of cytochromes b and c-1 in Bradyrhizobium japonicum. MUID91271320 A39715 preliminary protein 439-444 fcbH fcbH bifunctional protein cytochrome b homology cytochrome b6 homology cytochrome c1 heme protein homology plastoquinol--plastocyanin reductase 17K protein homology chromoprotein electron transfer heme iron membrane-associated complex metalloprotein oxidative phosphorylation oxidoreductase respiratory chain transmembrane protein product ubiquinol--cytochrome-c reductase, cytochrome b 1-412 predicted domain cytochrome b homology 24-356 domain cytochrome b6 homology 24-224 domain transmembrane 49-65 predicted domain transmembrane 94-112 predicted domain transmembrane 132-148 predicted domain transmembrane 193-215 predicted domain plastoquinol--plastocyanin reductase 17K protein homology 238-356 domain transmembrane 244-260 predicted domain transmembrane 303-319 predicted domain transmembrane 338-358 predicted domain transmembrane 368-383 predicted product ubiquinol--cytochrome-c reductase, cytochrome c1 413-687 predicted domain cytochrome c1 heme protein homology 440-687 binding-site heme iron (His) (axial ligands) (low potential) 96,197 predicted binding-site heme iron (His) (axial ligands) (high potential) 110,211 predicted binding-site heme (Cys) (covalent) 471,474 predicted binding-site heme iron (His, Met) (axial ligands) 475,616 predicted 687 complete MSGPSDYQPSNPALQWIERRLPILGLMHSSFVAYPTPRNLNYWWTFGAILSFMLGMQILT GVILAMHYTPHADLAFKSVELIVRDVNYGWLLRNMHACGASMFFFAVYVHMLRGLYYGSY KEPREVLWILGVIIYLLMMATGFMGYVLPWGQMSFWGATVITNLFSAIPYFGESIVTLLW GGYSVGNPTLNRFFSLHYLLPFLIAGVVVLHVWALHVAGQNNPEGVEPKSEKDTVPFTPH ATIKDMFGVACFLLLYAWFIFYMPNYLGDADNYIPANPGVTPPHIVPEWYYLPFYAILRS IPNKLAGVIGMFSAIIILCFLPWLDAAKTRSSKYRPLAKQFFWIFVAVCILLGYLGAQPP EGIYVIAGRVLTVCYFAYFLIVLPLLSRIETPRPVPNSISEAILAKGGKAVASVAIALVA AGALFLGSLQDARANEGSDKPPGNKWSFAGPFGKFDRGALQRGLKVYKEVCASCHGLSYI AFRNLAEAGGPSYSVAQVAAFASDYKIKDGPNDAGDMFERPGRPADYFPSPFPNEQAARA ANGGAAPPDLSLITKARSYGRGFPWFIFDFFTQYQEQGPDYVSAVLQGFEEKVPEGVTIP EGSYYNKYFPGHAIKMPKPLSDGQVTYDDGSPATVAQYSKDVTTFLMWTAEPHMEARKRL GFQVFVFLIIFAGLMYFTKKKVWADSH
CBSP6 S03021 A00161 S00429 03-Aug-1984 02-Aug-1994 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 spinach chloroplast spinach chloroplast Spinacia oleracea Westhoff, P. Herrmann, R.G. Eur. J. Biochem. 1711988551-564 Complex RNA maturation in chloroplasts. MUID88151952 S03021 not compared with conceptual translation DNA 1-22 this sequence is a revision to the sequence from reference S00429 Widger, W.R. Cramer, W.A. Herrmann, R.G. Trebst, A. unpublished results, 1984, cited by Widger, W.R., Cramer, W.A., Herrmann, R.G., Trebst, A., Proc. Natl. Acad. Sci. U.S.A. 81, 674-678 1984 A00161 nucleic acid sequence not shown DNA 'MIGSKNVSRFRRLRMI',21-215 Heinemeyer, W. Alt, J. Herrmann, R.G. Curr. Genet. 81984543-549 Nucleotide sequence of the clustered genes for apocytochrome b6 and subunit 4 of the cytochrome b/f complex in the spinach plastid chromosome. S00429 DNA 'MIGSKNVSRFRRLRMI',21-215 EMBLX07106 NIDg12283 this sequence has been revised in reference S03021 This cytochrome is the chloroplast counterpart of the mitochondrial cytochrome b. petB chloroplast 2/3 cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRP TVTDAFASVQYIMTEVNFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVT GVVLGVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTL TRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
CBZM6R S08592 31-Dec-1991 31-Dec-1991 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6, splice form 2 maize chloroplast maize chloroplast Zea mays Rock, C.D. Barkan, A. Taylor, W.C. Curr. Genet. 12198769-77 The maize plastid psbB-psbF-petB-petD gene cluster: spliced and unspliced petB and petD RNAs encode alternative products. MUID88210525 S08592 DNA 1-215 EMBLX05422 NIDg12434 PIDNCAA28999.1 PIDg311718 For splice form 1, see PIR:S58581. petB chloroplast 2/3 cytochrome b6 cytochrome b6 homology alternative splicing chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRP TVTEAFSSVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVT GVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPEAIPVIGSPLVELLRGSASVGQSTL TRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL
S04149 S04149 JN0381 07-Jun-1990 02-Aug-1994 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6, splice form 1 barley chloroplast barley chloroplast Hordeum vulgare Reverdatto, S.V. Andreeva, A.V. Buryakova, A.A. Chakhmakhcheva, O.G. Efimov, V.A. Nucleic Acids Res. 1719892859-2860 Nucleotide sequence of the 5.2 kbp barley chloroplast DNA fragment, containing psbB-psbH-petB-petD gene cluster. MUID89240047 S04149 DNA 1-232 EMBLX14107 NIDg11593 PIDNCAA32267.1 PIDg11596 For splice form 2, see PIR:S09186. petB chloroplast cytochrome b6 cytochrome b6 homology alternative splicing chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 32-232 binding-site heme iron (His) (axial ligands) (low potential) 103,204 predicted binding-site heme iron (His) (axial ligands) (high potential) 117,219 predicted 232 complete MKFSYTALRGGRGLVTYLNKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTC FLVQVATGFAMTFYYRPTVTEAFSSVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFR VYLTGGFKKPRELTWVTGVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGS PLVELLRGSASVGQSTLTRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL
CBNT6 A00162 30-Jun-1987 30-Jun-1987 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 cytochrome b563 common tobacco chloroplast common tobacco chloroplast Nicotiana tabacum Sugiura, M. submitted to the EMBL Data Library August1986 A00162 DNA 1-215 cv. Bright Yellow 4 Shinozaki, K. Ohme, M. Tanaka, M. Wakasugi, T. Hayashida, N. Matsubayashi, T. Zaita, N. Chunwongse, J. Obokata, J. Yamaguchi-Shinozaki, K. Ohto, C. Torazawa, K. Meng, B.Y. Sugita, M. Deno, H. Kamogashira, T. Yamada, K. Kusuda, J. Takaiwa, F. Kato, A. Tohdoh, N. Shimada, H. Sugiura, M. EMBO J. 519862043-2049 The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. annotation gene organization, sites, features This cytochrome is one of the components of a specific stoichiometric cytochrome b6-f complex that contains two molecules of cytochrome b6, one cytochrome f, and one nonheme iron-sulfur center. petB chloroplast 2/3 cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRP TVTEAFASVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVT GVVLAVLTASFGVTGYSLPWDQVGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTL TRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL
CBRZ6 JQ0256 S05136 31-Mar-1990 31-Mar-1990 31-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0256 DNA 1-215 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05136 nucleic acid sequence not shown translation not shown DNA 1-215 EMBLX15901 NIDg11957 PIDNCAA33977.1 PIDg669082 cv. Nihonbare This cytochrome is one of the components of a specific stoichiometric cytochrome b6-f complex that contains two molecules of cytochrome b6, one cytochrome f and one nonheme iron-sulfur center. petB CP1232-71237,72049-72690 chloroplast 2/3 cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRP TVTEAFSSVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVT GVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTL TRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
S09186 S09186 JN0348 07-Jun-1990 02-Aug-1994 16-Jun-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6, splice form 2 barley chloroplast barley chloroplast Hordeum vulgare Reverdatto, S.V. Andreeva, A.V. Buryakova, A.A. Chakhmakhcheva, O.G. Efimov, V.A. Nucleic Acids Res. 1719892859-2860 Nucleotide sequence of the 5.2 kbp barley chloroplast DNA fragment, containing psbB-psbH-petB-petD gene cluster. MUID89240047 S09186 DNA 1-215 EMBLX14107 NIDg11593 PIDNCAA32266.1 PIDg1617031 For splice form 1, see PIR:S04149. petB chloroplast 2/3 cytochrome b6 cytochrome b6 homology alternative splicing chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRP TVTEAFSSVQYIMTEANFGWLIRSVHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVT GVVLAVLTASFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGSPLVELLRGSASVGQSTL TRFYSLHTFVLPLLTAVFMLMHFPMIRKQGISGPL
CBLV6 S01552 S02432 A00163 30-Jun-1987 30-Jun-1987 21-Jul-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Fukuzawa, H. Kohchi, T. Sano, T. Shirai, H. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988333-351 Structure and organization of Marchantia polymorpha chloroplast genome. III. Gene organization of the large single copy region from rbcL to trnI(CAU). MUID89068687 S01552 DNA 1-215 EMBLX04465 NIDg11640 PIDNCAA28115.1 PIDg4376232 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features Fukuzawa, H. Yoshida, T. Kohchi, T. Okumura, T. Sawano, Y. Ohyama, K. FEBS Lett. 220198761-66 Splicing of group II introns in mRNAs coding for cytochrome b6 and subunit IV in the liverwort Marchantia polymorpha chloroplast genome. Exon specifying a region coding for two genes with the spacer region. S02432 not compared with conceptual translation mRNA 1-8 petB chloroplast 2/3 cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MGKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCLGGITLTCFLVQVATGFAMTFYYRP TVTEAFSSVQYIMTEVNFGWLIRSVHRWSASMMVLMMILHIFRVYLTGGFKKPRELTWVT GVILAVLTVSFGVTGYSLPWDQIGYWAVKIVTGVPEAIPIIGSPLVELLRGSVSVGQSTL TRFYSLHTFVLPLLTAIFMLMHFLMIRKQGISGPL
S34548 S34548 S34915 S41617 30-Sep-1993 02-Aug-1994 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 Euglena gracilis chloroplast chloroplast Euglena gracilis Hallick, R.B. Hong, L. Drager, R.G. Favreau, M. Monfort, A. Orsat, B. Spielmann, A. Stutz, E. submitted to the EMBL Data Library January1993 The complete sequence of the Euglena gracilis chloroplast genome (tentative). S34548 DNA 1-215 EMBLX70810 NIDg415327 PIDNCAA50129.1 PIDg415785 strain Pringsheim Z Hallick, R.B. Hong, L. Drager, R.G. Favreau, M.R. Monfort, A. Orsat, B. Spielmann, A. Stutz, E. Nucleic Acids Res. 2119933537-3544 Complete sequence of Euglena gracilis chloroplast DNA. MUID93347989 S34915 nucleic acid sequence not shown translation not shown DNA 1-215 EMBLX70810 NIDg415327 PIDNCAA50129.1 PIDg415785 the nucleotide sequence was submitted to the EMBL Data Library, January 1993 Hong, L. Hallick, R.B. Curr. Genet. 251994270-281 Gene structure and expression of a novel Euglena gracilis chloroplast operon encoding cytochrome b6 and the beta and epsilon subunits of the H(+)-ATP synthase complex. MUID95007823 S41617 preliminary DNA 1-215 EMBLX70810 NIDg415327 PIDNCAA50129.1 PIDg415785 the authors translated the codon TTC for residue 8 as Leu petB chloroplast 8/2; 22/1 cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSRVYDWFEERLEIQAIADDVSSKYVPPHVNIFYCLGGITFTCFIIQVATGFAMTFYYRP TVTEAFLSVKYIMNEVNFGWLIRSIHRWSASMMVLMMILHVCRVYLTGGFKKPRELTWVT GIILAILTVSFGVTGYSLPWDQVGYWAVKIVTGVPEAIPLIGNFIVELLRGSVSVGQSTL TRFYSLHTFVLPLLTATFMLGHFLMIRKQGISGPL
CBKL6P S06159 30-Sep-1991 30-Sep-1991 31-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 Chlorella protothecoides chloroplast chloroplast Chlorella protothecoides Reimann, A. Kueck, U. Plant Mol. Biol. 131989255-256 Nucleotide sequence of the plastid genes for apocytochrome b(6) (petB) and subunit IV of the cytochrome b(6)-f complex (petD) from the green alga Chlorella protothecoides: lack of introns. MUID92003673 S06159 DNA 1-215 EMBLX15244 NIDg18092 PIDNCAA33322.1 PIDg18093 petB chloroplast cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKIYDWFEERLEIQSIADDISSKYVPPHVNIFYCFGGITFTCFLVQVATGFAMTFYYRP TVAEAFTSVQYLMTQVNFGWLIRSIHRWSASMMVLMMILHIFRVYLTGGFKKPRELTWVT GVLMAVCTVSFGVTGYSLPWDQIGYWAVKIVTGVPDAIPVIGQVLLELLRGGVAVGQSTL TRFYSLHTFVLPLFTAVFMLMHFLMIRKQGISGPL
S21253 S21253 S16917 03-Feb-1994 02-Aug-1994 03-Mar-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 Chlamydomonas reinhardtii chloroplast chloroplast Chlamydomonas reinhardtii Huang, C. Liu, X.Q. Plant Mol. Biol. 181992985-988 Nucleotide sequence of the frxC, petB and trnL genes in the chloroplast genome of Chlamydomonas reinhardtii. MUID92256821 S21253 translation not shown DNA 1-215 EMBLX62905 NIDg12497 PIDNCAA44690.1 PIDg12499 Bueschlen, S. Choquet, Y. Kuras, R. Wollman, F.A. FEBS Lett. 2841991257-262 Nucleotide sequences of the continuous and separated petA, petB and petD chloroplast genes in Chlamydomonas reinhardtii. MUID91285146 S16917 DNA 1-215 EMBLX72918 NIDg603530 PIDNCAA51423.1 PIDg288909 petB chloroplast cytochrome b6 cytochrome b6 homology chloroplast chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MSKVYDWFEERLEIQAIADDITSKYVPPHVNIFYCIGGITFTCFLVQVATGFAMTFYYRP TVAEAFASVQYIMTDVNFGWLIRSIHRWSASMMVLMMVLHVFRVYLTGGFKRPRELTWVT GVIMAVCTVSFGVTGYSLPWDQVGYWAVKIVTGVPDAIPGVGGFIVELLRGGVGVGQATL TRFYSLHTFVLPLLTAVFMLMHFLMIRKQGISGPL
A30807 A30807 01-Dec-1989 02-Aug-1994 02-Jun-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) cytochrome b6 Nostoc sp. Nostoc sp. Kallas, T. Spiller, S. Malkin, R. J. Biol. Chem. 263198814334-14342 Characterization of two operons encoding the cytochrome b-6-f complex of the cyanobacterium Nostoc PCC 7906. Highly conserved sequences but different gene organization than in chloroplasts. MUID89008280 A30807 DNA 1-215 GBJ03967 NIDg145022 PIDNAAA23330.1 PIDg145023 PCC 7906 cytochrome b6 cytochrome b6 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase photosynthesis thylakoid domain cytochrome b6 homology 15-215 binding-site heme iron (His) (axial ligands) (low potential) 86,187 predicted binding-site heme iron (His) (axial ligands) (high potential) 100,202 predicted 215 complete MANVYDWFEERLEIQAIAEDVTSKYVPPHVNIFYCLGGITLTCFLIQFATGFAMTFYYKP TVAEAFSSVEYIMNEVNFGWLIRSIHRWSASMMVLMMILHVFRVYLTGGFKKPRELTWVS GVILAVITVSFGVTGYSLPWDQVGYWAVKIVSGVPEAIPVVGVLISDLLRGGSSVGQATL TRYYSAHTFVLPWLIAVFMLFHFLMIRKQGISGPL
WMLV17 A00166 S01553 S02433 30-Jun-1987 30-Jun-1987 11-Jun-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex protein 4 liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Ohyama, K. submitted to the EMBL Data Library October1986 A00166 DNA 1-160 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features Fukuzawa, H. Kohchi, T. Sano, T. Shirai, H. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988333-351 Structure and organization of Marchantia polymorpha chloroplast genome. III. Gene organization of the large single copy region from rbcL to trnI(CAU). MUID89068687 S01553 not compared with conceptual translation DNA 1-160 GBX04465 GBY00686 NIDg11640 PIDNCAA28116.1 PIDg453594 Fukuzawa, H. Yoshida, T. Kohchi, T. Okumura, T. Sawano, Y. Ohyama, K. FEBS Lett. 220198761-66 Splicing of group II introns in mRNAs coding for cytochrome b6 and subunit IV in the liverwort Marchantia polymorpha chloroplast genome. Exon specifying a region coding for two genes with the spacer region. S02433 preliminary DNA 1-160 petD chloroplast 3/2 plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MGVTKKPDLSDPILRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACTVGLAVLEPS MIGEPANPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMAAVPAGLLTVPFLENVNKF QNPFRRPVATTVFLIGTVVALWLGIGAALPIDKSLTLGLF
S58582 S58582 S08593 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b/f complex 17K protein cytochrome b6-f complex chain IV maize chloroplast maize chloroplast Zea mays Maier, R.M. Neckermann, K. Igloi, G.L. Koessel, H. J. Mol. Biol. 2511995614-628 Complete sequence of the maize chloroplast genome: gene content, hotspots of divergence and fine tuning of genetic information by transcript editing. MUID95395841 S58582 nucleic acid sequence not shown translation not shown DNA 1-160 EMBLX86563 NIDg902200 PIDNCAA60316.1 PIDg902252 the nucleotide sequence was submitted to the EMBL Data Library, April 1995 Rock, C.D. Barkan, A. Taylor, W.C. Curr. Genet. 12198769-77 The maize plastid psbB-psbF-petB-petD gene cluster: spliced and unspliced petB and petD RNAs encode alternative products. MUID88210525 S08593 DNA 1-68 EMBLX05422 NIDg12434 PIDNCAA29001.1 PIDg311719 petD chloroplast 3/2 plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast electron transfer membrane-associated complex oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPS MIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKF QNPFRRPVATTVFLIGTAVALWLGIGATLPIDKSLTLGLF
WMSP17 S00458 S03022 A00164 03-Aug-1984 02-Jul-1996 23-Mar-2001
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex chain IV spinach chloroplast spinach chloroplast Spinacia oleracea Heinemeyer, W. Alt, J. Herrmann, R.G. Curr. Genet. 81984543-549 Nucleotide sequence of the clustered genes for apocytochrome b6 and subunit 4 of the cytochrome b/f complex in the spinach plastid chromosome. S00458 DNA 'IYKNSPILI',4-160 EMBLX07106 this sequence has been revised in reference S03021 Westhoff, P. Herrmann, R.G. Eur. J. Biochem. 1711988551-564 Complex RNA maturation in chloroplasts. MUID88151952 S03022 DNA 1-22 Widger, W.R. Cramer, W.A. Herrmann, R.G. Trebst, A. unpublished results, 1984, cited by Widger, W.R., Cramer, W.A., Herrmann, R.G., Trebst, A., Proc. Natl. Acad. Sci. U.S.A. 81, 674-678 1984 A00164 nucleic acid sequence not shown DNA 22-27,32-116,118-160 This polypeptide is an essential component of the cytochrome b6-f complex; its sequence is homologous with that of the carboxyl end of mitochondrial cytochrome b. petD chloroplast 3/2 plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPS MIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMASVPAGLLTVPFLENVNKF QNPFRRPVATTVFLVGTVVALWLGIGATLPIDKSLTLGLF
S14962 S14962 S05315 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex chain IV wheat chloroplast common wheat chloroplast Triticum aestivum Hird, S.M. Wilson, R.J. Dyer, T.A. Gray, J.C. Plant Mol. Biol. 161991745-747 Nucleotide sequence of the wheat chloroplast petB and petD genes encoding apocytochrome b-563 and subunit IV of the cytochrome bf complex. MUID91329710 S14962 DNA 1-160 EMBLX54751 NIDg12361 PIDNCAA38552.1 PIDg12364 Hird, S.M. Dyer, T.A. Gray, J.C. Nucleic Acids Res. 1719896394 Nucleotide sequence of the rpoA gene in wheat chloroplast DNA. MUID89366674 S05315 DNA 149-160 EMBLX15595 NIDg12371 PIDNCAA33619.1 PIDg12373 petD chloroplast 3/2 plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast electron transfer membrane-associated complex oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPS MIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLFTVPFLENVNKF QNPFRRPVATTVFLIGTVVALWLGIGATLPIDKSLTLGLF
WMRZ17 JQ0257 S05137 31-Mar-1990 31-Mar-1990 11-Jun-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex protein 4 rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0257 DNA 1-160 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05137 nucleic acid sequence not shown translation not shown DNA 1-160 EMBLX15901 NIDg11957 PIDNCAA33978.1 PIDg669083 cv. Nihonbare This polypeptide of unknown function is one of the components of cytochrome b6-f complex; its sequence is homologous with that of carboxyl end of mitochondrial cytochrome b. petD CP72883-72890,73636-74110 chloroplast 3/2 plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MGVTKKPDLNDPVLRAKLAKGMGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPS MIGEPADPFATPLEILPEWYFFPVFQILRTVPNKLLGVLLMVSVPTGLLTVPFLENVNKF QNPFRRPVATTVFLIGTAVALWLGIGATLPIEKSLTLGLF
WMNT17 A00165 30-Jun-1987 30-Jun-1987 24-Feb-1995
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex protein 4 common tobacco chloroplast common tobacco chloroplast Nicotiana tabacum Sugiura, M. submitted to the EMBL Data Library August1986 A00165 DNA 1-139 cv. Bright Yellow 4 Shinozaki, K. Ohme, M. Tanaka, M. Wakasugi, T. Hayashida, N. Matsubayashi, T. Zaita, N. Chunwongse, J. Obokata, J. Yamaguchi-Shinozaki, K. Ohto, C. Torazawa, K. Meng, B.Y. Sugita, M. Deno, H. Kamogashira, T. Yamada, K. Kusuda, J. Takaiwa, F. Kato, A. Tohdoh, N. Shimada, H. Sugiura, M. EMBO J. 519862043-2049 The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. annotation gene organization, sites, features This polypeptide of unknown function is one of the components of the cytochrome b6-f complex; its sequence is homologous with that of the carboxyl end of mitochondrial cytochrome b. petD chloroplast plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 3-123 139 complete MGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYF FPVFQILRTVPNKLLGVLLMVSVPAGLLTVPFLENVNKFQNPFRRPVATTVFLIGTAVAL WLGIGATLPIDKSLTLGLF
S07297 S07297 S04385 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 15.2K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex protein 4 garden pea chloroplast garden pea chloroplast Pisum sativum Phillips, A.L. Gray, J.C. Mol. Gen. Genet. 1941984477-484 Location and nucleotide sequence of the gene for the 15.2 kDa polypeptide of the cytochrome b-f complex from pea chloroplasts. S07297 DNA 1-139 EMBLX00535 NIDg12150 PIDNCAA25212.1 PIDg12151 Purton, S. Gray, J.C. Mol. Gen. Genet. 217198977-84 The plastid rpoA gene encoding a protein homologous to the bacterial RNA polymerase alpha subunit is expressed in pea chloroplasts. MUID89364695 S04385 DNA 115-139 EMBLX15645 NIDg12178 PIDNCAA33669.1 PIDg12181 petD chloroplast plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast electron transfer membrane-associated complex oxidoreductase photosynthesis thylakoid transmembrane protein domain plastoquinol--plastocyanin reductase 17K protein homology 3-123 domain transmembrane 15-36 predicted domain transmembrane 74-93 predicted domain transmembrane 106-130 predicted 139 complete MGHNYYGEPAWPNDLLYIFPVVILGTIACNVGLAVLEPSMIGEPADPFATPLEILPEWYF FPVFQILRTVPNKLLGVLLMVSVPAGLLTVPFLENVNKFQNPFRRPVATTVFLIGTVVAL WLGIGATLPIEKSLTLGLF
WMKL17 S06160 S12478 30-Sep-1991 30-Sep-1991 11-Jun-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex chain IV Chlorella protothecoides chloroplast chloroplast Chlorella protothecoides Reimann, A. Kueck, U. Plant Mol. Biol. 131989255-256 Nucleotide sequence of the plastid genes for apocytochrome b(6) (petB) and subunit IV of the cytochrome b(6)-f complex (petD) from the green alga Chlorella protothecoides: lack of introns. MUID92003673 S06160 DNA 1-160 EMBLX15244 Reimann, A. submitted to the EMBL Data Library May1989 S12478 DNA 1-96,'G',98-160 EMBLX15244 NIDg18092 PIDNCAA33323.1 PIDg18094 petD chloroplast plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MAVTKKPDLSDPQLRAKLAKGMGHNYYGEPAWPNDIFYMFPVVIFGTFAGVIGLAVLDPA AIGEPANPFATPLEILPEWYFYPVFQLLRTVPNKLLVVLLMAAVPAGLITVPFIKIYNKF QNPFRRPVATTVFLVGTVAAIWLGIGAALPIDISLTLGLF
S05340 S05340 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex chain IV green alga KS3/2 chloroplast chloroplast Oocystaceae gen. sp. Kueck, U. Mol. Gen. Genet. 2181989257-265 The intron of a plastid gene from a green alga contains an open reading frame for a reverse transcriptase-like enzyme. MUID89384450 S05340 not compared with conceptual translation DNA 1-160 petD chloroplast plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MSVTKKPDLTDPVLKEKFAKGMGHNYYGEPAWPNDLLYIFPVVILGTFACVIGLSVLDPA AIGEPANPFATPLEILPEWYFYPVFQLLRTVPNKLLGVLLMAAVPAGLITVPFIENINKF QNPYRRPIATTLFLVGTLVAVWLGIGATLPIEISLTFGLF
S04089 S04089 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex chain IV Chlamydomonas eugametos chloroplast chloroplast Chlamydomonas eugametos Turmel, M. Boulanger, J. Bergeron, A. Nucleic Acids Res. 1719893593 Nucleotide sequence of the chloroplast petD gene of Chlamydomonas eugametos. MUID89263804 S04089 DNA 1-160 EMBLX14503 NIDg11349 PIDNCAA32656.1 PIDg11350 petD chloroplast plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MSVTKKPDLNDPVLRAKLAKGFGHNTYGEPAWPNDLLYIFPVVIFGTFACCIGLAVLDPA AMGEPANPFATPLEILPEWYFYPVFQILRTVPNKLLGVLAMAAVPVGLLTVPFIESINKF QNPYRRPIATILFLVGTLVAVWLGIGATFPIDISLTLGLF
S16918 S16918 S26837 S32589 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6/f complex chain IV Chlamydomonas reinhardtii chloroplast chloroplast Chlamydomonas reinhardtii Bueschlen, S. Choquet, Y. Kuras, R. Wollman, F.A. FEBS Lett. 2841991257-262 Nucleotide sequences of the continuous and separated petA, petB and petD chloroplast genes in Chlamydomonas reinhardtii. MUID91285146 S16918 DNA 1-160 EMBLX72919 NIDg1009385 PIDNCAA51424.1 PIDg603532 Yu, W. Spreitzer, R.J. Nucleic Acids Res. 191991957 Sequences of trnR-ACG and petD that contain a tRNA-like element within the chloroplast genome of Chlamydomonas reinhardtii. MUID91204459 S26837 nucleic acid sequence not shown translation not shown DNA 1-160 EMBLX56700 NIDg11461 PIDNCAA40030.1 PIDg11462 the nucleotide sequence was submitted to the EMBL Data Library, November 1990 petD chloroplast plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology chloroplast membrane-associated complex oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MSVTKKPDLSDPVLKAKLAKGMGHNTYGEPAWPNDLLYMFPVVILGTFACVIGLSVLDPA AMGEPANPFATPLEILPEWYFYPVFQILRVVPNKLLGVLLMAAVPAGLITVPFIESINKF QNPYRRPIATILFLLGTLVAVWLGIGSTFPIDISLTLGLF
B30807 B30807 10-Sep-1999 10-Sep-1999 02-Jun-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex 17K protein cytochrome b6-f complex protein 4 Nostoc sp. Nostoc sp. Kallas, T. Spiller, S. Malkin, R. J. Biol. Chem. 263198814334-14342 Characterization of two operons encoding the cytochrome b-6-f complex of the cyanobacterium Nostoc PCC 7906. Highly conserved sequences but different gene organization than in chloroplasts. MUID89008280 B30807 DNA 1-160 GBJ03967 NIDg145022 PIDNAAA23331.1 PIDg145024 PCC 7906 plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MATQKKPDLSDPQLRAKLAKGMGHNYYGEPAWPNDLLYVFPIVIMGSFAAIVALAVLDPA MTGEPANPFATPLEILPEWYLYPVFQILRSLPNKLLGVLAMASVPLGLILVPFIENVNKF QNPFRRPVATTVFLFGTLVTLWLGIGAALPLDKSLTLGLF
A61088 A61088 S76298 S15474 10-Sep-1999 10-Sep-1999 16-Jun-2000
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein cytochrome b6-f complex chain IV plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain IV Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Osiewacz, H.D. Arch. Microbiol. 1571992336-342 Construction of insertion mutants of Synechocystis sp. PCC 6803: evidence for an essential function of subunit IV of the cytochrome b-6/f complex. MUID92272582 A61088 DNA 1-160 EMBLX58522 NIDg47376 PIDNCAA41412.1 PIDg47377 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S76298 preliminary DNA 1-160 EMBLD64000 GBAB001339 NIDg1001484 PIDNBAA10150.1 PIDg1001523 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 petD plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology oxidoreductase photosynthesis thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MSIIKKPDLSDPDLRAKLAKGMGHNYYGEPAWPNDILYMFPICILGALGLIAGLAILDPA MIGEPADPFATPLEILPEWYLYPTFQILRILPNKLLGIAGMAAIPLGLMLVPFIESVNKF QNPFRRPIAMTVFLFGTAAALWLGAGATFPIDKSLTLGLF
S26194 S26194 S18124 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) 17K protein Synechococcus sp. (PCC 7002) Synechococcus sp. PCC 7002 Brand, S.N. Tan, X. Widger, W.R. Plant Mol. Biol. 201992481-491 Cloning and sequencing of the petBD operon from the cyanobacterium Synechococcus sp. PCC 7002. MUID93043038 S26194 DNA 1-160 EMBLX63049 NIDg38962 PIDNCAA44775.1 PIDg38964 petD plastoquinol--plastocyanin reductase 17K protein plastoquinol--plastocyanin reductase 17K protein homology oxidoreductase thylakoid domain plastoquinol--plastocyanin reductase 17K protein homology 24-144 160 complete MSIMKKPDLSDPKLRAKLAQNMGHNYYGEPAWPNDILFTFPICIAGTIGLITGLAILDPA MIGEPGNPFATPLEILPEWYLYPVFQILRVLPNKLLGIACQGAIPLGLMMVPFIESVNKF QNPFRRPVAMAVFLFGTAVTLWLGAGACFPIDESLTLGLF
WMRZ4 JQ0245 S05125 31-Mar-1990 31-Mar-1990 20-Aug-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6-f complex protein 5 rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0245 DNA 1-37 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05125 nucleic acid sequence not shown translation not shown DNA 1-37 EMBLX15901 NIDg11957 PIDNCAA33967.1 PIDg12006 cv. Nihonbare petE CP63799-63912 chloroplast cytochrome b6-f complex 4.2K protein chloroplast electron transfer oxidoreductase photosynthesis 37 complete MIEVFLFGIVLGLIPITLAGLFVTAYLQYRRGDQLDL
A32159 A32159 S58570 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6-f complex 4K protein cytochrome b6-f complex chain 5 maize chloroplast maize chloroplast Zea mays Haley, J. Bogorad, L. Proc. Natl. Acad. Sci. U.S.A. 8619891534-1538 A 4-kDa maize chloroplast polypeptide associated with the cytochrome b-6-f complex: subunit 5, encoded by the chloroplast petE gene. MUID89160811 A32159 preliminary DNA 1-37 GBJ04502 NIDg342582 PIDNAAA84480.1 PIDg342588 Maier, R.M. Neckermann, K. Igloi, G.L. Koessel, H. J. Mol. Biol. 2511995614-628 Complete sequence of the maize chloroplast genome: gene content, hotspots of divergence and fine tuning of genetic information by transcript editing. MUID95395841 S58570 nucleic acid sequence not shown translation not shown DNA 1-37 EMBLX86563 NIDg902200 PIDNCAA60304.1 PIDg902240 the nucleotide sequence was submitted to the EMBL Data Library, April 1995 chloroplast cytochrome b6-f complex 4.2K protein chloroplast electron transfer membrane-associated complex oxidoreductase photosynthesis 37 complete MIEVFLFGIVLGLIPITLAGLFVTAYLQYRRGDQLDL
S20474 S20474 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6-f complex chain V southern Asian dodder chloroplast southern Asian dodder chloroplast Cuscuta reflexa Haberhausen, G. Valentin, K. Zetsche, K. Mol. Gen. Genet. 2321992154-161 Organization and sequence of photosynthetic genes from the plastid genome of the holoparasitic flowering plant Cuscuta reflexa. MUID92204128 S20474 DNA 1-37 EMBLX61698 NIDg58330 PIDNCAA43864.1 PIDg58331 petG chloroplast cytochrome b6-f complex 4.2K protein chloroplast electron transfer oxidoreductase photosynthesis 37 complete MIEVFLFGIVLGLIPITLAGLFVTAYLQYRRGGRLDV
A05054 S01541 A05054 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Fukuzawa, H. Kohchi, T. Sano, T. Shirai, H. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988333-351 Structure and organization of Marchantia polymorpha chloroplast genome. III. Gene organization of the large single copy region from rbcL to trnI(CAU). MUID89068687 S01541 DNA 1-37 EMBLX04465 NIDg11640 PIDNCAA28104.1 PIDg11692 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features chloroplast cytochrome b6-f complex 4.2K protein chloroplast oxidoreductase 37 complete MVEALLSGIVLGLIPITLLGLFVTAYLQYRRGDQLDL
S51367 S51367 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6/f complex chain V Chlamydomonas eugametos chloroplast chloroplast Chlamydomonas eugametos Turmel, M. Otis, C. Curr. Genet. 27199454-61 The chloroplast gene cluster containing psbF, psbL, petG and rps3 is conserved in Chlamydomonas. MUID95269309 S51367 DNA 1-37 EMBLL29282 NIDg575472 PIDNAAA84158.1 PIDg575475 petG chloroplast cytochrome b6-f complex 4.2K protein chloroplast electron transfer membrane-associated complex oxidoreductase photosynthesis thylakoid 37 complete MVEPLLSGIVLGLVPVTIAGLFVTAYLQYRRGDLATF
S26880 S26880 T08172 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6-f complex 4K protein Chlamydomonas reinhardtii chloroplast chloroplast Chlamydomonas reinhardtii Fong, S.E. Surzycki, S.J. Curr. Genet. 211992527-530 Organization and structure of plastome psbF, psbL, petG and ORF712 genes in Chlamydomonas reinhardtii. MUID92315354 S26880 DNA 1-37 EMBLX66250 NIDg393459 PIDNCAA46979.1 PIDg393462 petG chloroplast cytochrome b6-f complex 4.2K protein chloroplast electron transfer membrane-associated complex oxidoreductase photosynthesis thylakoid 37 complete MVEPLLCGIVLGLVPVTIAGLFVTAYLQYLRGDLATY
S06916 S06916 T06908 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6-f complex 4K protein Cyanophora paradoxa cyanelle cyanelle Cyanophora paradoxa Stirewalt, V.L. Bryant, D.A. Nucleic Acids Res. 17198910095 Molecular cloning and nucleotide sequence of the petG gene of the cyanelle genome of Cyanophora paradoxa. MUID90098772 S06916 DNA 1-37 EMBLX16974 NIDg12548 PIDNCAA34846.1 PIDg12549 Stirewalt, V.L. Michalowski, C.B. Luffelhardt, W. Bohnert, H.J. Bryant, D.A. submitted to the EMBL Data Library July1995 Nucleotide sequence of the cyanelle genome from Cyanophora paradoxa. T06908 preliminary translated from GB/EMBL/DDBJ DNA 1-37 EMBLU30821 NIDg1016083 PIDNAAA81251.1 PIDg1016164 strain Pringsheim LB555 petG 65 cyanelle cytochrome b6-f complex 4.2K protein cyanelle electron transfer membrane-associated complex oxidoreductase photosynthesis 37 complete MVEPLLSGIVLGLIPVTLIGLFVAAYLQYRRGNQFEF
S26087 S26087 S34880 S34513 10-Sep-1999 10-Sep-1999 10-Sep-1999
plastoquinol--plastocyanin reductase (EC 1.10.99.1) chain V cytochrome b6-f complex chain V Euglena gracilis chloroplast chloroplast Euglena gracilis Hallick, R.B. submitted to the EMBL Data Library March1992 S26087 DNA 1-37 EMBLZ11874 NIDg14353 PIDNCAA77909.1 PIDg14359 strain Z Hallick, R.B. Hong, L. Drager, R.G. Favreau, M.R. Monfort, A. Orsat, B. Spielmann, A. Stutz, E. Nucleic Acids Res. 2119933537-3544 Complete sequence of Euglena gracilis chloroplast DNA. MUID93347989 S34880 nucleic acid sequence not shown translation not shown DNA 1-37 EMBLX70810 NIDg415327 PIDNCAA50092.1 PIDg415748 the nucleotide sequence was submitted to the EMBL Data Library, January 1993 petG chloroplast 5/3 cytochrome b6-f complex 4.2K protein chloroplast membrane-associated complex oxidoreductase photosynthesis thylakoid 37 complete MVETLLSGIILGLIPITICGLFFTAYLQYMRSGNSFY
CBBOC6 A24096 28-Dec-1987 28-Dec-1987 13-Jun-1997
cytochrome b-c1 complex 6.4K protein bovine cattle Bos primigenius taurus Schagger, H. Borchart, U. Aquila, H. Link, T.A. von Jagow, G. FEBS Lett. 190198589-94 Isolation and amino acid sequence of the smallest subunit of beef heart b-c1 complex. MUID86005499 A24096 protein 1-56 This protein is the smallest of the 11 polypeptide chains of the cytochrome b-c1 complex; it may be closely linked to the iron-sulfur protein in the complex and function as an iron-sulfur protein binding factor. cytochrome b-c1 6.4K protein membrane protein domain transmembrane 16-36 predicted 56 complete MLTRFLGPRYRQLARNWVPTAQLWGAVGAVGLVSATDSRLILDWVPYINGKFKKDD
CBNT55 S55791 B25714 30-Sep-1987 30-Sep-1987 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain common tobacco chloroplast common tobacco chloroplast Nicotiana tabacum Carrillo, N. Seyer, P. Tyagi, A. Herrmann, R.G. Curr. Genet. 101986619-624 Cytochrome b-559 genes from Oenothera hookeri and Nicotiana tabacum show a remarkably high degree of conservation as compared to spinach. MUID88165110 S55791 DNA 1-83 EMBLX03781 NIDg11794 PIDNCAA27412.1 PIDg11795 Sugiura, M. submitted to the EMBL Data Library August1986 B25714 DNA 1-83 cv. Bright Yellow 4 Shinozaki, K. Ohme, M. Tanaka, M. Wakasugi, T. Hayashida, N. Matsubayashi, T. Zaita, N. Chunwongse, J. Obokata, J. Yamaguchi-Shinozaki, K. Ohto, C. Torazawa, K. Meng, B.Y. Sugita, M. Deno, H. Kamogashira, T. Yamada, K. Kusuda, J. Takaiwa, F. Kato, A. Tohdoh, N. Shimada, H. Sugiura, M. EMBO J. 519862043-2049 The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. annotation gene organization, sites, features psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:F2NT4) chains tightly associated with the reaction center of photosystem II; may be part of the water-oxidation complex photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITGRFDPLEQLDEFSRSF
S00418 S00418 A22550 30-Sep-1989 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain spinach chloroplast spinach chloroplast Spinacia oleracea Herrmann, R.G. Alt, J. Schiller, B. Widger, W.R. Cramer, W.A. FEBS Lett. 1761984239-244 Nucleotide sequence of the gene for apocytochrome b-559 on the spinach plastid chromosome: implications for the structure of the membrane protein. S00418 DNA 1-83 EMBLM35673 NIDg343357 PIDNAAA84628.1 PIDg343358 part of this sequence, including the amino end of the mature protein, was confirmed by protein sequencing Widger, W.R. Cramer, W.A. Hermodson, M. Meyer, D. Gullifor, M. J. Biol. Chem. 25919843870-3876 Purification and partial amino acid sequence of the chloroplast cytochrome b-559. MUID84162067 A22550 protein 2-22,'X',24-28 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S35262) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITGRFDSLEQLDEFSRSF
CBRZ55 JQ0243 S05123 31-Mar-1990 31-Mar-1990 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0243 DNA 1-83 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05123 nucleic acid sequence not shown translation not shown DNA 1-83 EMBLX15901 NIDg11957 PIDNCAA33965.1 PIDg12004 cv. Nihonbare the nucleotide sequence was submitted to the EMBL Data Library, July 1989 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:F2RZ4) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITDRFDSLEQLDEFSRSF
CBWT5E S03621 PW0015 A26015 31-Dec-1992 31-Dec-1992 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain wheat chloroplast common wheat chloroplast Triticum aestivum Webber, A.N. Hird, S.M. Packman, L.C. Dyer, T.A. Gray, J.C. Plant Mol. Biol. 121989141-151 A photosystem II polypeptide is encoded by an open reading frame cotranscribed with genes for cytochrome b-559 in wheat chloroplast DNA. S03621 DNA 1-83 EMBLX15225 NIDg14259 PIDNCAA33294.1 PIDg14260 PW0015 protein 2-7,'X',9-16 Hird, S.M. Willey, D.L. Dyer, T.A. Gray, J.C. Mol. Gen. Genet. 203198695-100 Location and nucleotide sequence of the gene for cytochrome b-559 in wheat chloroplast DNA. A26015 DNA 1-83 EMBLX03776 NIDg12338 PIDNCAA27405.1 PIDg12339 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:F2KT5F) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 experimental domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITDRFDSLEQLDEFSRSF
A29956 A29956 A31182 JN0350 S04062 15-Dec-1988 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain barley chloroplast barley chloroplast Hordeum vulgare Krupinska, K. Berry-Lowe, S. Carlsberg Res. Commun. 53198843-55 Characterization and in vitro expression of the cytochrome b-559 genes of barley I. localization and sequence of the genes. MUID89374539 A29956 DNA 1-83 GBM35977 NIDg336408 PIDNAAA84044.1 PIDg336409 Krupinska, K. Carlsberg Res. Commun. 531988233-246 Characterization and in vitro expression of the cytochrome b-559 genes of barley. II. In vitro transcription and translation. MUID89351277 A31182 DNA 1-83 GBM35616 NIDg336415 PIDNAAA84048.1 PIDg336416 Efimov, V.A. Andreeva, A.V. Reverdatto, S.V. Chakhmakhcheva, O.G. Bioorg. Khim. 1719911369-1385 Nucleotide sequence of the barley chloroplast psbB, psbC, psbE, psbF, psbH gene coding for the polypeptides of photosystem II. MUID92207253 JN0350 DNA 1-83 article in Russian with English abstract Chakhmakhcheva, O.G. Andreeva, A.V. Buryakova, A.A. Reverdatto, S.V. Efimov, V.A. Nucleic Acids Res. 1719892858 Nucleotide sequence of the barley chloroplast psbE, psbF genes and flanking regions. MUID89240046 S04062 DNA 1-15,'C',17-22,'R',24-83 EMBLX14108 NIDg12351 PIDNCAA32270.1 PIDg12352 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S04063) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITDRFDSLEQLDEFSRSF
S03191 S03191 07-Jun-1990 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain rye chloroplast rye chloroplast Secale cereale Kolosov, V.L. Klezovich, O.N. Zolotarev, A.S. Nucleic Acids Res. 1719891760 Nucleotide sequence of the rye chloroplast DNA fragment, comprising psbE and psbF genes. MUID89160331 S03191 DNA 1-83 EMBLX13326 NIDg12230 PIDNCAA31698.1 PIDg12231 the authors translated the codon CCT for residue 28 as Leu psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S03192) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITDRFDSLEQLDEFSRSF
S58568 S58568 29-Nov-1995 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain maize chloroplast maize chloroplast Zea mays Maier, R.M. Neckermann, K. Igloi, G.L. Koessel, H. J. Mol. Biol. 2511995614-628 Complete sequence of the maize chloroplast genome: gene content, hotspots of divergence and fine tuning of genetic information by transcript editing. MUID95395841 S58568 nucleic acid sequence not shown translation not shown DNA 1-83 EMBLX86563 NIDg902200 PIDNCAA60302.1 PIDg902238 the nucleotide sequence was submitted to the EMBL Data Library, April 1995 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S58567) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITDRFDSLEQLDEFSRSF
A48310 A48310 31-Dec-1993 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain garden pea chloroplast garden pea chloroplast Pisum sativum Willey, D.L. Gray, J.C. Curr. Genet. 151989213-220 Two small open reading frames are co-transcribed with the pea chloroplast genes for the polypeptides of cytochrome b-559. MUID89354671 A48310 DNA 1-83 GBX15767 NIDg12152 PIDNCAA33772.1 PIDg12153 chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:B48310) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGERSFADIITSIRYWIIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTETR QGIPLITGRFDSLEQLDEFSRSF
S55789 S55789 27-Oct-1995 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain Hooker's evening primrose chloroplast Hooker's evening primrose chloroplast Oenothera hookeri subsp. hookeri Carrillo, N. Seyer, P. Tyagi, A. Herrmann, R.G. Curr. Genet. 101986619-624 Cytochrome b-559 genes from Oenothera hookeri and Nicotiana tabacum show a remarkably high degree of conservation as compared to spinach. MUID88165110 S55789 DNA 1-83 EMBLX03780 NIDg11923 PIDNCAA27410.1 PIDg11924 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S55790) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGGRSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITGRFDSLEQLDEFSRSF
S01243 S01243 30-Jun-1989 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain evening primrose chloroplast evening primrose chloroplast Oenothera villaricae Schuster, W. Brennicke, A. Nucleic Acids Res. 1619887728 A plastid fragment from the psbE-psbF coding region in the mitochondrial genome of Oenothera berteriana. MUID88319966 S01243 DNA 1-83 EMBLX07951 NIDg11913 PIDNCAA30776.1 PIDg11914 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S01244) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGSTGGRSFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTESR QGIPLITGRFDSLEQLDEFSRSF
CBLV55 S01536 B25809 30-Sep-1987 30-Sep-1987 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Fukuzawa, H. Kohchi, T. Sano, T. Shirai, H. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988333-351 Structure and organization of Marchantia polymorpha chloroplast genome. III. Gene organization of the large single copy region from rbcL to trnI(CAU). MUID89068687 S01536 DNA 1-83 EMBLX04465 NIDg11640 PIDNCAA28101.1 PIDg11689 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:F2LV4) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-83 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-83 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 83 complete MSGNTGERPFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTENR QEVPLITGRFNSLEQIDEFTKSF
S53882 S53882 B41170 27-Oct-1995 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain Chlamydomonas reinhardtii chloroplast chloroplast Chlamydomonas reinhardtii Mor, T.S. Ohad, I. Hirschberg, J. Pakrasi, H.B. Mol. Gen. Genet. 2461995600-604 An unusual organization of the genes encoding cytochrome b(559) in Chlamydomonas reinhardtii: psbE and psbF genes are separately transcribed from different regions of the plastid chromosome. MUID95214620 S53882 DNA 1-82 EMBLX79565 NIDg1052575 PIDNCAA56102.1 PIDg1052576 de Vitry, C. Diner, B.A. Popot, J.L. J. Biol. Chem. 266199116614-16621 Photosystem II particles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation. MUID91358452 B41170 protein 2-13 psbE chloroplast heterodimer of alpha (psbE) and beta (psbF, see PIR:S53883) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-82 experimental domain transmembrane 19-43 predicted domain thylakoid lumenal 44-82 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 82 complete MAGKPVERPFSDILTSIRYWVIHSITVPALFIAGWLFVSTGLAYDVFGTPRPNEYFTEDR QEAPLITDRFNALEQVKKLSGN
S00689 S00689 S34516 S34883 30-Jun-1989 19-Jul-1996 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain Euglena gracilis chloroplast chloroplast Euglena gracilis Cushman, J.C. Christopher, D.A. Little, M.C. Hallick, R.B. Price, C.A. Curr. Genet. 131988173-180 Organization of the psbE, psbF, orf38, and orf42 gene loci on the Euglena gracilis chloroplast genome. MUID88223485 S00689 DNA 1-81 EMBLX07073 NIDg11492 PIDNCAA30108.1 PIDg11493 Hallick, R.B. Hong, L. Drager, R.G. Favreau, M. Monfort, A. Orsat, B. Spielmann, A. Stutz, E. submitted to the EMBL Data Library January1993 The complete sequence of the Euglena gracilis chloroplast genome (tentative). S34516 DNA 1-81 EMBLX70810 NIDg415327 PIDNCAA50095.1 PIDg415751 Hallick, R.B. Hong, L. Drager, R.G. Favreau, M.R. Monfort, A. Orsat, B. Spielmann, A. Stutz, E. Nucleic Acids Res. 2119933537-3544 Complete sequence of Euglena gracilis chloroplast DNA. MUID93347989 S34883 nucleic acid sequence not shown translation not shown DNA 1-81 EMBLX70810 NIDg415327 PIDNCAA50095.1 PIDg415751 Pringsheim strain Z the nucleotide sequence was submitted to the EMBL Data Library, January 1993 psbE chloroplast 13/3; 23/3 heterodimer of alpha (psbE) and beta (psbF, see PIR:S00690) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-81 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 44-81 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 81 complete MAGSTGERPFSDIITSIRYWVIHSVTIPSLFVGGWIFVSTGIVYDIFGTPRPSEYFTETR QQAPLISDRFNALEQMDQFTK
CBKT5E T06866 S09182 31-Dec-1992 21-May-1999 03-Mar-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain Cyanophora paradoxa cyanelle cyanelle Cyanophora paradoxa Stirewalt, V.L. Michalowski, C.B. Luffelhardt, W. Bohnert, H.J. Bryant, D.A. submitted to the EMBL Data Library July1995 Nucleotide sequence of the cyanelle genome from Cyanophora paradoxa. T06866 translated from GB/EMBL/DDBJ DNA 1-74 EMBLU30821 NIDg1016083 PIDNAAA81209.1 PIDg1016122 strain Pringsheim LB555 Cantrell, A. Bryant, D.A. Prog. Photosyn. Res. 41987659-662 Molecular cloning and nucleotide sequences of the genes encoding cytochrome B-559 from the cyanelle genome of Cyanophora paradoxa. S09182 nucleic acid sequence not shown not compared with conceptual translation DNA 1-29,'FFI',33-74 psbE cyanelle heterodimer of alpha (psbE) and beta (psbF, see PIR:CBKT5F) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chromoprotein cyanelle electron transfer heme heterodimer iron metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-74 predicted domain transmembrane 20-44 predicted domain thylakoid lumenal 45-74 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 24 predicted 74 complete MSGGTTGERPFSDIVTSIRYWVIHTVTIPSLFVAGWLFVSTGLAYDVFGTPRPDEYFTEE RQEVPIINQRFSTN
CBYB55 S00338 S75178 S67978 30-Sep-1990 30-Sep-1990 16-Jun-2000
cytochrome b559 component psbE cytochrome b559 9K component cytochrome b559 alpha chain protein ssr3451 Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Pakrasi, H.B. Williams, J.G.K. Arntzen, C.J. EMBO J. 71988325-332 Targeted mutagenesis of the psbE and psbF genes blocks photosynthetic electron transport: evidence for a functional role of cytochrome b559 in photosystem II. MUID88211541 S00338 DNA 1-81 EMBLX06988 NIDg47430 PIDNCAA30048.1 PIDg47431 the sequence from Fig. 3 is inconsistent with that from Fig. 2 in having 77-Glu Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S75178 nucleic acid sequence not shown translation not shown DNA 1-81 EMBLD90903 GBAB001339 NIDg1652127 PIDNBAA17092.1 PIDg1652168 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 Barbato, R. Polverino de Laureto, P. Rigoni, F. de Martini, E. Giacometti, G.M. Eur. J. Biochem. 2341995459-465 Pigment-protein complexes from the photosynthetic membrane of the cyanobacterium Synechocystis sp. PCC 6803. MUID96128174 S67978 protein 2-6 psbE heterodimer of alpha (psbE) and beta (psbF, see PIR:F2YB4) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component E chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbE 2-81 predicted domain transmembrane 19-43 predicted domain thylakoid lumenal 45-74 predicted binding-site heme iron (His) (axial ligand) (shared with beta chain) 23 predicted 81 complete MSGTTGERPFSDIVTSIRYWVIHSITIPMLFIAGWLFVSTGLAYDAFGTPRPDEYFTQTR QELPILQERYDINQEIQEFNQ
F2NT4 A05065 S55792 A25714 30-Sep-1987 30-Sep-1987 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain common tobacco chloroplast common tobacco chloroplast Nicotiana tabacum Sugiura, M. submitted to the EMBL Data Library August1986 A05065 DNA 1-39 cv. Bright Yellow 4 Shinozaki, K. Ohme, M. Tanaka, M. Wakasugi, T. Hayashida, N. Matsubayashi, T. Zaita, N. Chunwongse, J. Obokata, J. Yamaguchi-Shinozaki, K. Ohto, C. Torazawa, K. Meng, B.Y. Sugita, M. Deno, H. Kamogashira, T. Yamada, K. Kusuda, J. Takaiwa, F. Kato, A. Tohdoh, N. Shimada, H. Sugiura, M. EMBO J. 519862043-2049 The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. annotation gene organization, sites, features Carrillo, N. Seyer, P. Tyagi, A. Herrmann, R.G. Curr. Genet. 101986619-624 Cytochrome b-559 genes from Oenothera hookeri and Nicotiana tabacum show a remarkably high degree of conservation as compared to spinach. MUID88165110 S55792 DNA 1-16,'I',18-39 EMBLX03781 NIDg11794 PIDNCAA27413.1 PIDg11796 psbF chloroplast heterodimer of alpha (psbE, see PIR:CBNT55) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR
F2RZ4 JQ0242 S05122 S08015 31-Mar-1990 31-Mar-1990 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0242 DNA 1-39 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05122 DNA 1-39 EMBLX15901 NIDg11957 PIDNCAA33964.1 PIDg12003 cv. Nihonbare Zhao, X.P. Zhong-Xun, L. Jean-Charles, C. Wu, R. submitted to the EMBL Data Library April1989 S08015 DNA 1-39 EMBLX15057 NIDg11935 PIDNCAA33156.1 PIDg11936 psbF CP62072-61953 chloroplast heterodimer of alpha (psbE, see PIR:CBRZ55) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR
S58567 S58567 29-Nov-1995 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain maize chloroplast maize chloroplast Zea mays Maier, R.M. Neckermann, K. Igloi, G.L. Koessel, H. J. Mol. Biol. 2511995614-628 Complete sequence of the maize chloroplast genome: gene content, hotspots of divergence and fine tuning of genetic information by transcript editing. MUID95395841 S58567 nucleic acid sequence not shown translation not shown DNA 1-39 EMBLX86563 NIDg902200 PIDNCAA60301.1 PIDg902237 the nucleotide sequence was submitted to the EMBL Data Library, April 1995 psbF chloroplast heterodimer of alpha (psbE, see PIR:S58568) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVFFLGSISAMQFIQR
F2KT5F B26015 JG0012 S03622 31-Dec-1992 31-Dec-1992 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 4K component cytochrome b559 beta chain wheat chloroplast common wheat chloroplast Triticum aestivum Hird, S.M. Willey, D.L. Dyer, T.A. Gray, J.C. Mol. Gen. Genet. 203198695-100 Location and nucleotide sequence of the gene for cytochrome b-559 in wheat chloroplast DNA. B26015 DNA 1-39 Webber, A.N. Hird, S.M. Packman, L.C. Dyer, T.A. Gray, J.C. Plant Mol. Biol. 121989141-151 A photosystem II polypeptide is encoded by an open reading frame cotranscribed with genes for cytochrome b-559 in wheat chloroplast DNA. JG0012 DNA 1-39 EMBLX15225 NIDg14259 PIDNCAA33295.1 PIDg14261 psbF chloroplast heterodimer of alpha (psbE, see PIR:CBWT5E) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAIHGLAVPTVFFLGSISAMQFIQR
S03192 S03192 JN0357 07-Jun-1990 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain rye chloroplast rye chloroplast Secale cereale Kolosov, V.L. Klezovich, O.N. Zolotarev, A.S. Nucleic Acids Res. 1719891760 Nucleotide sequence of the rye chloroplast DNA fragment, comprising psbE and psbF genes. MUID89160331 S03192 DNA 1-39 EMBLX13326 NIDg12230 PIDNCAA31699.1 PIDg12232 Kolosov, V.L. Klezovich, O.N. Abdulaev, N.G. Zolotonev, A.S. Bioorg. Khim. 1519891284-1286 Nucleotide sequences of the rye chloroplast psbE, psbF and psbL genes coding for the polypeptides of photosystem II. MUID90073796 JN0357 preliminary DNA 1-39 psbF chloroplast heterodimer of alpha (psbE, see PIR:S03191) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAIHGLAVPTVFFLGSISAMQFIQR
S04063 S04063 B29956 B31182 D31182 JN0351 01-Dec-1989 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain barley chloroplast barley chloroplast Hordeum vulgare Chakhmakhcheva, O.G. Andreeva, A.V. Buryakova, A.A. Reverdatto, S.V. Efimov, V.A. Nucleic Acids Res. 1719892858 Nucleotide sequence of the barley chloroplast psbE, psbF genes and flanking regions. MUID89240046 S04063 DNA 1-39 EMBLX14108 NIDg12351 PIDNCAA32271.1 PIDg12353 Krupinska, K. Berry-Lowe, S. Carlsberg Res. Commun. 53198843-55 Characterization and in vitro expression of the cytochrome b-559 genes of barley I. localization and sequence of the genes. MUID89374539 B29956 DNA 1-39 GBM35977 NIDg336408 PIDNAAA84045.1 PIDg336410 the authors translated the codon CAG for residue 35 as Glu Krupinska, K. Carlsberg Res. Commun. 531988233-246 Characterization and in vitro expression of the cytochrome b-559 genes of barley. II. In vitro transcription and translation. MUID89351277 B31182 DNA 1-39 GBM35616 NIDg336415 PIDNAAA84049.1 PIDg336417 the authors translated the codon CAG for residue 35 as Glu D31182 DNA 'MNLVDPFRRPS',1-39 GBM35616 the authors translated the codon CAG for residue 35 as Glu psbF chloroplast heterodimer of alpha (psbE, see PIR:A29956) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAIHGLAVPTVFFLGSISAMQFIQR
S35262 S35262 S60023 S00419 A24223 10-Dec-1993 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain spinach chloroplast spinach chloroplast Spinacia oleracea Bock, R. Hagemann, R. Koessel, H. Kudla, J. Mol. Gen. Genet. 2401993238-244 Tissue- and stage-specific modulation of RNA editing of the psbF and psbL transcript from spinach plastids - a new regulatory mechanism? MUID93360903 S35262 mRNA 1-39 cv. Matador S60023 DNA 1-25,'S',27-39 cv. Matador 26-Ser is translated as 26-Phe due to RNA editing Herrmann, R.G. Alt, J. Schiller, B. Widger, W.R. Cramer, W.A. FEBS Lett. 1761984239-244 Nucleotide sequence of the gene for apocytochrome b-559 on the spinach plastid chromosome: implications for the structure of the membrane protein. S00419 DNA 1-25,'S',27-39 EMBLM35673 NIDg343357 PIDNAAA84629.1 PIDg343359 Widger, W.R. Cramer, W.A. Hermodson, M. Herrmann, R.G. FEBS Lett. 1911985186-190 A24223 protein 2-10 psbF chloroplast heterodimer of alpha (psbE, see PIR:A22550) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAIHGLAVPTVFFLGSISAMQFIQR
F2LV4 A25809 S01537 30-Sep-1987 30-Sep-1987 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Ohyama, K. submitted to the EMBL Data Library October1986 A25809 DNA 1-39 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features Fukuzawa, H. Kohchi, T. Sano, T. Shirai, H. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988333-351 Structure and organization of Marchantia polymorpha chloroplast genome. III. Gene organization of the large single copy region from rbcL to trnI(CAU). MUID89068687 S01537 DNA 1-39 EMBLX04465 NIDg11640 PIDNCAA28100.1 PIDg11688 psbF chloroplast heterodimer of alpha (psbE, see PIR:CBLV55) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVFFLGAISAMQFIQR
B48310 B48310 31-Dec-1993 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain garden pea chloroplast garden pea chloroplast Pisum sativum Willey, D.L. Gray, J.C. Curr. Genet. 151989213-220 Two small open reading frames are co-transcribed with the pea chloroplast genes for the polypeptides of cytochrome b-559. MUID89354671 B48310 DNA 1-39 GBX15767 NIDg12152 PIDNCAA33773.1 PIDg12154 chloroplast heterodimer of alpha (psbE, see PIR:A48310) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVSFLGSISAMQFIQR
S01244 S01244 30-Jun-1989 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain evening primrose chloroplast evening primrose chloroplast Oenothera villaricae Schuster, W. Brennicke, A. Nucleic Acids Res. 1619887728 A plastid fragment from the psbE-psbF coding region in the mitochondrial genome of Oenothera berteriana. MUID88319966 S01244 DNA 1-39 EMBLX07951 NIDg11913 PIDNCAA30777.1 PIDg11915 psbF chloroplast heterodimer of alpha (psbE, see PIR:S01243) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVSFLGSISAMQFIQR
S55790 S55790 27-Oct-1995 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain Hooker's evening primrose chloroplast Hooker's evening primrose chloroplast Oenothera hookeri subsp. hookeri Carrillo, N. Seyer, P. Tyagi, A. Herrmann, R.G. Curr. Genet. 101986619-624 Cytochrome b-559 genes from Oenothera hookeri and Nicotiana tabacum show a remarkably high degree of conservation as compared to spinach. MUID88165110 S55790 DNA 1-39 EMBLX03780 NIDg11923 PIDNCAA27411.1 PIDg11925 psbF chloroplast heterodimer of alpha (psbE, see PIR:S55789) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 15-31 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 18 predicted 39 complete MTIDRTYPIFTVRWLAVHGLAVPTVSFLGSISAMQFIQR
S00690 S00690 S34884 S34517 30-Jun-1989 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain Euglena gracilis chloroplast chloroplast Euglena gracilis Cushman, J.C. Christopher, D.A. Little, M.C. Hallick, R.B. Price, C.A. Curr. Genet. 131988173-180 Organization of the psbE, psbF, orf38, and orf42 gene loci on the Euglena gracilis chloroplast genome. MUID88223485 S00690 DNA 1-41 EMBLX07073 NIDg11492 PIDNCAA30109.1 PIDg11494 Hallick, R.B. Hong, L. Drager, R.G. Favreau, M.R. Monfort, A. Orsat, B. Spielmann, A. Stutz, E. Nucleic Acids Res. 2119933537-3544 Complete sequence of Euglena gracilis chloroplast DNA. MUID93347989 S34884 nucleic acid sequence not shown translation not shown DNA 1-41 EMBLX70810 NIDg415327 PIDNCAA50096.1 PIDg415752 Pringsheim strain Z the nucleotide sequence was submitted to the EMBL Data Library, January 1993 psbF chloroplast 5/3 heterodimer of alpha (psbE, see PIR:S00689) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 17-33 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 20 predicted 41 complete MTTNKDTRYPIFTFRWLAVHALAIPTVFFLGSISAMQFIQR
F2YB4 S00339 S75179 30-Sep-1990 30-Sep-1990 16-Jun-2000
cytochrome b559 component psbF cytochrome b559 beta chain protein smr0006 Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Pakrasi, H.B. Williams, J.G.K. Arntzen, C.J. EMBO J. 71988325-332 Targeted mutagenesis of the psbE and psbF genes blocks photosynthetic electron transport: evidence for a functional role of cytochrome b559 in photosystem II. MUID88211541 S00339 DNA 1-44 EMBLX06988 NIDg47430 PIDNCAA30049.1 PIDg47432 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S75179 nucleic acid sequence not shown translation not shown DNA 1-44 EMBLD90903 GBAB001339 NIDg1652127 PIDNBAA17093.1 PIDg1652169 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 psbF heterodimer of alpha (psbE, see PIR:CBYB55) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein product cytochrome b559 component psbF 2-44 experimental domain transmembrane 20-36 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 23 predicted 44 complete MATQNPNQPVTYPIFTVRWLAVHTLAVPSVFFVGAIAAMQFIQR
S51365 S51365 01-Aug-1995 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain Chlamydomonas eugametos chloroplast chloroplast Chlamydomonas eugametos Turmel, M. Otis, C. Curr. Genet. 27199454-61 The chloroplast gene cluster containing psbF, psbL, petG and rps3 is conserved in Chlamydomonas. MUID95269309 S51365 DNA 1-44 EMBLL29282 NIDg575472 PIDNAAA84156.1 PIDg575473 psbF chloroplast heterodimer of alpha (psbE, see PIR:S53882) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 20-36 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 23 predicted 44 complete MTTRKSAEVITYPIFTVRWVSIHALAVPTIFFLGSITAMQFIQR
S53883 S53883 S26878 T08170 27-Oct-1995 07-Jun-1996 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain Chlamydomonas reinhardtii chloroplast chloroplast Chlamydomonas reinhardtii Mor, T.S. Ohad, I. Hirschberg, J. Pakrasi, H.B. Mol. Gen. Genet. 2461995600-604 An unusual organization of the genes encoding cytochrome b(559) in Chlamydomonas reinhardtii: psbE and psbF genes are separately transcribed from different regions of the plastid chromosome. MUID95214620 S53883 DNA 1-44 EMBLX79564 NIDg853811 PIDNCAA56101.1 PIDg853812 Fong, S.E. Surzycki, S.J. Curr. Genet. 211992527-530 Organization and structure of plastome psbF, psbL, petG and ORF712 genes in Chlamydomonas reinhardtii. MUID92315354 S26878 not compared with conceptual translation DNA 1-21,'TTVLQYQQF',31-44 GBX66250 NIDg393459 PIDNCAA46977.1 PIDg393460 psbF chloroplast heterodimer of alpha (psbE, see PIR:S53882) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chloroplast chromoprotein electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 20-36 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 23 predicted 44 complete MTTKKSAEVLVYPIFTVRWLAIHGIAVPTIFFLGAITAMQFIQR
CBKT5F S09482 T06867 31-Dec-1992 31-Dec-1992 03-Mar-2000
cytochrome b559 component psbF cytochrome b559 beta chain Cyanophora paradoxa cyanelle cyanelle Cyanophora paradoxa Cantrell, A. Bryant, D.A. Prog. Photosyn. Res. 41987659-662 Molecular cloning and nucleotide sequences of the genes encoding cytochrome B-559 from the cyanelle genome of Cyanophora paradoxa. S09482 nucleic acid sequence not shown not compared with conceptual translation DNA 1-42 Stirewalt, V.L. Michalowski, C.B. Luffelhardt, W. Bohnert, H.J. Bryant, D.A. submitted to the EMBL Data Library July1995 Nucleotide sequence of the cyanelle genome from Cyanophora paradoxa. T06867 preliminary translated from GB/EMBL/DDBJ DNA 1-42 EMBLU30821 NIDg1016083 PIDNAAA81210.1 PIDg1016123 strain Pringsheim LB555 psbF cyanelle heterodimer of alpha (psbE, see PIR:CBKT5E) and beta (psbF) chains; tightly associated with the reaction center of photosystem II may be part of the water-oxidation complex of photosystem II photosystem II cytochrome b559 component F chromoprotein cyanelle electron transfer heme heterodimer iron membrane-associated complex metalloprotein photosynthesis photosystem II thylakoid transmembrane protein domain transmembrane 18-34 predicted binding-site heme iron (His) (axial ligand) (shared with alpha chain) 21 predicted 42 complete MNNPNQPVSYPIFTVRWLAIHAIGIPAVFFIGSITAMQFIQR
CBHU5 A28936 S04976 A91933 A00167 A24211 A32912 29-Jul-1981 05-Apr-1995 20-Apr-2000
cytochrome b5, microsomal splice form [validated] human man Homo sapiens Yoo, M. Steggles, A.W. Biochem. Biophys. Res. Commun. 1561988576-580 The complete nucleotide sequence of human liver cytochrome b5 mRNA. MUID89025904 A28936 mRNA 1-134 GBM22865 NIDg181226 PIDNAAA35729.1 PIDg181227 liver Ozols, J. Biochim. Biophys. Acta 9971989121-130 Structure of cytochrome b(5) and its topology in the microsomal membrane. MUID89323209 S04976 protein 2-3,'E',5-36;84-121,'V',123-134 liver Rashid, M.A. Hagihara, B. Kobayashi, M. Tani, S. Tsugita, A. J. Biochem. 741973985-1002 Structural studies of cytochrome b-5. III. Sequential studies on human liver cytochrome b-5. MUID74074962 A91933 protein 'QZA',5-14,'Q',16-17,'E',19-21,23-61,'D',63-88,'K',90,'R' liver blocked amino-terminal peptide attributed to pyrrolidone carboxylic acid Nobrega, F.G. Ozols, J. J. Biol. Chem. 24619711706-1717 Amino acid sequences of tryptic peptides of cytochromes b-5 from microsomes of human, monkey, porcine, and chicken liver. MUID71134790 A00167 protein 5-14,'Q',16-17,'E',19-61,'D',63-88,'K',90,'R' liver Yoo, M. Steggles, A.W. Biochem. Biophys. Res. Commun. 163198918-24 The characterization of three types of partially processed mRNA and two pseudogenes for human liver cytochrome b-5. MUID89374222 annotation introns Abe, K. Kimura, S. Kizawa, R. Anan, F.K. Sugita, Y. J. Biochem. 9719851659-1668 Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. MUID85289161 annotation amino-terminal acetylation Ozols, J. J. Biol. Chem. 24719722242-2245 Cytochrome b-5 from a normal human liver. Isolation and the partial amino acid sequence. MUID72154531 annotation Cytochrome b5 exists in at least two alternative splice forms. This longer form is found bound in microsome membranes, on the cytoplasmic side of the endoplasmic reticulum. The shorter form (see PIR:CBHU5E) is found in erythrocytes. GDBCYB5 GDB125236 OMIM250790 18q22.3-18q23 86/3 the list of introns may be incomplete acts an electron carrier for membrane bound oxygenases; with cytochrome-b5 reductase enables exchange between NADPH and membrane bound oxidases cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein electron transfer heme iron membrane protein metalloprotein microsome product cytochrome b5, microsomal splice form 2-134 experimental domain cytochrome b5 core homology 9-84 domain transmembrane 119-131 predicted modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 predicted 134 complete MAEQSDEAVKYYTLEEIQKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDAREMSKTFIIGELHPDDRPKLNKPPETLITTIDSSSSWWTNWVIPAISA VAVALMYRLYMAED
CBHU5E JN0075 B24211 08-Aug-1987 05-Apr-1995 20-Apr-2000
cytochrome b5, erythrocyte splice form [validated] human man Homo sapiens Giordano, S.J. Steggles, A.W. Biochem. Biophys. Res. Commun. 178199138-44 The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene. MUID91298976 JN0075 mRNA 1-98 GBM60174 NIDg181391 PIDNAAA52165.1 PIDg181392 erythrocyte Abe, K. Kimura, S. Kizawa, R. Anan, F.K. Sugita, Y. J. Biochem. 9719851659-1668 Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. MUID85289161 B24211 protein 2-88,'K',90,'R',92-98 erythrocyte Cytochrome b5 exists in at least two alternative splice forms. This shorter form is found in erythrocyte cytoplasm. The longer form (see PIR:CBHU5) is found bound in microsome membranes. GDBCYB5 GDB125236 OMIM250790 18q23-18q23 86/3 the list of introns may be incomplete acts to reduce methemoglobin to functional hemoglobin; the oxidized form is reduced by cytochrome b5 reductase with NADPH a deficiency of this protein causes type IV hereditary methemoglobinemia cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein electron transfer erythrocyte heme iron metalloprotein product cytochrome b5, erythrocyte splice form 2-98 experimental domain cytochrome b5 core homology 9-84 modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 predicted 98 complete MAEQSDEAVKYYTLEEIQKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDAREMSKTFIIGELHPDDRPKLNKPPEP
CBRB5 S03373 S07961 A91920 A93774 A92068 A91953 A92269 A61482 A00168 A31221 29-Jul-1981 31-Dec-1993 20-Apr-2000
cytochrome b5, microsomal splice form [validated] rabbit domestic rabbit Oryctolagus cuniculus Dariush, N. Fisher, C.W. Steggles, A.W. Protein Seq. Data Anal. 11988351-353 The nucleotide sequence of rabbit liver cytochrome b(5) mRNA. MUID89128816 S03373 mRNA 1-134 GBM24844 NIDg1431635 PIDNAAB03878.1 PIDg164785 the authors translated the codon GAC for residues 6 and 8 as Asn, AAC for residue 21 as Asp, GAT for residues 58 and 104 as Asn, and ATG for residue 126 as Phe Ozols, J. Biochim. Biophys. Acta 9971989121-130 Structure of cytochrome b(5) and its topology in the microsomal membrane. MUID89323209 S07961 protein 2-4 Tsugita, A. Kobayashi, M. Kajihara, T. Hagihara, B. J. Biochem. 641968727-730 Primary structure of rabbit liver cytochrome b5. MUID69108767 A91920 protein 9-46;40-61,'D',63-91 Tsugita, A. Kobayashi, M. Tani, S. Kyo, S. Rashid, M.A. Yoshida, Y. Kajihara, T. Hagihara, B. Proc. Natl. Acad. Sci. U.S.A. 671970442-447 Comparative study of the primary structures of cytochrome b-5 from four species. MUID70289989 A93774 protein 7-8;47-49 Ozols, J. J. Biol. Chem. 24519704863-4874 Amino acid sequence of rabbit liver microsomal cytochrome b-5. MUID71001482 A92068 protein 5-15,'Q',17-98 the two minor components have either 11-Phe and 14-Glu or 96-Thr and an additional carboxyl-terminal Glx Kondo, K. Tajima, S. Sato, R. Narita, K. J. Biochem. 8619791119-1128 Primary structure of the membrane-binding segment of rabbit cytochrome b-5. MUID80049603 A91953 protein 92-103,'N',105-134 this segment corresponds to the membrane-binding carboxyl end of the molecule Takagaki, Y. Gerber, G.E. Nihei, K. Khorana, H.G. J. Biol. Chem. 25519801536-1541 Amino acid sequence of the membranous segment of rabbit liver cytochrome b-5. Methodology for separation of hydrophobic peptides. MUID80115672 A92269 protein 99-134 Gibson, B.W. Falick, A.M. Lipka, J.J. Waskell, L.A. J. Protein Chem. 91990695-703 Mass spectrometric analysis of rabbit and bovine trypsin-solubilized cytochrome b-5. MUID91158806 A61482 protein 2-3,'E',5-16 cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein heme iron metalloprotein product cytochrome b5 2-134 experimental domain cytochrome b5 core homology 9-84 modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 predicted 134 complete MAAQSDKDVKYYTLEEIKKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTFIIGELHPDDRSKLSKPMETLITTVDSNSSWWTNWVIPAISA LIVALMYRLYMADD
JN0316 JN0316 S29841 20-Apr-2000 20-Apr-2000 16-Jun-2000
cytochrome b5, erythrocyte splice form [validated] soluble cytochrome b5 rabbit domestic rabbit Oryctolagus cuniculus Takematsu, H. Kozutsumi, Y. Suzuki, A. Kawasaki, T. Biochem. Biophys. Res. Commun. 1851992845-851 Molecular cloning of rabbit cytochrome B5 genes; evidence for the occurrence of two separate genes encoding the soluble and microsomal forms. MUID92328788 JN0316 mRNA 1-98 GBD10901 NIDg471149 PIDNBAA01712.1 PIDg471150 Thr-96 was also found Giordano, S.J. Steggles, A.W. Biochim. Biophys. Acta 1172199395-100 Differential expression of the mRNAs for the soluble and membrane-bound forms of rabbit cytochrome b(5). MUID93176833 S29841 preliminary mRNA 1-98 EMBLZ14091 NIDg1542 this translation is not annotated in GenBank entry OCCYTB5, release 113.0 cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein electron transfer heme iron liver metalloprotein domain cytochrome b5 core homology 9-84 modified-site acetylated amino end (Ala) (in mature form) 2 predicted binding-site heme iron (His) (axial ligands) 44,68 predicted 98 complete MAAQSDKDVKYYTLEEIKKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTFIIGELHPDDRSKLSKPMEP
CBHO5 S07964 A92196 A92218 A00169 29-Jul-1981 20-Apr-2000 05-May-2000
cytochrome b5, microsomal form [validated] hepatic cytochrome b5 membrane-bound cytochrome b5 horse domestic horse Equus caballus Ozols, J. Biochim. Biophys. Acta 9971989121-130 Structure of cytochrome b(5) and its topology in the microsomal membrane. MUID89323209 S07964 protein 1-133 Ozols, J. Gerard, C. Nobrega, F.G. J. Biol. Chem. 25119766767-6774 Proteolytic cleavage of horse liver cytochrome b5. MUID77028943 A92196 protein 'Z',2,'DAS',6-41,'D',43-98 the amino terminal is shown to be blocked by acetylation and not pyroglutamic acid in reference S07964, MUID:89323209 Ozols, J. Gerard, C. J. Biol. Chem. 25219778549-8553 Covalent structure of the membranous segment of horse cytochrome b-5. Chemical cleavage of the native hemoprotein. MUID78045981 A92218 protein 89-133 cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein electron transfer heme iron liver metalloprotein domain cytochrome b5 core homology 8-83 domain transmembrane 108-129 predicted modified-site acetylated amino end (Ala) 1 experimental binding-site heme iron (His) (axial ligands) 43,67 predicted 133 complete AEQSDKAVKYYTLEEIKKHNHSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDATE NFEDIGHSTDARELSKTFIIGELHPDDRSKIAKPVETLITTVDSNSSWWTNWVIPAISAV VVALMYRIYTAED
CBBO5 A47215 S03428 F24211 S07963 A90383 A92053 B93774 A92231 A00170 12-Aug-1981 05-May-1995 15-Sep-2000
cytochrome b5, microsomal form [validated] cytochrome b5, erythrocyte form bovine cattle Bos primigenius taurus Cristiano, R.J. Giordano, S.J. Steggles, A.W. Genomics 171993348-354 The isolation and characterization of the bovine cytochrome b5 gene, and a transcribed pseudogene. MUID94010928 A47215 DNA 1-134 GBM63226 GBM63227 GBM63228 GBM63329 GBL22966 NIDg387580 sequence extracted from NCBI backbone and corrected to correspond with the published sequence the authors conclude that the erythrocyte form is generated by posttranslational processing of the microsomal form and not from the possible alternative splicing Cristiano, R.J. Steggles, A.W. Nucleic Acids Res. 171989799 The complete nucleotide sequence of bovine liver cytochrome b(5) mRNA. MUID89128451 S03428 mRNA 1-134 EMBLX13617 NIDg297 PIDNCAA31949.1 PIDg298 Abe, K. Kimura, S. Kizawa, R. Anan, F.K. Sugita, Y. J. Biochem. 9719851659-1668 Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. MUID85289161 F24211 protein 2,'Z',4-98 erythrocyte residues 2-3 were positioned by homology with the bovine liver sequence Ozols, J. Biochim. Biophys. Acta 9971989121-130 Structure of cytochrome b(5) and its topology in the microsomal membrane. MUID89323209 S07963 protein 2-6;15-18 Ozols, J. Biochemistry 131974426-434 Cytochrome beta-5 from microsomal membranes of equine, bovine, and porcine livers. Isolation and properties of preparations containing the membranous segment. MUID74080219 A90383 protein 'ZB',2,'ZZ',5-11;131-133,'D' Ozols, J. Strittmatter, P. J. Biol. Chem. 24419696617-6618 Correction of the amino acid sequence of calf liver microsomal cytochrome b5. MUID70067001 A92053 protein 6-15,'QEI',19-61,'D',63-97 liver Tsugita, A. Kobayashi, M. Tani, S. Kyo, S. Rashid, M.A. Yoshida, Y. Kajihara, T. Hagihara, B. Proc. Natl. Acad. Sci. U.S.A. 671970442-447 Comparative study of the primary structures of cytochrome b-5 from four species. MUID70289989 B93774 protein 6-17,'E',19-61,'D',63-96 Fleming, P.J. Dailey, H.A. Corcoran, D. Strittmatter, P. J. Biol. Chem. 25319785369-5372 The primary structure of the nonpolar segment of bovine cytochrome b5. MUID78218214 A92231 protein 92-134 Muskett, F.W. Kelly, G.P. Whitford, D. submitted to the Brookhaven Protein Data Bank February1996 PDB1WDB annotation conformation by (1)H-, (15)N-NMR, residues 6-89 Muskett, F.W. Kelly, G.P. Whitford, D. J. Mol. Biol. 2581996172-189 The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods. MUID96200988 annotation conformation by (1)H-, (15)N-NMR Durley, R.C.E. Mathews, F.S. submitted to the Brookhaven Protein Data Bank August1994 PDB1CYO annotation X-ray crystallography, 1.5 angstroms, residues 6-93 Mathews, F.S. Durley, R.C.E. submitted to the Brookhaven Protein Data Bank January1990 PDB3B5C annotation X-ray crystallography, 1.5 angstroms, 8-92 Mathews, F.S. Argos, P. Levine, M. Cold Spring Harb. Symp. Quant. Biol. 371971387-395 The structure of cytochrome b-5 at 2.0 angstrom resolution. annotation oxidized form, X-ray crystallography, 2.0 angstroms revision to residues 18 and 19 Argos, P. Mathews, F.S. J. Biol. Chem. 2501975747-751 The structure of ferrocytochrome b5 at 2.8 A resolution. MUID75095526 annotation reduced form, X-ray crystallography, 2.8 angstroms the structure of the reduced form was found to be the same as that of the oxidized form, except for a slight displacement of one lysine side chain caused by the binding of a cation at the entrance of the heme crevice This protein contains two domains: a hydrophilic, catalytic, amino-terminal segment consisting of about 85 residues and a hydrophobic carboxyl-terminal segment that is required for binding the cytochrome to biological membranes. CYB5 43/3; 86/3; 96/3; 108/2 acts as an electron carrier for membrane bound oxygenases; with cytochrome-b5 reductase enables exchange between NADPH and membrane bound oxidases microsomal form acts to reduce methemoglobin to functional hemoglobin; the oxidized form is reduced by cytochrome b5 reductase with NADPH erythrocyte form cytochrome b5 cytochrome b5 core homology acetylated amino end chromoprotein electron transfer heme iron membrane protein metalloprotein microsome product cytochrome b5, microsomal form 2-134 experimental product cytochrome b5, erythrocyte form 2-98 experimental domain cytochrome b5 core homology 9-84 domain membrane-bound 105-127 predicted modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 experimental 134 complete MAEESSKAVKYYTLEEIQKHNNSKSTWLILHYKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTFIIGELHPDDRSKITKPSESIITTIDSNPSWWTNWLIPAISA LFVALIYHLYTSEN
CBPG5 JC5782 C24211 S07962 B90383 B92077 A93813 A00171 29-Jul-1981 20-Apr-2000 05-May-2000
cytochrome b5, microsomal splice form [validated] hepatic cytochrome b5 membrane-bound cytochrome b5 pig domestic pig Sus scrofa domestica VanDerMark, P.K. Steggles, A.W. Biochem. Biophys. Res. Commun. 240199780-83 The isolation and characterization of the soluble and membrane-bound porcine cytochrome b5 cDNAs. MUID98042520 JC5782 mRNA 1-134 GBAF016388 NIDg2642485 PIDNAAC48779.1 PIDg2642486 testis Abe, K. Kimura, S. Kizawa, R. Anan, F.K. Sugita, Y. J. Biochem. 9719851659-1668 Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. MUID85289161 sequence revisions C24211 protein 2-134 Ozols, J. Biochim. Biophys. Acta 9971989121-130 Structure of cytochrome b(5) and its topology in the microsomal membrane. MUID89323209 S07962 protein 2-134 Ozols, J. Biochemistry 131974426-434 Cytochrome beta-5 from microsomal membranes of equine, bovine, and porcine livers. Isolation and properties of preparations containing the membranous segment. MUID74080219 B90383 protein 'ZZDAS',7 Nobrega, F.G. Ozols, J. J. Biol. Chem. 24619711706-1717 Amino acid sequences of tryptic peptides of cytochromes b-5 from microsomes of human, monkey, porcine, and chicken liver. MUID71134790 B92077 protein 8-14,'ZZ',17,'Z',19-89 Ozols, J. Gerard, C. Proc. Natl. Acad. Sci. U.S.A. 7419773725-3729 Primary structure of the membranous segment of cytochrome b-5. MUID78012290 A93813 protein 15-16;'D';90-134 the residue 62 was identified as Asp cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein electron transfer heme iron liver metalloprotein domain cytochrome b5 core homology 9-84 domain transmembrane 109-130 predicted modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 predicted 134 complete MAEQSDKAVKYYTLEEIQKHNNSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTFIIGELHPDDRSKIAKPSETLITTVESNSSWWTNWVIPAISA LVVSLMYHFYTSEN
JC5783 JC5783 D24211 20-Apr-2000 20-Apr-2000 19-May-2000
cytochrome b5, erythrocyte splice form [validated] soluble cytochrome b5 pig domestic pig Sus scrofa domestica VanDerMark, P.K. Steggles, A.W. Biochem. Biophys. Res. Commun. 240199780-83 The isolation and characterization of the soluble and membrane-bound porcine cytochrome b5 cDNAs. MUID98042520 JC5783 mRNA 1-98 GBAF016389 NIDg2642487 PIDNAAC48780.1 PIDg2642488 testis this splice form is not completely annotated in GenBank entry AF016389, release 113.0 Abe, K. Kimura, S. Kizawa, R. Anan, F.K. Sugita, Y. J. Biochem. 9719851659-1668 Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. MUID85289161 D24211 protein 2-98 cytochrome b5 cytochrome b5 core homology acetylated amino end chromoprotein electron transfer heme iron liver metalloprotein domain cytochrome b5 core homology 9-84 modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 predicted 98 complete MAEQSDKAVKYYTLEEIQKHNNSKSTWLILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTFIIGELHPDDRSKIAKPSES
CBRT5 S28404 A00172 A23338 JC5597 JS0745 S07960 15-Oct-1982 31-Dec-1992 16-Jun-2000
cytochrome b5, microsomal splice form [validated] rat Norway rat Rattus norvegicus Mitoma, J. Ito, A. EMBO J. 1119924197-4203 The carboxy-terminal 10 amino acid residues of cytochrome b(5) are necessary for its targeting to the endoplasmic reticulum. MUID93011015 S28404 mRNA 1-134 EMBLD13205 NIDg220729 PIDNBAA02492.1 PIDg220730 Ozols, J. Heinemann, F.S. Biochim. Biophys. Acta 7041982163-173 Chemical structure of rat liver cytochrome b-5. Isolation of peptides by high-pressure liquid chromatography. MUID82232110 A00172 protein 2-134 Lederer, F. Ghrir, R. Guiard, B. Cortial, S. Ito, A. Eur. J. Biochem. 132198395-102 Two homologous cytochromes b-5 in a single cell. MUID83182449 A23338 protein 7,'B',9-17,'E',19-89 Yoo, M. Biochem. Biophys. Res. Commun. 2361997641-642 Identification of two homologous cytochrome b5s in rat brain. MUID97396150 JC5597 mRNA 1-134 DDBJAF007108 NIDg2257956 PIDNAAB67610.1 PIDg2257957 brain This protein is a small heme-containing protein which supplies electrons for many cytochrome P450 catalyzed reactions in the liver and for the reduction of methemoglobin in erythrocyte cell. cytochrome b5 cytochrome b5 core homology acetylated amino end alternative splicing chromoprotein electron transfer heme iron membrane protein metalloprotein product cytochrome b5 2-134 experimental domain cytochrome b5 core homology 9-84 modified-site acetylated amino end (Ala) (in mature form) 2 experimental binding-site heme iron (His) (axial ligands) 44,68 predicted 134 complete MAEQSDKDVKYYTLEEIQKHKDSKSTWVILHHKVYDLTKFLEEHPGGEEVLREQAGGDAT ENFEDVGHSTDARELSKTYIIGELHPDDRSKIAKPSETLITTVESNSSWWTNWVIPAISA LVVALMYRLYMAED
CBRT5M A00173 S66501 04-Dec-1986 29-Aug-1997 16-Jun-2000
cytochrome b5, outer mitochondrial membrane rat Norway rat Rattus norvegicus Lederer, F. Ghrir, R. Guiard, B. Cortial, S. Ito, A. Eur. J. Biochem. 132198395-102 Two homologous cytochromes b-5 in a single cell. MUID83182449 A00173 protein 1-92 de Silvestris, M. D'Arrigo, A. Borgese, N. FEBS Lett. 370199569-74 The targeting information of the mitochondrial outer membrane isoform of cytochrome b(5) is contained within the carboxyl-terminal region. MUID95377460 S66501 mRNA 32-135 GBX96392 EMBLS79339 NIDg1217654 PIDNCAA65256.1 PIDg1217655 Cytochrome b5, found attached to various hepatic cell membranes, is a major component of the electron transport system, catalyzing the NADH-linked desaturation of fatty acids in the endoplasmic reticulum. It may also be involved in the NADH-linked pathway of drug hydroxylation reactions catalyzed by cytochrome p450. nuclear cytochrome b5 cytochrome b5 core homology chromoprotein electron transfer heme iron membrane protein metalloprotein mitochondrion domain heme binding 1-92 predicted domain cytochrome b5 core homology 9-84 binding-site heme iron (His) (axial ligands) 44,68 predicted 135 complete DGQGSDPAVTYYRLEEVAKRNTAEETWMVIHGRVYDITRFLSEHPGGEEVLLEQAGADAT ESFEDVGHSPDAREMLKQYYIGDVHPNDLKPKDGDKDPSKNNSCQSSWAYWIVPIVGAIL IGFLYRHFWADSKSS
CBCH5 A28811 S10746 S04977 A00174 24-Apr-1984 10-Nov-1995 03-Mar-2000
cytochrome b5 precursor chicken chicken Gallus gallus Zhang, H. Somerville, C. Arch. Biochem. Biophys. 2641988343-347 The primary structure of chicken liver cytochrome b-5 deduced from the DNA sequence of a cDNA clone. MUID88280278 A28811 mRNA 1-138 GBM18539 NIDg211692 PIDNAAA48733.1 PIDg211693 Zhang, H. Somerville, C. Arch. Biochem. Biophys. 2801990412-415 Soluble and membrane-bound forms of cytochrome b5 are the products of a single gene in chicken. MUID90314412 S10746 mRNA 1-138 EMBLM32293 NIDg211706 PIDNAAA48740.1 PIDg211707 Ozols, J. Biochim. Biophys. Acta 9971989121-130 Structure of cytochrome b(5) and its topology in the microsomal membrane. MUID89323209 S04977 protein 4-11,'E',13-113,'W',115-123,'T',125-138,'E' Nobrega, F.G. Ozols, J. J. Biol. Chem. 24619711706-1717 Amino acid sequences of tryptic peptides of cytochromes b-5 from microsomes of human, monkey, porcine, and chicken liver. MUID71134790 A00174 protein 14-26,'Z',28,'B',30-66,'D',68-97 cytochrome b5 cytochrome b5 core homology acetylated amino end chromoprotein electron transfer heme iron membrane protein metalloprotein product cytochrome b5 7-138 experimental domain cytochrome b5 core homology 14-89 modified-site acetylated amino end (Ala) (in mature form) 7 predicted binding-site heme iron (His) (axial ligands) 49,73 predicted 138 complete MVGSSEAGGEAWRGRYYRLEEVQKHNNSQSTWIIVHHRIYDITKFLDEHPGGEEVLREQA GGDATENFEDVGHSTDARALSETFIIGELHPDDRPKLQKPAETLITTVQSNSSSWSNWVI PAIAAIIVALMYRSYMSE
S44303 A58972 S54768 S44303 S47414 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) component K phenolhydroxylase chain A Pseudomonas putida Pseudomonas putida Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 A58972 preliminary DNA 1-92 EMBLX79063 NIDg483477 PIDNCAA55660.1 PIDg483478 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54768 preliminary nucleic acid sequence not shown translation not shown DNA 1-87,'L',89-92 EMBLX80765 NIDg527546 PIDNCAA56740.1 PIDg527547 the nucleotide sequence was submitted to the EMBL Data Library, July 1994 phlA phhK phenol 2-monooxygenase component K oxidoreductase 92 complete MAVTNTPTPTFDQFTRYIRVRSEPEAKFVEFDFALGHPELFVELVLPQDAFVKFCQHNRV VAMDEAMAKAVDDDMVKWRFGDVGRRLPKDPG
A37831 A37831 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain P0 Pseudomonas sp. (strain CF600) Pseudomonas sp. Nordlund, I. Powlowski, J. Shingler, V. J. Bacteriol. 17219906826-6833 Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. MUID91072230 A37831 preliminary DNA 1-92 GBM60276 GBM37764 NIDg151449 PIDNAAA25939.1 PIDg151450 phenol 2-monooxygenase component K oxidoreductase 92 complete MTVTNTPTPTFDQLTRYIRVRSEPEAKFVEFDFAIGHPELFVELVLPQDAFVKFCQHNRV VAMDEAMAKAVDDDMVKWRFGDVGRRLPKDPG
S47287 S70080 S47287 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain mopK phenol hydroxylase Acinetobacter calcoaceticus Acinetobacter calcoaceticus Ehrt, S. Schirmer, F. Hillen, W. Mol. Microbiol. 18199513-20 Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. MUID96154937 S70080 nucleic acid sequence not shown translation not shown DNA 1-96 EMBLZ36909 NIDg535279 PIDNCAA85380.1 PIDg535280 strain NCIB8250 the nucleotide sequence was submitted to the EMBL Data Library, September 1994 mopK phenol 2-monooxygenase component K aromatic hydrocarbon catabolism oxidoreductase 96 complete MIDAKQPTALVKYIRITGERNAKFVEFDFAIQDPTLFVELILPQQAFQHFCEINHVIEMT AEQQAWNDAQEDKWRYGIEPTVLNHARQHSDQDDQT
S44304 C58972 S54767 S44304 S47415 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) component L phenolhydroxylase chain B Pseudomonas putida Pseudomonas putida Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 C58972 preliminary DNA 1-331 EMBLX79063 NIDg483477 PIDNCAA55661.1 PIDg483479 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54767 preliminary nucleic acid sequence not shown translation not shown DNA 'MGIQQQEGTVD',1-8,'T',10-57,'R',59-86,'G',88-331 EMBLX80765 NIDg527546 PIDNCAA56741.1 PIDg527548 strain H the nucleotide sequence was submitted to the EMBL Data Library, July 1994 phlB phhL phenol 2-monooxygenase component L oxidoreductase 331 complete MSVEIKTNAVDPIRQTYGNLQRRFGDKPASRYQEASYDIEAVTNFHYRPLWDPQHELHDP TRTAIRMTDWHKVTDPRQFYYGAYVQTRARMQEATEHAYGFCEKRELLSRLPAELQAKLL RCLVPLRHAELGANMNNSSIAGDSIAATVTQMHIYQAMDRLGMGQYLSRIGLLLDGGTGE ALDQAKAYWLDDPIWQGLRRYVEDSFVIRDWFELGLAQNLVLDGLLQPLMYQRFDQWLTE NGGSDVAMLTEFMRDWYGESTRWVDAMFKTVLAENDANREQVQAWLEVWEPRAYEALLPL AEEATGIAALDEVRSAFATRLQKIGLKSREE
B37831 B37831 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain P1 Pseudomonas sp. (strain CF600) Pseudomonas sp. Nordlund, I. Powlowski, J. Shingler, V. J. Bacteriol. 17219906826-6833 Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. MUID91072230 B37831 preliminary DNA 1-331 GBM60276 GBM37764 NIDg151449 PIDNAAA25940.1 PIDg151451 phenol 2-monooxygenase component L oxidoreductase 331 complete MSVEIKTNTVDPIRQTYGNLQRRFGDKPASRYQEASYDIEAVTNFHYRPLWDPQHELHDP TRTAIRMTDWHKVTDPRQFYYGAYVQTRARMQEATEHAYGFCEKRELLSRLPAELQAKLL RCLVPLRHAELGANMNNSSIAGDSIAATVTQMHIYQAMDRLGMGQYLSRIGLLLDGGTGE ALDQAKAYWLDDPIWQGLRRYVEDSFVIRDWFELGLAQNLVLDGLLQPLMYQRFDQWLTE NGGSDVAMLTEFMRDWYGESTRWVDAMFKTVLAENDANREQVQAWLEVWEPRAYEALLPL AEEATGIAALDEVRSAFATRLQKIGLKSREE
S47288 S70081 S47288 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain mopL phenol hydroxylase Acinetobacter calcoaceticus Acinetobacter calcoaceticus Ehrt, S. Schirmer, F. Hillen, W. Mol. Microbiol. 18199513-20 Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. MUID96154937 S70081 nucleic acid sequence not shown translation not shown DNA 1-333 EMBLZ36909 NIDg535279 PIDNCAA85381.1 PIDg535281 strain NCIB8250 the nucleotide sequence was submitted to the EMBL Data Library, September 1994 mopL phenol 2-monooxygenase component L aromatic hydrocarbon catabolism oxidoreductase 333 complete MTLEIKTSNLQPIRQTYAYIERRFGAKPATRYQEVSFDIQASTNFHYRPLWKPDKTLNDK THTALQMQDWYAFKDPRQFYYGAYVQHRARLQDTAESHYAFFEKRQLVNNLSDEVKQKII QCLLPFRYVEQTANLHMMSGSAYGYGTVITQACIFAAMDRLGMAQYISRIGLILDGNTGE SLQQAKHAWLNDETWQPLRKLCEQSLTEQDWFKLYILQNLLIDSMLQELVFGQLDEWLVE NGGRDIAILTEFMKDCLTDLAKWSDSVLKTAISESEDNKTLIQSWITELLPQVKQAFSAW AQTALTDSGIDSGLNKISERSKKTGNILLDLAA
S44305 D58972 S54766 S44305 S47416 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) component M phenolhydroxylase chain C Pseudomonas putida Pseudomonas putida Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 D58972 preliminary DNA 1-90 EMBLX79063 NIDg483477 PIDNCAA55662.1 PIDg483480 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54766 preliminary nucleic acid sequence not shown translation not shown DNA 1-41,'V',43-55,'K',57-76,'V',78-90,'N' EMBLX80765 NIDg527546 PIDNCAA56742.1 PIDg527549 strain H the nucleotide sequence was submitted to the EMBL Data Library, July 1994 phlC phhM phenol 2-monooxygenase component M oxidoreductase 90 complete MSSLVYIAFQDNDNARYLVEAIIQDNPHAVVQHHPAMIRIEAEKRLEIRRETVEENLGRA WDVQEMLVDVITIGGNIDEDDDRFVLEWKN
C37831 C37831 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain P2 Pseudomonas sp. (strain CF600) Pseudomonas sp. Nordlund, I. Powlowski, J. Shingler, V. J. Bacteriol. 17219906826-6833 Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. MUID91072230 C37831 preliminary DNA 1-90 GBM60276 GBM37764 NIDg151449 PIDNAAA25941.1 PIDg151452 phenol 2-monooxygenase component M oxidoreductase 90 complete MSSLVYIAFQDNDNARYVVEAIIQDNPHAVVQHHPAMIRIEAEKRLEIRRETVEENLGRA WDVQEMLVDVITIGGNVDEDDDRFVLEWKN
S47289 S70082 S47289 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain mopM phenol hydroxylase Acinetobacter calcoaceticus Acinetobacter calcoaceticus Ehrt, S. Schirmer, F. Hillen, W. Mol. Microbiol. 18199513-20 Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. MUID96154937 S70082 nucleic acid sequence not shown translation not shown DNA 1-89 EMBLZ36909 NIDg535279 PIDNCAA85382.1 PIDg535282 strain NCIB8250 the nucleotide sequence was submitted to the EMBL Data Library, September 1994 mopM phenol 2-monooxygenase component M aromatic hydrocarbon catabolism oxidoreductase 89 complete MTSKVYLALQDNDTSRYIIEAIEQDNPEATIQYLPAMIRVESTGELVVRAETVSEKLGQN WDIQELQLNMITLGGNVDEDDDSFTLKWN
S44306 E58972 S54765 S44306 S47417 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) component N phenolhydroxylase chain D Pseudomonas putida Pseudomonas putida Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 E58972 preliminary DNA 1-516 EMBLX79063 NIDg483477 PIDNCAA55663.1 PIDg483481 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54765 preliminary nucleic acid sequence not shown translation not shown DNA 1-63,'H',65-100,'F',102-106,'M',108-137,'EL',140-512,'Q',514-516 EMBLX80765 NIDg527546 PIDNCAA56743.1 PIDg527550 strain H the nucleotide sequence was submitted to the EMBL Data Library, July 1994 phlD phhN phenol 2-monooxygenase component N oxidoreductase 516 complete MTTNKKRLNLKDKYRYLTRDLGWEPSYQKKEDVFPLEHFEGIKITDWDKWEDPFRLTMDS YWKYQAEKEKKLYAIFDAFAQNNGHQNISDARYVNALKLFLTGVSPLEYQAFQGFSRVGR QFSGAGARVACQMQAIDDVRHVQTQVHAMSHYNKHFDGLHDFAHMYDRVWFLSVPKSFMD DARTAGPFEFLTAVSFSFEYVLTNLLFVPFMSGAAYNGDMATVTFGFSAQSDEARHMTLG LEVIKFMLEQHEDNVPIIQRWIDKWFWRGYRLLTLIGMMMDYMLPNKVMSWSEAWGVYFE QAGGALFKDLERYGIRPPKYVEQTTIGKEHITHQVWGAFYQYSKATNFHTWIPGDEELNW LSEKYPDTFDKYYRPRFEFWREQQAKGERFYNDTLPHLCQVCQVPAIFTEPDDPTKLSLR SLVHEGERYHFCSDGCCDIFKNEPVKYIQAWLPVHQIYQGNCEGGDVETVVQKYYHIKSG VDNLEYLGSPEHQRWLALKGQTPPTAAPADKSLDAA
D37831 D37831 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain P3 Pseudomonas sp. (strain CF600) Pseudomonas sp. Nordlund, I. Powlowski, J. Shingler, V. J. Bacteriol. 17219906826-6833 Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. MUID91072230 D37831 preliminary DNA 1-517 GBM60276 GBM37764 NIDg151449 PIDNAAA25942.1 PIDg151453 phenol 2-monooxygenase component N oxidoreductase 517 complete MATHNKKRLNLKDKYRYLTRDLAWETTYQKKEDVFPLEHFEGIKITDWDKWEDPFRLTMD TYWKYQAEKEKKLYAIFDAFAQNNGHQNISDARYVNALKLFLTAVSPLEYQAFQGFSRVG RQFSGAGARVACQMQAIDELRHVQTQVHAMSHYNKHFDGLHDFAHMYDRVWYLSVPKSYM DDARTAGPFEFLTAVSFSFEYVLTNLLFVPFMSGAAYNGDMATVTFGFSAQSDEARHMTL GLEVIKFMLEQHEDNVPIIQRWIDKWFWRGYRLLTLIGMMMDYMLPNKVMSWSEAWGVYF EQAGGALFKDLERYGIRPPKYVEQTTIGKEHITHQVWGALYQYSKATSFHTWIPGDEELN WLSEKYPDTFDKYYRPRFEFWREQQAKGERFYNDTLPHLCQVCQLPVIFTEPDDPTKLSL RSLVHEGERYQFCSDGCCDIFKNEPVKYIQAWLPVHQIYQGNCEGGDVETVVQKYYHIKS GVDNLEYLGSPEHQRWLALKGQTPPTAAPADKSLGAA
S47290 S70083 S47290 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain mopN phenol hydroxylase Acinetobacter calcoaceticus Acinetobacter calcoaceticus Ehrt, S. Schirmer, F. Hillen, W. Mol. Microbiol. 18199513-20 Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. MUID96154937 S70083 nucleic acid sequence not shown translation not shown DNA 1-511 EMBLZ36909 NIDg535279 PIDNCAA85383.1 PIDg535283 strain NCIB8250 the nucleotide sequence was submitted to the EMBL Data Library, September 1994 mopN phenol 2-monooxygenase component N aromatic hydrocarbon catabolism oxidoreductase 511 complete MIKMNSQAKVNNKKLNAKERYRILTRDLDWDFSYADRKDAFPYEEFEGIKITDWSKWEDP FRLTMDNYWKYQAEKEKKLYAIFDAFAQNNGQMNVSNERYVNAIKLFLTAVTPLEYQAYQ GYAHVGRQFSGIGARIASQMQSIDELRHVQTQIHAMSHYNKFFDGFQDWAHMHDRVWYLS VPKSFFEDARSAGPFEFLLAISFAFEYVLTNLLFVPFMSGAAYNGDMATVTFGFSAQSDE ARHMTLGLEIVKFLLEQHEDNVPIVQEWIDKWFWRGTRLLSIVGMMMDYMLPNKVMSWKE AWETFFEEAGGALFKDLSRYGIRMPKYSEVISKEKEHVSHQAWWIFYNFGHAAGFHTWIP TDEEMDWLSEKYPDTFDKYYRPRWELARKMEAEGKRFYSAGLPQLCQVCQIPMTFTEMDG DPTLFSYRDSIYKDERYHTCSDGCHDIFEREPEKYIQAWLPVHQILQGNCGGPDLESILR DYYNFNVGADNLDIEGSPDQQRWKKWKGNAA
S44307 F58972 S54764 S44307 S47418 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) component O phenolhydroxylase chain E Pseudomonas putida Pseudomonas putida Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 F58972 preliminary DNA 1-119 EMBLX79063 NIDg483477 PIDNCAA55664.1 PIDg483482 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54764 preliminary nucleic acid sequence not shown translation not shown DNA 1-9,'T',11-40,'G',42-119 EMBLX80765 NIDg527546 PIDNCAA56744.1 PIDg527551 strain H the nucleotide sequence was submitted to the EMBL Data Library, July 1994 phlE phhO phenol 2-monooxygenase component O oxidoreductase 119 complete MTVNSIGEYPATPRDVQANFNGMQLLYLYWEEHLMYCSALAFLVAPGMPFAEFLEQVLKP AIHAHPDSARIDFSQALWQLNDQPFTPDYAASLEANGIDHKSMLRLNTPGLNGIQGSCS
E37831 E37831 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain P4 Pseudomonas sp. (strain CF600) Pseudomonas sp. Nordlund, I. Powlowski, J. Shingler, V. J. Bacteriol. 17219906826-6833 Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600. MUID91072230 E37831 preliminary DNA 1-119 GBM60276 GBM37764 NIDg151449 PIDNAAA25943.1 PIDg151454 phenol 2-monooxygenase component O oxidoreductase 119 complete MTVNSIGEYTATPRDVQANFNGMQLLYLYWEEHLMYCSALAFLVAPGMPFAEFLEQVLKP AIHAHPDSAKIDFSQALWQLNDQPFTPDYAASLEANGIDHKSMLRLNTPGLNGIQGSCS
S47291 S70084 S47291 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) chain mopO phenol hydroxylase Acinetobacter calcoaceticus Acinetobacter calcoaceticus Ehrt, S. Schirmer, F. Hillen, W. Mol. Microbiol. 18199513-20 Genetic organization, nucleotide sequence and regulation of expression of genes encoding phenol hydroxylase and catechol 1,2-dioxygenase in Acinetobacter calcoaceticus NCIB8250. MUID96154937 S70084 nucleic acid sequence not shown translation not shown DNA 1-120 EMBLZ36909 NIDg535279 PIDNCAA85384.1 PIDg535284 strain NCIB8250 the nucleotide sequence was submitted to the EMBL Data Library, September 1994 mopO phenol 2-monooxygenase component O aromatic hydrocarbon catabolism oxidoreductase 120 complete MTVQAIVEKYQFEPLDLQQNYGENMLLFIGWDHHTLFCSAHAFVVSPKQSLQALIDGQIQ AGFEQHPDFKHIDWSKVEFRLNRNLLQADFSKSLEDLGFDHKSLLRFVTPDLAGYQGTHV
S44308 G58972 S54763 S44308 S47419 10-Sep-1999 10-Sep-1999 10-Sep-1999
phenol 2-monooxygenase (EC 1.14.13.7) reductase component phenol hydroxylase P1 component phenolhydroxylase chain F Pseudomonas putida Pseudomonas putida Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 G58972 preliminary DNA 1-353 EMBLX79063 NIDg483477 PIDNCAA55665.1 PIDg483483 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54763 preliminary nucleic acid sequence not shown translation not shown DNA 1-8,'P',10-35,'A',37-79,'M',81-144,'I',146-176,'G',178-201,'G',203-223,'V',225-227,'LAQ',231-353 EMBLX80765 NIDg527546 PIDNCAA56745.1 PIDg527552 strain H the nucleotide sequence was submitted to the EMBL Data Library, July 1994 phlF phhP methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 22-78 domain cytochrome-b5 reductase homology 109-334 binding-site 2Fe-2S cluster (Cys) (covalent) 37,42,45,77 predicted 353 complete MTYNVTIEATGEIIEVEEGQTILQAALRQGVWLPFPCGHGTCATCKVQVVEGEADHGAAS PFALMDMERDEGKVLACCAIPMSDMVIEADIDVDPDFAGHHVEDYRGVVSALVDLSPTIK GVHIKLDRPMTFQAGQYINLTLPGVEGSRAFSLANPPSQADEVELHIRLVEGGAATSFIH RQLKVGDAVELSGPYGQFFVRDSQAGDLIFIAGGSGLSSPQSMIFDLFERGDTRQITLFQ GARNRAELYNRELFEELAARHSNFSYVPALNQAHDDPEWQGFKGFVHDAAKAHFDGRFSG HKAYLCGPPPMIDAAITTLMQGRLFERDIFMERFFTAADGAEDSTRSALFKRI
S65531 S65531 10-Sep-1999 10-Sep-1999 01-Sep-2000
sodium-translocating NADH dehydrogenase (ubiquinone) (EC 1.6.5.-) nqrF chain Vibrio alginolyticus Vibrio alginolyticus Hayashi, M. Hirai, K. Unemoto, T. FEBS Lett. 363199575-77 Sequencing and the alignment of structural genes in the nqr operon encoding the Na(+)-translocating NADH-quinone reductase from Vibrio alginolyticus. MUID95246889 S65531 preliminary DNA 1-407 EMBLD49364 NIDg2558472 PIDNBAA22915.1 PIDg2558478 nqr6 methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 54-111 domain cytochrome-b5 reductase homology 136-405 binding-site 2Fe-2S cluster (Cys) (covalent) 69,75,78,110 predicted 407 complete MDIILGVVMFTLIVLALVLVILFAKSKLVPTGDITISVNDDPSLAIVTQPGGKLLSALAG AGVFVSSACGGGGSCGQCRVKVKSGGGDILPTELDHITKGEAREGERLACQVAMKTDMDI ELPEEIFGVKKWECTVISNDNKATFIKELKLQIPDGESVPFRAGGYIQIEAPAHHVKYAD YDIPEEYREDWEKFNLFRYESKVNEETIRAYSMANYPEEHGIIMLNVRIATPPPNNPDVP PGIMSSYIWSLKEGDKCTISGPFGEFFAKDTDAEMVFVGGGAGMAPMRSHIFDQLKRLHS KRKMSFWYGARSKREMFYVEDFDMLQAENDNFVWHCALSDPLPEDNWDGYTGFIHNVLYE NYLRDHEAPEDCEYYMCGPPMMNAAVIGMLKDLGVEDENILLDDFGG
A36952 A36952 B47070 10-Sep-1999 10-Sep-1999 10-Sep-1999
CDP-6-deoxy-Delta(3,4)-glucoseen reductase (EC 1.3.1.-) Yersinia pseudotuberculosis Yersinia pseudotuberculosis Lo, S.F. Miller, V.P. Lei, Y. Thorson, J.S. Liu, H.W. Schottel, J.L. J. Bacteriol. 1761994460-468 CDP-6-deoxy-delta(3,4)-glucoseen reductase from Yersinia pseudotuberculosis: enzyme purification and characterization of the cloned gene. MUID94117382 A36952 DNA 1-329 GBL25594 NIDg456127 PIDNAAA16760.1 PIDg456128 Kessler, A.C. Haase, A. Reeves, P.R. J. Bacteriol. 17519931412-1422 Molecular analysis of the 3,6-dideoxyhexose pathway genes of Yersinia pseudotuberculosis serogroup IIA. MUID93186709 B47070 preliminary DNA 1-329 GBL01777 NIDg896325 PIDNAAB49398.1 PIDg155495 serogroup IIA, M85 sequence extracted from NCBI backbone (NCBIN:126815, NCBIP:126827) ascD methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 22-76 domain cytochrome-b5 reductase homology 105-325 binding-site 2Fe-2S cluster (Cys) (covalent) 37,42,45,75 predicted 329 complete MSLNVKLHPSGIIFTSDGTSTILDAALDSNIHIEYSCKDGTCGSCKAILISGEVDSAENT FLTEEDVAKGAILTCCSKAKSDIELDVNYYPELSHIQKKTYPCKLDSIEFIGEDIAILSL RLPPTAKIQYLAGQYIDLIINGQRRSYSIANAPGGNGNIELHVRKVVNGVFSNIIFNELK LQQLLRIEGPQGTFFVREDNLPIVFLAGGTGFAPVKSMVEALINKNDQRQVHIYWGMPAG HNFYSDIANEWAIKHPNIHYVPVVSGDDSTWTGATGFVHQAVLEDIPDLSLFNVYACGSL AMITAARNDFINHGLAENKFFSDAFVPSK
D64052 D64052 10-Sep-1999 10-Sep-1999 10-Sep-1999
Na+-translocating NADH-ubiquinone oxidoreductase (EC 1.-.-.-) beta chain Haemophilus influenzae (strain Rd KW20) Haemophilus influenzae Fleischmann, R.D. Adams, M.D. White, O. Clayton, R.A. Kirkness, E.F. Kerlavage, A.R. Bult, C.J. Tomb, J.F. Dougherty, B.A. Merrick, J.M. McKenney, K. Sutton, G. FitzHugh, W. Fields, C. Gocayne, J.D. Scott, J. Shirley, R. Liu, L.I. Glodek, A. Kelley, J.M. Weidman, J.F. Phillips, C.A. Spriggs, T. Hedblom, E. Cotton, M.D. Utterback, T.R. Hanna, M.C. Nguyen, D.T. Saudek, D.M. Brandon, R.C. Fine, L.D. Fritchman, J.L. Fuhrmann, J.L. Geoghagen, N.S.M. Gnehm, C.L. McDonald, L.A. Small, K.V. Fraser, C.M. Smith, H.O. Venter, J.C. Science 2691995496-512 Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. MUID95350630 D64052 nucleic acid sequence not shown translation not shown DNA 1-411 GBU32702 GBL42023 NIDg1573118 PIDNAAC21841.1 PIDg1573127 TIGRHI0171 methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 58-115 domain cytochrome-b5 reductase homology 140-409 binding-site 2Fe-2S cluster (Cys) (covalent) 73,79,82,114 predicted 411 complete MSDSVILALGIAAFTVIVLVLVAIILFAKSKLVDSGDITIDINDDPEKAITLPAGGKLLG ALASKGIFVSSACGGGGSCGQCIVKVKNGGGEILPTELSHINKREAKEGYRLACQVNVKG NMEVELPEEIFGVKKWECTVISNDNKATFIKELKLAIPEGEEVPFRAGGYIQIEAEPHVV NYKDFDIPEEYHEDWDKYDLWRYVSKVDEHIIRAYSMASYPEEKGIIMLNVRIATPPPRQ PDAPPGQMSSYIWSLKAGDKVTISGPFGEFFAKETDAEMVFIGGGAGMAPMRSHIFDQLK RLHSKRKMSFWYGARSKREIFYQEDFDQLQAENPNFVWHVALSDALPEDNWTGYTGFIHN VLYENYLKNHEAPEDCEYYMCGPPVMNAAVIKMLKDLGVEDENILLDDFGG
S15303 S15303 10-Sep-1999 10-Sep-1999 10-Sep-1999
probable CDP-6-deoxy-Delta(3,4)-glucoseen reductase (EC 1.3.1.-) hypothetical protein 7.6 Salmonella typhimurium Salmonella typhimurium Jiang, X.M. Neal, B. Santiago, F. Lee, S.J. Romana, L.K. Reeves, P.R. Mol. Microbiol. 51991695-713 Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2). MUID91260454 S15303 preliminary DNA 1-330 methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 22-72 domain cytochrome-b5 reductase homology 101-320 binding-site 2Fe-2S cluster (Cys) (covalent) 37,42,45,71 predicted 330 complete MSHIIKIFPSNIEFSGREDESILDAALSAGIHLEHSCKAGDCGICESDLLAGEVVDSKGN IFGQGDKILTCCCKPKTALELNAHFFPELAGQTKKIVPCKVNSAVLVSGDVMTLKLRTPP TAKIGFLPGQYINLHYKGVTRSYSIANSDESNGIELHVRNVPNGQMSSLIFGELQENTLM RIEGPCGTFFIRESDRPIIFLAGGTGFAPVKSMVEHLIQGKCRREIYIYWGMQYSKDFYS ALPQQWSEQHDNVHYIPVVSGDDAEWGGRKGFVHHAVMDDFDSLEFFDIYACGSPVMIDA SKKDFMMKNLSVEHFYSDAFTASNNIEDNL
S23479 S23479 10-Sep-1999 10-Sep-1999 10-Sep-1999
probable benzoate 1,2-dioxygenase (EC 1.14.12.10) reductase component benC Acinetobacter calcoaceticus Acinetobacter calcoaceticus Neidle, E.L. Hartnett, C. Ornston, L.N. Bairoch, A. Rekik, M. Harayama, S. Eur. J. Biochem. 2041992113-120 Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. MUID92155191 S23479 preliminary translation not shown DNA 1-338 EMBLM76990 NIDg141746 PIDg141749 methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 26-84 domain cytochrome-b5 reductase homology 113-335 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,83 predicted 338 complete MSNHQVALQFEDGVTRFICIAQGETLSDAAYRQQINIPMDCREGECGTCRAFCESGNYDM PEDNYIEDALTPEEAQQGYVLACQCRPTSDAVFQIQASSEVCKTKIHHFEGTLARVENLS DSTITFDIQLDDGQPDIHFLAGQYVNVTLPGTTETRSYSFSSQPGNRLTGFVVRNVPQGK MSEYLSVQAKAGDKMSFTGPFGSFYLRDVKRPVLMLAGGTGIAPFLSMLQVLEQKGSEHP VRLVFGVTQDCDLVALEQLDALQQKLPWFEYRTVVAHAESQHERKGYVTGHIEYDWLNGG EVDVYLCGPVPMVEAVRSWLDTQGIQPANFLFEKFSAN
C48360 C48360 E39049 10-Sep-1999 10-Sep-1999 10-Sep-1999
methane monooxygenase (EC 1.14.13.25) reductase chain Methylosinus trichosporium Methylosinus trichosporium Cardy, D.L. Laidler, V. Salmond, G.P. Murrell, J.C. Arch. Microbiol. 1561991477-483 The methane monooxygenase gene cluster of Methylosinus trichosporium: cloning and sequencing of the mmoC gene. MUID92153031 C48360 preliminary DNA 1-340 GBS81887 NIDg245213 PIDNAAB21393.1 PIDg245216 OB3b sequence extracted from NCBI backbone (NCBIN:81887, NCBIP:81915) Fox, B.G. Liu, Y. Dege, J.E. Lipscomb, J.D. J. Biol. Chem. 2661991540-550 Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction. MUID91093180 E39049 preliminary protein 1-13 methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 21-77 domain cytochrome-b5 reductase homology 108-336 binding-site 2Fe-2S cluster (Cys) (covalent) 37,41,44,76 predicted 340 complete MYQIVIETEDGETCRRMRPSEDWISRAEAERNLLASCRAGCATCKADCTDGDYELIDVKV QAVPPDEEEDGKVLLCRTFPRSDLHLLVPYTYDRISFEAIQTNWLAEILACDRVSSNVVR LVLQRSRPMAARISLNFVPGQFVDIEIPGTHTRRSYSMASVAEDGQLEFIIRLLPDGAFS KFLQTEAKVGMRVDLRGPAGSFFLHDHGGRSRVFVAGGTGLSPVLSMIRQLGKASDPSPA TLLFGVTNREELFYVDELKTLAQSMPTLGVRIAVVNDDGGNGVDKGTVIDLLRAELEIDL LLGHARRRRRRETARSCREDHRDRCPAWRSDFLEKFLASG
JQ0701 JQ0701 PS0319 10-Sep-1999 10-Sep-1999 10-Sep-1999
methane monooxygenase (EC 1.14.13.25) reductase component Methylococcus capsulatus Methylococcus capsulatus Stainthorpe, A.C. Lees, V. Salmond, G.P.C. Dalton, H. Murrell, J.C. Gene 91199027-34 The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). MUID90382694 JQ0701 DNA 1-348 GBM90050 GBM32314 NIDg149833 PIDNAAB62391.1 PIDg2243160 GBM58498 NIDg150022 PIDNAAA25384.1 PIDg150025 PS0319 protein 1,'T',3-16 This multicomponent enzyme catalyzes the conversion of methane to methanol using molecular oxygen. mmoC methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 27-83 domain cytochrome-b5 reductase homology 113-342 binding-site 2Fe-2S cluster (Cys) (covalent) 42,47,50,82 predicted 348 complete MQRVHTITAVTEDGESLRFECRSDEDVITAALRQNIFLMSSCREGGCATCKALCSEGDYD LKGCSVQALPPEEEEEGLVLLCRTYPKTDLEIELPYTHCRISFGEVGSFEAEVVGLNWVS SNTVQFLLQKRPDECGNRGVKFEPGQFMDLTIPGTDVSRSYSPANLPNPEGRLEFLIRVL PEGRFSDYLRNDARVGQVLSVKGPLGVFGLKERGMAPRYFVAGGTGLAPVVSMVRQMQEW TAPNETRIYFGVNHEPELFYIDELKSLERSMRNLTVKACVWHPSGDWEGEQGSPIDALRE DLESSDANPDIYLCGPPGMIDAACELVRSRGIPGEQVFFEKFLPSGAA
C41659 C41659 S23484 10-Sep-1999 10-Sep-1999 10-Sep-1999
benzoate 1,2-dioxygenase (EC 1.14.12.10) reductase component Pseudomonas putida plasmid TOL pWW0 Pseudomonas putida Harayama, S. Rekik, M. Bairoch, A. Neidle, E.L. Ornston, L.N. J. Bacteriol. 17319917540-7548 Potential DNA slippage structures acquired during evolutionary divergence of Acinetobacter calcoaceticus chromosomal benABC and Pseudomonas putida TOL pWWO plasmid xylXYZ, genes encoding benzoate dioxygenases. MUID92041666 C41659 preliminary DNA 1-336 GBM64747 NIDg151718 PIDNAAA26049.1 PIDg151721 Neidle, E.L. Hartnett, C. Ornston, L.N. Bairoch, A. Rekik, M. Harayama, S. Eur. J. Biochem. 2041992113-120 Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. MUID92155191 S23484 preliminary DNA 1-336 EMBLM64747 NIDg151718 PIDNAAA26049.1 PIDg151721 xylZ plasmid methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 25-82 domain cytochrome-b5 reductase homology 111-332 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,81 predicted 336 complete MTHKVATDFEDGVTRFIDANTGETVADAAYRQGINLPLDCRDGACGACKCFAESGRYSLG EEYIEDALSEAEAEQGYVLTCQMRAESDCVIRVPAASDVCKTQQAGYQAAISNVRQLSES TIALSIKSASLNQLAFLPGQYVNLQVPGSDQTRAYSFSSLQKDGEVSFLIRKLPGGLMSS FLTSLAKVGDSVSLAGPLGAFYLREIKRPLLLLAGGTGLAPFTAMLEKIAEQGGEHPLHL IYGVTHDHDLVEMDKLEAFAARIPNFSYSACVASPDSAYPQKGYVTQYIEPKQLNGGEVD IYLCGPPPMVEAVSQYIRAQGIQPANFYYEKFAASA
JN0640 JN0640 03-Dec-1999 03-Dec-1999 03-Dec-1999
naphthalene 1,2-dioxygenase (EC 1.14.12.12) reductase component nahAa protein Pseudomonas putida (strain G7) Pseudomonas putida Simon, M.J. Osslund, T.D. Saunders, R. Ensley, B.D. Suggs, S. Harcourt, A. Suen, W. Cruden, D.L. Gibson, D.T. Zylstra, G.J. Gene 127199331-37 Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB9816-4. MUID93252277 JN0640 DNA 1-328 GBM83949 NIDg151384 PIDNAAA25900.1 PIDg151385 This protein is a member of naphthalene dioxygenase multicomponent enzyme system, and is involved in the catabolism of naphthalene. nahAa methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 20-74 domain cytochrome-b5 reductase homology 103-323 binding-site 2Fe-2S cluster (Cys) (covalent) 35,40,43,73 predicted 328 complete MELLIQPNNRLISFSPGANLLEVLRENGVAISYSCMSGRCGTCRCRVTDGSVIDSGAGSG LPNLVDEHYVLACQSVLTHNCAIEIPETDEIVTHPARIIKGTVVAVESPTHDIRRLRVRL AKPFEFSPGQYATLQFSPEHARPYSMAGLPDDQEMEFHIRKVPGGRVTEYVFEHVREGTS IKLSGPLGTAYLRQNHTGPMLCVGGGTGLAPVLSIVRGALKLGMTNPILLYFGVRSQQDL YDAERLHKLAADHPQLTVHTVIAMGPINESQRAGLVTDVIEKDIISLAGWRAYLCGAPAM VEALCTVTKHLGISPEHIYADAFYPGGI
JN0642 JN0642 03-Dec-1999 03-Dec-1999 03-Dec-1999
naphthalene 1,2-dioxygenase (EC 1.14.12.12) reductase component nahAa protein Pseudomonas putida (strain NCIB9816-4) Pseudomonas putida Simon, M.J. Osslund, T.D. Saunders, R. Ensley, B.D. Suggs, S. Harcourt, A. Suen, W. Cruden, D.L. Gibson, D.T. Zylstra, G.J. Gene 127199331-37 Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida strains G7 and NCIB9816-4. MUID93252277 JN0642 DNA 1-328 GBM83950 NIDg151389 PIDNAAA25904.1 PIDg151390 This protein is a member of naphthalene dioxygenase multicomponent enzyme system, and is involved in the catabolism of naphthalene. nahAa methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 20-74 domain cytochrome-b5 reductase homology 103-323 binding-site 2Fe-2S cluster (Cys) (covalent) 35,40,43,73 predicted 328 complete MELLIQPNNRIIPFSAGANLLEVLRENGVAISYSCLSGRCGTCRCRVIDGSVIDSGAENG QSNLTDKQYVLACQSVLTGNCAIEVPEADEIVTHPARIIKGTVVAVESPTHDIRRLRVRL SKPFEFSPGQYATLQFSPEHARPYSMAGLPDDQEMEFHIRKVPGGRVTEYVFEHVREGTS IKLSGPLGTAYLRQKHTGPMLCVGGGTGLAPVLSIVRGALKSGMTNPILLYFGVRSQQDL YDAERLHKLAADHPQLTVHTVIATGPINEGQRAGLITDVIEKDILSLAGWRAYLCGAPAM VEALCTVTKHLGISPEHIYADAFYPGGI
A47016 A47016 10-Sep-1999 10-Sep-1999 10-Sep-1999
toluene-4-monooxygenase (EC 1.-.-.-) reductase component Pseudomonas mendocina Pseudomonas mendocina Yen, K.M. Karl, M.R. J. Bacteriol. 17419927253-7261 Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. MUID93054339 A47016 preliminary DNA 1-326 GBM95045 NIDg151596 PIDNAAA26004.1 PIDg151597 KR1 sequence extracted from NCBI backbone (NCBIN:118027, NCBIP:118029) tmoF methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 21-77 domain cytochrome-b5 reductase homology 107-320 binding-site 2Fe-2S cluster (Cys) (covalent) 36,41,44,76 predicted 326 complete MFNIQSDDLLHHFEADSNDTLLSAALRAELVFPYECNSGGCGACKIELLEGEVSNLWPDA PGLAARELRKNRFLACQCKPLSDLKIKVINRAEGRASHPPKRFSTRVVSKRFLSDEMFEL RLEAEQKVVFSPGQYFMVDVPELGTRAYSAANPVDGNTLTLIVKAVPNGKVSCALANETI ETLQLDGPYGLSVLKTADETQSVFIAGGSGIAPMVSMVNTLIAQGYEKPITVFYGSRLEA ELEAAETLFGWKENLKLINVSSSVVGNSEKKYPTGYVHEIIPEYMEGLLGAEFYLCGPPQ MINSVQKLLMIENKVPFEAIHFDRFF
JC5499 JC5499 PC4335 10-Sep-1999 10-Sep-1999 10-Sep-1999
para-isopropyl toluene methyl hydroxylase (EC 1.-.-.-) p-cymene methyl hydroxylase Pseudomonas aureofaciens Pseudomonas aureofaciens Dutta, T.K. Gunsalus, I.C. Biochem. Biophys. Res. Commun. 2331997502-506 Reductase gene sequences and protein structures: p-Cymene methyl hydroxylase. MUID97289661 JC5499 DNA 1-349 GBU86603 NIDg1840136 PIDNAAC45296.1 PIDg1840137 strain PJC the authors translated the codon ACC for residue 53 as Leu PC4335 protein 11-320 cymA methane monooxygenase reductase component cytochrome-b5 reductase homology ferredoxin [2Fe-2S] homology 2Fe-2S flavoprotein iron-sulfur protein metalloprotein oxidoreductase domain ferredoxin [2Fe-2S] homology 34-90 domain cytochrome-b5 reductase homology 119-343 binding-site 2Fe-2S cluster (Cys) (covalent) 49,54,57,89 predicted 349 complete MRSFFQSIFGKATPKQVQILPQDVTIVLEPGQTLLEAALANGIAYPHDCTVGTCASCKTR LKQGRVREATPFGYTLSKAELDAGYILACQAFPRDELTVVEIDPPSADLPPVEQFAATIV ATEPLTHDILKVTIQTDRPVHYLAGRYANVRVPGWPRFRCYSFANAPQRKGRNVLEFYIR KVPAGEFTEALFRGELDGQPLEMEAPQGTFHLHGGDAPMLCIAGGSGLAPLVSILEHARA NRIKRDCILLFGARTEGDLYQLEAIGNIAANWQGEFRFIPVLSHEPEHSDWTGARGLVTE HIPADFCEGAEGYLCGPPPMIDAAIARLLDNRLPLEKIFYDKFTDGRNS
O4HUD1 S01199 A28883 JC4156 A33629 A30335 31-Mar-1992 31-Mar-1992 03-Mar-2000
debrisoquine 4-hydroxylase (EC 1.14.14.-) cytochrome P450 2D6 CYP2D6 cytochrome P450 isozyme 2D cytochrome P450db1 human man Homo sapiens Gonzalez, F.J. Skoda, R.C. Kimura, S. Umeno, M. Zanger, U.M. Nebert, D.W. Gelboin, H.V. Hardwick, J.P. Meyer, U.A. Nature 3311988442-446 Characterization of the common genetic defect in humans deficient in debrisoquine metabolism. MUID88122614 S01199 translation not shown mRNA 1-497 EMBLX08006 NIDg30450 PIDNCAA30807.1 PIDg30451 Gonzalez, F.J. Vilbois, F. Hardwick, J.P. McBride, O.W. Nebert, D.W. Gelboin, H.V. Meyer, U.A. Genomics 21988174-179 Human debrisoquine 4-hydroxylase (P450IID1): cDNA and deduced amino acid sequence and assignment of the CYP2D locus to chromosome 22. MUID88314109 A28883 mRNA 1-497 EMBLM20403 NIDg181349 PIDNAAA52153.1 PIDg181350 Jiang, Q. Voigt, J.M. Colby, H.D. Biochem. Biophys. Res. Commun. 20919951149-1156 Molecular cloning and sequencing of a guinea pig cytochrome P4502D (CYP2D16): high level expression in adrenal microsomes. MUID95251703 JC4156 preliminary mRNA 1-497 Kimura, S. Umeno, M. Skoda, R.C. Meyer, U.A. Gonzalez, F.J. Am. J. Hum. Genet. 451989889-904 The human debrisoquine 4-hydroxylase (CYP2D) locus: sequence and identification of the polymorphic CYP2D6 gene, a related gene, and a pseudogene. MUID90072069 A33629 DNA 1-373,'V',375-497 EMBLM33388 NIDg181303 PIDNAAA53500.1 PIDg181304 Manns, M.P. Johnson, E.F. Griffin, K.J. Tan, E.M. Sullivan, K.F. J. Clin. Invest. 8319891066-1072 Major antigen of liver kidney microsomal autoantibodies in idiopathic autoimmune hepatitis is cytochrome P450db1. MUID89155788 A30335 mRNA 125-373,'V',375-485,'T',487-497 EMBLM24499 NIDg522194 PIDNAAA36403.1 PIDg522195 GDBCYP2D6 GDB132127 OMIM124030 22q13.1-22q13.1 60/3; 118/1; 169/1; 222/3; 281/3; 329/1; 391/3; 439/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 302-465 binding-site heme iron (Cys) (axial ligand) 443 predicted 497 complete MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVA DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI HEVQRFGDIVPLGMTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV FAFLVSPSPYELCAVPR
G02938 G02938 10-Sep-1999 10-Sep-1999 03-Mar-2000
probable debrisoquine 4-hydroxylase (EC 1.14.14.-) cytochrome P450 crab-eating macaque crab-eating macaque Macaca fascicularis Lawton, M.P. Laddison, K.J. Speirs, A.A. Mankowski, D.C. Tweedie, D.J. submitted to the EMBL Data Library October1995 G02938 translated from GB/EMBL/DDBJ mRNA 1-497 EMBLU38218 NIDg1022899 PIDNAAA79722.1 PIDg1022900 CYP2D17 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 302-465 binding-site heme iron (Cys) (axial ligand) 443 predicted 497 complete MELDALVPLAVTVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFKNTPYCFDQ LRRRFGNVFSLQLAWTPVVVLNGLAAVREALVTCGEDTADRPPVPINQVLGFGPRSQGVF LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFTDQAGRPFRPNSLLDK AVSNVIASLTYGRRFEYDDPRFLRLFDLTHEALKEESGFLREVLNAIPLLLRIPGLAGKV LRSQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNEENLRMVVA DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQARMPYTTAVI HEVQRFGDIVPLGVTHMTSRDIELQGFLIPKGTTLFTNLSSVLKDEAVWEKPFRFHPEHF LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPAGQPRPSHHGV FAFLVTPSPYELCAVPR
JC5819 JC5819 PC4502 S27177 S17048 10-Sep-1999 10-Sep-1999 18-Aug-2000
cytochrome P450 2D [validated] 25-hydroxyvitamin D(3) 25-monooxygenase cytochrome P450(14DM) cytochrome P450(25) lanosterol 14 alpha-demethylase vitamin D3 25-hydroxylase (EC 1.14.14.-) pig domestic pig Sus scrofa domestica Postlind, H. Axen, E. Bergman, T. Wikvall, K. Biochem. Biophys. Res. Commun. 2411997491-497 Cloning, structure, and expression of a cDNA encoding vitamin D3 25-hydroxylase. MUID98086378 JC5819 DNA 1-500 GBY16417 NIDg2956687 PIDNCAA76205.1 PIDg2956688 PC4502 protein 2-57;249-273;408-430 liver Axen, E. Bergman, T. Wikvall, K. Biochem. J. 2871992725-731 Purification and characterization of a vitamin D(3) 25-hydroxylase from pig liver microsomes. MUID93075023 S27177 protein 2-17 liver Sono, H. Sonoda, Y. Sato, Y. Biochim. Biophys. Acta 10781991388-394 Purification and characterization of cytochrome P-450(14DM) (lanosterol 14-alpha-demethylase) from pig liver microsomes. MUID91316123 S17048 preliminary protein 2-11 6-Leu was also found This enzyme catalyzes the first step in the metabolic activation of vitamin D3 into its hormonal form 1-alpha,25-dihydroxyvitamin D3. human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MGLLTGDLLGILALAMVIFLLLVDLMHRRSRWAPRYPPGPMPLPGLGNLLQVNFQDPRLS FIQLRRRFGDVFSLQQIWRPVVVLNGLAAVREALVSHSHETSDRPPVFILEHLGYGPRSE GVILARYGKAWREQRRFSVSTLRNFGLGKKSLEEWVTQEASCLCAAFADQAGRPFSPNNL LNKAVSNVIASLTFARRFEYNDPRMLKLLDLVLEGLKEEVGLMRQVLEAMPVLRHIPGLC AKLFPRQKAFLVMIDELITEHKMTRDLAQPPRDLTDAFLDEMKEAKGNPESSFNDENLRL VVAHLFSAGMITTSTTLAWALLLMILHPDVQRRVQQEIDEVIGHVRQPEIKDQALMPFTL AVLHEVQRFGDIVPLGVAHMTSCDIEVQGFLIPKGTTLITNLTSVLKDETVWKKPFRFYP EHFLDAQGRFTKQEAFMPFSAGRRSCLGEPLARMELFLFFTTLLQAFSFSVPTGQPCPSD HGVFAFLLFPSPYQLCAVPR
B26822 B26822 D32970 C31579 S16871 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 2D2 cytochrome P450CMF2 cytochrome P450db2 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Gonzalez, F.J. Matsunaga, T. Nagata, K. Meyer, U.A. Nebert, D.W. Pastewka, J. Kozak, C.A. Gillette, J. Gelboin, H.V. Hardwick, J.P. DNA 61987149-161 Debrisoquine 4-hydroxylase: characterization of a new P450 gene subfamily, regulation, chromosomal mapping, and molecular analysis of the DA rat polymorphism. MUID87217961 B26822 mRNA 1-500 EMBLM16655 NIDg203835 PIDNAAA41055.1 PIDg203836 the authors translated the codon CCT for residue 240 as Ala Matsunaga, E. Zanger, U.M. Hardwick, J.P. Gelboin, H.V. Meyer, U.A. Gonzalez, F.J. Biochemistry 2819897349-7355 The CYP2D gene subfamily: analysis of the molecular basis of the debrisoquine 4-hydroxylase deficiency in DA rats. MUID90057430 D32970 not compared with conceptual translation mRNA 1-500 Ishida, N. Tawaragi, Y. Inuzuka, C. Sugita, O. Kubota, I. Nakazato, H. Noguchi, T. Sassa, S. Biochem. Biophys. Res. Commun. 1561988681-688 Four species of cDNAs for cytochrome P450 isozymes immunorelated to P450c-M/F encode for members of P450IID subfamily, increasing the number of members within the subfamily. MUID89050091 C31579 mRNA 1-116,'D',118-345,'R',347-357,'F',359-406,'K',408-500 EMBLM22330 NIDg203823 PIDNAAA41049.1 PIDg203824 Matsunaga, E. Umeno, M. Gonzalez, F.J. J. Mol. Evol. 301990155-169 The rat P450 IID subfamily: complete sequences of four closely linked genes and evidence that gene conversions maintained sequence homogeneity at the heme-binding region of the cytochrome P450 active site. MUID90189185 S16871 DNA 1-345,'R',347-357,'F',359-406,'K',408-500 EMBLX52027 NIDg57811 PIDNCAA36269.1 PIDg57812 CYP2D2 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MGLLIGDDLWAVVIFTAIFLLLVDLVHRHKFWTAHYPPGPVPLPGLGNLLQVDFENMPYS LYKLRSRYGDVFSLQIAWKPVVVINGLKAVRELLVTYGEDTADRPLLPIYNHLGYGNKSK GVVLAPYGPEWREQRRFSVSTLRDFGVGKKSLEQWVTEEAGHLCDTFAKEAEHPFNPSIL LSKAVSNVIASLVYARRFEYEDPFFNRMLKTLKESFGEDTGFMAEVLNAIPILLQIPGLP GKVFPKLNSFIALVDKMLIEHKKSWDPAQPPRDMTDAFLAEMQKAKGNPESSFNDENLRL VVIDLFMAGMVTTSTTLSWALLLMILHPDVQRRVHEEIDEVIGQVLRPEMADQARMPLTN AVIHEVQRFADIVPTNIPHMTSRDIKFQGFLIPKGTTLIPNLSSVLEDETVWEKPLRFHP EHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVLAGRPRPST HGVYALPVTPQPYQLCAVAR
JE0258 JE0258 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 2D23 oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Yamamoto, Y. Ishizuka, M. Takada, A. Fujita, S. J. Biochem. 1241998503-508 Cloning, tissue distribution, and functional expression of two novel rabbit cytochrome P450 isozymes,CYP2D23 and CYP2D24. MUID98391821 JE0258 mRNA 1-500 DDBJAB008784 liver This protein shows high drug metabolizing activity. human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MGLLSGEALAPLAVAVAIFLLLVDLMHKRPRWAARYPPGPVGIPGLGNLLQVDFRGIPNC FRQLRRRYGDVFSLQLAWTPVVVLNGPAVIREALVTYGEDTADRPPAHTLEPLGFGPHAQ GVVMARYGPAWREQRRFSVSTLRNFGLGKKSLEQWVTEEATCLCAAFADHAGCPFSPSML LNKAVCNVIASLTHGCRFEYDDHRLTRLMDLTQTILKESTGNLPQVLNVIPILLRIPGLV DKVFRGQKAFMALLDELVTEHRMTRDPAQPPRDLTDAFLDQVEKAKGNPESSFNDDNLRL VVTDLFAAGMVTTSITLSWALLLMILHPDVQRRVQQEIDEVIGPARRPEMGDQARMPYTT AVVHEVQRFADIIPLGVPHQTSRDIEVQGFLIPKGTVLFTNLSSVLKDEAVWEKPFRFHP GHFLDAQGRFVKQEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPTGQPRPSD QGAPATLVTPAPYQLCAVAR
JE0259 JE0259 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 2D24 oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Yamamoto, Y. Ishizuka, M. Takada, A. Fujita, S. J. Biochem. 1241998503-508 Cloning, tissue distribution, and functional expression of two novel rabbit cytochrome P450 isozymes,CYP2D23 and CYP2D24. MUID98391821 JE0259 mRNA 1-500 DDBJAB008785 This protein shows high drug metabolizing activity. human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MGLLSGEALAPLAVAVAIFLLLVDLMHKRPRWAARYPPGPVGIPGLGNLLQVDFRGIPNC FRQLRCRYGDVFSLQLAWTPVVVLNGPAAMREALVTYGEDTADRPYSLSLEHLGFGPQAQ GVIMACYGHAWREQRRFSVSTLRNFGMGKKSLEHWVTEEAACLCAVFSEHAGHPFSPKAL LNKAIGNVIASLTFGCRFEYDDHRLTRLMDLIEIMLEESTGILPLVLNVIPILLRIPGLV DKVFHGQKAFMALLDELVTEHRMTRDPAQPPRDLTDAFLDQVEKAKGNPESSFNDDNLRL VVADLFVAGMFTTSFTLSWALLLMILHPDVQRRVQQEIDEVIGPARRPEMGDQARMPYTT AVVHEVQRFADIVPLGVPHQTLRDIEVQGFLIPKGTMLFTNLSSVLKDEAVWEKPFRFHP GHFLDAQGRFVKQEAFMPFSAGHRACLGEPLARMELFLFFTCLLQRFSFSVPAGQPQPSD QGAPATLVTPAPYQLCAVAR
JC4157 JC4157 S65962 S65898 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 2D, endoplasmic reticulum cytochrome P450 2D, microsomal oxidoreductase (EC 1.-.-.-) dog dog Canis lupus familiaris Jiang, Q. Voigt, J.M. Colby, H.D. Biochem. Biophys. Res. Commun. 20919951149-1156 Molecular cloning and sequencing of a guinea pig cytochrome P4502D (CYP2D16): high level expression in adrenal microsomes. MUID95251703 JC4157 mRNA 1-500 GBU21486 NIDg862481 Sakamoto, K. Kirita, S. Baba, T. Nakamura, Y. Yamazoe, Y. Kato, R. Takanaka, A. Matsubara, T. Arch. Biochem. Biophys. 3191995372-382 A new cytochrome P450 form belonging to the CYP2D in dog liver microsomes: purification, cDNA cloning, and enzyme characterization. MUID95305574 S65962 preliminary mRNA 1-500 EMBLD17397 NIDg397824 PIDNBAA04220.1 PIDg397825 S65898 protein 2-37,'X',39 This protein is a member of the CYP2D subfamily, it represents the isozyme associated with adrenal xenobiotic metabolism. CYP2D15 human cytochrome P450 CYP2D6 cytochrome P450 homology adrenal gland chromoprotein endoplasmic reticulum heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MGLLTGDTLGPLAVAVAIFLLLVDLMHRRRRWATRYPPGPTPVPMVGNLLQMDFQEPICY FSQLQGRFGNVFSLELAWTPVVVLNGLEAVREALVHRSEDTADRPPMPIYDHLGLGPESQ GLFLARYGRAWREQRRFSLSTLRNFGLGRKSLEQWVTEEASCLCAAFAEQAGRPFGPGAL LNKAVSNVISSLTYGRRFEYDDPRLLQLLELTQQALKQDSGFLREALNSIPVLLHIPGLA SKVFSAQKAIITLTNEMIQEHRKTRDPTQPPRHLIDAFVDEIEKAKGNPKTSFNEENLCM VTSDLFIAGMVSTSITLTWALLLMILHPDVQRRVQQEIDEVIGREQLPEMGDQTRMPFTV AVIHEVQRFGDIVPLGVPHMTSRDTEVQGFLIPKGTTLITNLSSVLKDEKVWKKPFRFYP EHFLDAQGHFVKHEAFMPFSAGRRVCLGEPLARMELFLFFTCLLQRFSFSVPAGQPRPSD HGVFTFLKVPAPFQLCVEPR
O4RTD5 S09611 A32970 S16874 B31579 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome P450 2D5 cytochrome P450CMF1b cytochrome P450db5 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Ishida, N. Inuzuka, C. Tawaragi, Y. Sugita, O. Nakazato, H. Noguchi, T. Sassa, S. Kappas, A. Nucleic Acids Res. 1719896407 Cytochrome P450CMF cDNA: nucleotide sequence of P450CMF1b. MUID89366685 S09611 mRNA 1-504 EMBLM25143 NIDg203775 PIDNAAA41034.1 PIDg203776 Matsunaga, E. Zanger, U.M. Hardwick, J.P. Gelboin, H.V. Meyer, U.A. Gonzalez, F.J. Biochemistry 2819897349-7355 The CYP2D gene subfamily: analysis of the molecular basis of the debrisoquine 4-hydroxylase deficiency in DA rats. MUID90057430 A32970 mRNA 1-504 EMBLJ02869 NIDg203673 PIDNAAA41003.1 PIDg203674 Matsunaga, E. Umeno, M. Gonzalez, F.J. J. Mol. Evol. 301990155-169 The rat P450 IID subfamily: complete sequences of four closely linked genes and evidence that gene conversions maintained sequence homogeneity at the heme-binding region of the cytochrome P450 active site. MUID90189185 S16874 DNA 1-504 EMBLX52030 NIDg57817 PIDNCAA36272.1 PIDg57818 Ishida, N. Tawaragi, Y. Inuzuka, C. Sugita, O. Kubota, I. Nakazato, H. Noguchi, T. Sassa, S. Biochem. Biophys. Res. Commun. 1561988681-688 Four species of cDNAs for cytochrome P450 isozymes immunorelated to P450c-M/F encode for members of P450IID subfamily, increasing the number of members within the subfamily. MUID89050091 B31579 mRNA 18-504 EMBLM22329 NIDg203806 PIDNAAA41045.1 PIDg203807 CYP2D5 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 504 complete MELLNGTGLWPMAIFTVIFILLVDLMHRHQRWTSRYPPGPVPWPVLGNLLQVDPSNMPYS MYKLQHRYGDVFSLQMGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQ GVVFASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQNGRSINPKAM LNKALCNVIASLIFARRFEYEDPYLIRMLTLVEESLIEVSGFIPEVLNTFPALLRIPGLA DKVFQGQKTFMAFLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRM VVVDLFTAGMVTTATTLTWALLLMILYPDVQRRVQQEIDEVIGQVRCPEMTDQAHMPYTN AVIHEVQRFGDIAPLNLPRITSCDIEVQDFVIPKGTTLIINLSSVLKDETVWEKPLRFHP EHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQHFSFSVPAGQPRPST LGNFAISVAPLPYQLCAAVREQGH
A26822 A26822 A30495 B32970 C32970 A31579 JC4158 S39761 03-Dec-1999 03-Dec-1999 03-Mar-2000
debrisoquine 4-hydroxylase (EC 1.14.14.-) cytochrome P450 2D1 cytochrome P450 UT-7 cytochrome P450db1 rat Norway rat Rattus norvegicus Gonzalez, F.J. Matsunaga, T. Nagata, K. Meyer, U.A. Nebert, D.W. Pastewka, J. Kozak, C.A. Gillette, J. Gelboin, H.V. Hardwick, J.P. DNA 61987149-161 Debrisoquine 4-hydroxylase: characterization of a new P450 gene subfamily, regulation, chromosomal mapping, and molecular analysis of the DA rat polymorphism. MUID87217961 A26822 mRNA 1-504 EMBLM16654 NIDg203833 PIDNAAA41054.1 PIDg203834 A30495 protein 'X',5-7,'X',9,'XX',12-23 Matsunaga, E. Zanger, U.M. Hardwick, J.P. Gelboin, H.V. Meyer, U.A. Gonzalez, F.J. Biochemistry 2819897349-7355 The CYP2D gene subfamily: analysis of the molecular basis of the debrisoquine 4-hydroxylase deficiency in DA rats. MUID90057430 B32970 mRNA 1-504 EMBLJ02867 NIDg203669 PIDNAAA41001.1 PIDg203670 C32970 mRNA 1-122,'VF',125-172,'R',174-379,'I',381-504 Ishida, N. Tawaragi, Y. Inuzuka, C. Sugita, O. Kubota, I. Nakazato, H. Noguchi, T. Sassa, S. Biochem. Biophys. Res. Commun. 1561988681-688 Four species of cDNAs for cytochrome P450 isozymes immunorelated to P450c-M/F encode for members of P450IID subfamily, increasing the number of members within the subfamily. MUID89050091 A31579 mRNA 1-122,'VF',125-172,'R',174-379,'I',381-504 EMBLM22328 NIDg203802 PIDNAAA41043.1 PIDg203803 Jiang, Q. Voigt, J.M. Colby, H.D. Biochem. Biophys. Res. Commun. 20919951149-1156 Molecular cloning and sequencing of a guinea pig cytochrome P4502D (CYP2D16): high level expression in adrenal microsomes. MUID95251703 JC4158 preliminary mRNA 1-504 Ohishi, N. Imaoka, S. Suzuki, T. Funae, Y. Biochim. Biophys. Acta 11581993227-236 Characterization of two P-450 isozymes placed in the rat CYP2D subfamily. MUID94072607 S39761 protein 1-9,'X',11-13 CYP2D1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein product cytochrome P450 2D1 1-504 experimental product cytochrome P450 2D1v 4-504 experimental domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 504 complete MELLNGTGLWSMAIFTVIFILLVDLMHRRHRWTSRYPPGPVPWPVLGNLLQVDLSNMPYS LYKLQHRYGDVFSLQKGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQ GVILASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQAGQSINPKAM LNKALCNVIASLIFARRFEYEDPYLIRMVKLVEESLTEVSGFIPEVLNTFPALLRIPGLA DKVFQGQKTFMALLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRM VVVDLFTAGMVTTATTLTWALLLMILYPDVQRRVQQEIDEVIGQVRCPEMTDQAHMPYTN AVIHEVQRFGDIAPLNLPRFTSCDIEVQDFVIPKGTTLIINLSSVLKDETVWEKPHRFHP EHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPVGQPRPST HGFFAFPVAPLPYQLCAVVREQGL
I49428 I49428 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 16a-ms2 oxidoreductase (EC 1.-.-.-) western wild mouse western wild mouse Mus spretus Sueyoshi, T. Kobayashi, R. Nishio, K. Aida, K. Moore, R. Wada, T. Handa, H. Negishi, M. Mol. Cell. Biol. 1519954158-4166 A nuclear factor (NF2d9) that binds to the male-specific P450 (Cyp 2d-9) gene in mouse liver. MUID95349581 I49428 preliminary translated from GB/EMBL/DDBJ mRNA 1-504 EMBLU20088 NIDg951101 PIDNAAC52246.1 PIDg951102 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 504 complete MELLNGTDLWPVAIFTVIFILLVDLTHQRQRWTSRYPPGPVPWPVLGNLLQVDLDNMPYS LYKLQKRYGDVFSLQMGWKPMVVINGLKAMKEVLLTCGEDTADRPPVPIFEHLGVKPGSQ GVILAPYGPEWREQRRFSVSTLRNFGLGKKSLEDWVTKEARHLCDAFTAQAGQSINPNTM LNNAVCNVIASLIFARRLEYEDPYLIRMLKVLKECFTEISGFIPGVLNAFPIFLRIPGLA DMVFQGQKSFMAILDNLLTENRTTWDPDQPPRNLTDAFLAEIEKAKGNPESSFNHENLRM VVGDLFTAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDAVIGQVRHPEMADQAHMPYTN AVIHEVQRFGDIAPLNLPRITSRDIEVQDFLIPKGSTLIPNLSSVLKDETVWEKPLHFHP EHFLDAQGHFVKPEAFMPFSAGHRSCLGEPLARMELFLFFTCLLQRFSISVPDGQPQPSN YRVHAIPVAPFPYQLCAVMREQEH
A27384 S15806 A27384 B30247 03-Dec-1999 03-Dec-1999 03-Mar-2000
steroid 16alpha-hydroxylase (EC 1.14.14.-) cytochrome P450 2D9 cytochrome P450 16alpha cytochrome P450ca testosterone 16alpha-hydroxylase mouse house mouse Mus musculus Wong, G. Itakura, T. Kawajiri, K. Skow, L. Negishi, M. J. Biol. Chem. 26419892920-2927 Gene family of male-specific testosterone 16-alpha-hydroxylase (C-P-450(16-alpha)) in mice. Organization, differential regulation, and chromosome localization. MUID89123394 S15806 translation not shown DNA 1-504 EMBLM24262 Wong, G. Kawajiri, K. Negishi, M. Biochemistry 2619878683-8690 Gene family of male-specific testosterone 16-alpha-hydroxylase (C-P-450-16-alpha) in mouse liver: cDNA sequences, neonatal imprinting, and reversible regulation by androgen. MUID88163547 A27384 mRNA 1-504 EMBLM23998 NIDg201972 PIDNAAA40427.1 PIDg201973 Ichikawa, T. Itakura, T. Negishi, M. Biochemistry 2819894779-4784 Functional characterization of two cytochrome P-450s within the mouse, male-specific steroid 16alpha-hydroxylase gene family: expression in mammalian cells and chimeric proteins. MUID89352551 B30247 mRNA 1-504 EMBLM27168 the authors translated the codon CAG for residue 54 as Leu and GAT for residue 55 as Gly the sequence shown follows the authors' translation Cyp2d-9 15 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 504 complete MELLTGTDLWPVAIFTVIFILLVDLTHQRQRWTSRYPPGPVPWPVLGNLLQVDLGNMPYS LYKLQNRYGDVFSLQMAWKPMVVINGLKAMKEMLLTCGEDTADRPPVPIFEYLGVKPGSQ GVVLAPYGPEWREQRRFSVSTLRNFGLGKKSLEDWVTKEANHLCDAFTAQAGQPINPNPM LNKSTCNVIASLIFARRFEYEDPFLIRMLKVLEQSLTEVSGLIPEVLNAFPILLRIPRLA DKALQGQKSFIAILDNLLTENRTTWDPVQAPRNLTDAFLAQIEKAKGNPESSFNDENLLM VVRDLFGAGMLTTSTTLSWALMLMILHPDVQRRVQQEIDEVIGQVRHPEMADQAHMPYTN AVIHEVQRFGDIVPVNLPRITSHDIEVQDFLIPKGTILLPNMSSMLKDESVWEKPLRFHP EHFLDAQGHFVKPEAFMPFSAGRRSCLGEALARMELFLFFTCLLQRFSFSVPDGQPQPSN SGVYGILVAPSPYQLCAVVRDQGH
B27384 B27384 10-Sep-1999 10-Sep-1999 10-Sep-1999
probable truncated cytochrome P450 2D9 (clone p16alpha-16) mouse house mouse Mus musculus Wong, G. Kawajiri, K. Negishi, M. Biochemistry 2619878683-8690 Gene family of male-specific testosterone 16-alpha-hydroxylase (C-P-450-16-alpha) in mouse liver: cDNA sequences, neonatal imprinting, and reversible regulation by androgen. MUID88163547 B27384 mRNA 1-294 EMBLM23997 NIDg201974 PIDNAAA40428.1 PIDg201975 This truncated protein is derived from a cDNA lacking exon 6 and, consequently, part of the heme-binding domain. It may be a structural component of testosterone 16alpha hydroxylase. Cyp2d-9 human cytochrome P450 CYP2D6 cytochrome P450 homology alternative splicing microsome transmembrane protein 294 complete MELLTGTDLWPVAIFTVIFILLVDLTHQRQRWTSRYPPGPVPWPVLGNLLQVDLGNMPYS LYKLQNRYGDVFSLQMAWKPMVVINGLKAMKEMLLTCGEDTADRPPVPIFEYLGVKPGSQ GVVLAPYGPEWREQRRFSVSTLRNFGLGKKSLEDWVTKEANHLCDAFTAQAGQPINPNPM LNKSTCNVIASLIFARRFEYEDPFLIRMLKVLEQSLTEVSGLIPEVLNAFPILLRIPRLA DKALQGQKSFIAILDNLLTENRTTWDPVQAPRNLTDAFLAQIEKAESNKKSMRS
A30247 A30247 S15807 S19168 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 2D10 cytochrome P450cb oxidoreductase (EC 1.-.-.-) mouse house mouse Mus musculus Ichikawa, T. Itakura, T. Negishi, M. Biochemistry 2819894779-4784 Functional characterization of two cytochrome P-450s within the mouse, male-specific steroid 16alpha-hydroxylase gene family: expression in mammalian cells and chimeric proteins. MUID89352551 A30247 mRNA 1-504 EMBLM27167 NIDg529437 PIDNAAA39878.1 PIDg529438 Wong, G. Itakura, T. Kawajiri, K. Skow, L. Negishi, M. J. Biol. Chem. 26419892920-2927 Gene family of male-specific testosterone 16-alpha-hydroxylase (C-P-450(16-alpha)) in mice. Organization, differential regulation, and chromosome localization. MUID89123394 S15807 translation not shown DNA 1-504 EMBLM24263 this sequence has been revised in reference S19168 Wong, G. Itakura, T. Kawajiri, K. Skow, L. Negishi, M. submitted to the EMBL Data Library July1989 S19168 DNA 1-45,'L',47-220,'LAYS',225-504 EMBLM24263 NIDg192919 PIDNAAA79023.1 PIDg387141 Cyp2d10 15 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 504 complete MELLTGAGLWSVAIFTVIFILLVDLMHRHQRWTSRYPPGPVPWPVQGNLLQVDLDNMPYS LYKLQNRYGDVFSLQMGWKPMVVINGLKAMKEVLLTCGEDTADRPQVPIFEYLGVKPGSQ GVVLAPYGPEWREQRRFSVSTLRNFGLGKKSLEDWVTKEARHLCDAFTAQAGQPINPNTM LNNAVCNVIASLIFARRFEYEDPYLIRMQKVLEDSLTEISGLIPEVLNMFPILLRIPGLP GKVFQGQKSLLAIVENLLTENRNTWDPDQPPRNLTDAFLAEIEKVKGNAESSFNDENLRM VVLDLFTAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDAVIGQVRHPEMADQARMPYTN AVIHEVQRFGDIAPLNLPRITSRDIEVQDFLIPKGSILIPNMSSVLKDETVWEKPLRFHP EHFLDAQGHFVKPEAFMPFSAGRRSCLGEPLARMELFLFFTCLLQHFSFSVPNGQPRPRN LGVFPFPVAPYPYQLCAVMREQGH
S19169 S19169 S15808 03-Dec-1999 03-Dec-1999 21-Jul-2000
cytochrome P450 2D11 cytochrome P450cc oxidoreductase (EC 1.-.-.-) mouse house mouse Mus musculus Wong, G. Itakura, T. Kawajiri, K. Skow, L. Negishi, M. submitted to the EMBL Data Library July1989 S19169 DNA 1-505 EMBLM24264 NIDg192921 PIDNAAA37514.1 PIDg387142 strain BALB/cJ Wong, G. Itakura, T. Kawajiri, K. Skow, L. Negishi, M. J. Biol. Chem. 26419892920-2927 Gene family of male-specific testosterone 16-alpha-hydroxylase (C-P-450(16-alpha)) in mice. Organization, differential regulation, and chromosome localization. MUID89123394 annotation the published nucleotide sequence has been revised in reference S19169 Cyp2d-11 15 63/3; 120/3; 172/1; 225/3; 284/3; 332/1; 395/3; 443/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-469 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 447 predicted 505 complete MELLTGAGLWSVAIFTVIFILLVDLMHRHQHWTSRCPPGPVPWPVLGNLLQVDLDNMPYS LYKLQNRYGDVFSLQMAWKPMVVINGLKAMKEMLLTCGEDTADRPPVPIFEYLGVKPGSQ GVVLAPYGPEWREQRRFSVSTLRNFGLGKKSLEEWVTKEARHLCDAFTAQAGQPINPNPM LNKSTCNVIASLIFARRFEYEDPFLIRMLKMLKECFTEISGFIPGVLNEFPIFLRIPGLA DMVFQGQKSFMAILDNLLTENRTTWDPDQPPRNLTDAFLAEIEKAKGNAESSFNDENLRM VVLDLFTAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDAVIGQVQHPEMADQARMPYTN AVIHEVQRFGTLLHCLCHASQVVTFTQVQDFLVTKGSTLIPNLSSVLKGETVWEKPLRFH PEHFLDAQGHFVKPEAFMPFSAGHRSCLGEALARMELFLFFTCLLQRFSISVPDGQPQPS NYRVHAIPVAPFPYQLCAVMHEQGH
JC4153 JC4153 PC4052 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 2D16, CYP2D16 oxidoreductase (EC 1.-.-.-) guinea pig guinea pig Cavia porcellus Jiang, Q. Voigt, J.M. Colby, H.D. Biochem. Biophys. Res. Commun. 20919951149-1156 Molecular cloning and sequencing of a guinea pig cytochrome P4502D (CYP2D16): high level expression in adrenal microsomes. MUID95251703 JC4153 mRNA 1-500 GBU21486 NIDg862481 PIDNAAA68479.1 PIDg862482 PC4052 protein 1-37 This protein is a member of the CYP2D subfamily, it represents the isozyme associated with adrenal xenobiotic metabolism. human cytochrome P450 CYP2D6 cytochrome P450 homology adrenal gland chromoprotein heme iron metalloprotein microsome oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 496 predicted 500 complete MGLLTGDALFSVAVAVAIFLLLVDLMHRRQRWAARYPPGPVPVPGLGNLLQVDFENMAYS CDKLRHQFGDVFSLQFVWTPVVVVNGLLAVREALVNNSTDTSDRPTLPTNALLGFGPKAQ GVIGAYYGPAWREQRRFSVSSLRNFGLGKKSLEQWVTEEAACLCAAFTNHAGQPFCPKAL LNKAVCNVISSLIYARRFDYDDPMVLRLLEFLEETLRENSSLKIQVLNSIPLLLRIPCVA AKVLSAQRSFIALNDKLLAEHNTGWAPDQPPRDLTDAFLTEMHKAQGNSESSFNDENLRL LVSDLFGAGMVTTSVTLSWALLLMILHPDVQRHVQEEIDEVIGQVRCPEMADQAHMPFTN AVIHEVQRFADIVPMGVPHMTSRDTEVQGFLIPKGTMLFTNLSSVLKDETVWEKPLHFHP GHFLDAEGRFVKREAFMPFSAGPRICLGEPLARMELFLFFTSLLQRFSFSVPEGQPRPSD RGAPYLVVLPSPYQLCAVLR
S37284 S37284 S29295 S29862 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 2D oxidoreductase (EC 1.-.-.-) bovine cattle Bos primigenius taurus Tsuneoka, Y. Matsuo, Y. Higuchi, R. Ichikawa, Y. Eur. J. Biochem. 2081992739-746 Characterization of the cytochrome P-450IID subfamily in bovine liver. Nucleotide sequences and microheterogeneity. MUID93011103 S37284 mRNA 1-500 EMBLX68481 NIDg295 PIDNCAA48501.1 PIDg296 clone pBVL 180 S29295 mRNA 14-111,'R',113-131,'R',133-162,'L',164-178,'G',180-219,'F',221-247,'R',249-255,'G',257-367,'A',369-412,'Q',414-500 EMBLX68013 NIDg293 PIDNCAA48149.1 PIDg294 clone pBVL 76 CYP2D human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MGLLSGDTLGPLAVALLIFLLLLDLMHRRSRWAPRYPPGPTPLPVLGNLLQVDFEDPRPS FNQLRRRFGNVFSLQQVWTPVVVLNGLAAVREALVYRSQDTADRPPPAVYEHLGYGPRAE GVILARYGDAWAEQRRFSLTTLRNFGLGKKSLEQWVTEEASCSCAAFADQAGRPFSPMDL LNKAVSNVIASLTFGCRFEYNDPRIIKLLDLTEDGLKEEPNLVRKVVEAVPVLLSIPGLA ARVFPAQKAFMALIDELIAEQKMTRDPTQPPRHLTDAFLDEVKEAKGNPESSFNDENLRL VVADLFSAGMVTTSTTLAWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMGDQALMPFTV AVVHEVQRFADIVPLGLPHMTSRDIEVQGFHIPKGTTLITNLSSVLKDETVWEKPFRFHP EHFLDAQGRFVKQEAFIPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPAGQPRPSE HGVFAFLVTPAPYQLCAVPR
D31579 S16873 D31579 I52313 03-Dec-1999 03-Dec-1999 21-Jul-2000
cytochrome P450 2D4 cytochrome P450CMF3 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Matsunaga, E. Umeno, M. Gonzalez, F.J. J. Mol. Evol. 301990155-169 The rat P450 IID subfamily: complete sequences of four closely linked genes and evidence that gene conversions maintained sequence homogeneity at the heme-binding region of the cytochrome P450 active site. MUID90189185 S16873 DNA 1-500 EMBLX52029 NIDg57815 PIDNCAA36271.1 PIDg57816 Ishida, N. Tawaragi, Y. Inuzuka, C. Sugita, O. Kubota, I. Nakazato, H. Noguchi, T. Sassa, S. Biochem. Biophys. Res. Commun. 1561988681-688 Four species of cDNAs for cytochrome P450 isozymes immunorelated to P450c-M/F encode for members of P450IID subfamily, increasing the number of members within the subfamily. MUID89050091 D31579 mRNA 177-500 EMBLM22331 NIDg203829 PIDNAAA41052.1 PIDg203830 Kawashima, H. Strobel, H.W. Biochem. Biophys. Res. Commun. 2091995535-540 cDNA cloning of a novel rat brain cytochrome P450 belonging to the CYP2D subfamily. MUID95251650 I52313 preliminary translated from GB/EMBL/DDBJ mRNA 1-326,'R',328-399,'I',401-472,'A',474-479,'N',481-482,'V',484-500 GBS77859 NIDg1200515 PIDNAAC52882.1 PIDg1200516 brain, strain Sprague-Dawley CYP2D4 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MRMPTGSELWPIAIFTIIFLLLVDLMHRRQRWTSRYPPGPVPWPVLGNLLQIDFQNMPAG FQKLRCRFGDLFSLQLAFESVVVLNGLPALREALVKYSEDTADRPPLHFNDQSGFGPRSQ GVVLARYGPAWRQQRRFSVSTFRHFGLGKKSLEQWVTEEARCLCAAFADHSGFPFSPNTL LDKAVCNVIASLLFACRFEYNDPRFIRLLDLLKDTLEEESGFLPMLLNVFPMLLHIPGLL GKVFSGKKAFVAMLDELLTEHKVTWDPAQPPRDLTDAFLAEVEKAKGNPESSFNDENLRV VVADLFMAGMVTTSTTLTWALLFMILHPDVQCRVQQEIDEVIGQVRRPEMADQARMPFTN AVIHEVQRFADILPLGVPHKTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHP EHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPTGQPRPSD YGIFGALTTPRPYQLCASPR
S16872 S16872 E32970 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 2D3 cytochrome P450db3 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Matsunaga, E. Umeno, M. Gonzalez, F.J. J. Mol. Evol. 301990155-169 The rat P450 IID subfamily: complete sequences of four closely linked genes and evidence that gene conversions maintained sequence homogeneity at the heme-binding region of the cytochrome P450 active site. MUID90189185 S16872 DNA 1-500 EMBLX52028 NIDg57813 PIDNCAA36270.1 PIDg57814 Matsunaga, E. Zanger, U.M. Hardwick, J.P. Gelboin, H.V. Meyer, U.A. Gonzalez, F.J. Biochemistry 2819897349-7355 The CYP2D gene subfamily: analysis of the molecular basis of the debrisoquine 4-hydroxylase deficiency in DA rats. MUID90057430 E32970 mRNA 1-500 EMBLJ02868 NIDg203671 PIDNAAA41002.1 PIDg203672 CYP2D3 63/3; 121/1; 172/1; 225/3; 284/3; 332/1; 394/3; 442/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 9-25 predicted domain cytochrome P450 homology 305-468 domain transmembrane 310-326 predicted binding-site heme iron (Cys) (axial ligand) 446 predicted 500 complete MELLAGTGLWPMAIFTVIFILLVDLMHRRQRWTSRYPPGPVPWPVLGNLLQVDLCNMPYS MYKLQNRYGDVFSLQMGWKPVVVINGLKAVQELLVTCGEDTADRPEMPIFQHIGYGHKAK GVVLCTYGPEWREQRRFSVSTLRNFGVGKKSLEQWVTDEASHLCDALTAEAGRPLDPYTL LNKAVCNVIASLIYARRFDYGDPDFIKVLKILKESMGEQTGLFPEVLNMFPVLLRIPGLA DKVFPGQKTFLTMVDNLVTEHKKTWDPDQPPRDLTDAFLAEIEKAKGNPESSFNDANLRL VVNDLFGAGMVTTSITLTWALLLMILHPDVQCRVQQEIDEVIGQVRHPEMADQAHMPFTN AVIHEVQRFADIVPMNLPHKTSRDIEVQGFLIPKGTTLIPNLSSVLKDETVWEKPLRFHP EHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPTGQPRPSD YGVFAFLLSPSPYQLCAFKR
A40938 A40938 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 ib oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Kikuta, Y. Sogawa, K. Haniu, M. Kinosaki, M. Kusunose, E. Nojima, Y. Yamamoto, S. Ichihara, K. Kusunose, M. Fujii-Kuriyama, Y. J. Biol. Chem. 266199117821-17825 A novel species of cytochrome P-450 (P-450-ib) specific for the small intestine of rabbits. cDNA cloning and its expression in COS cells. MUID92011499 A40938 preliminary mRNA 1-501 GBD90405 NIDg217717 PIDNBAA14401.1 PIDg217718 CYP2J1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 308-469 binding-site heme iron (Cys) (axial ligand) 447 predicted 501 complete MVAALSSLAAALGAGLHPKTLLLGAVAFLFFAYFLKTRRPKNYPPGPWRLPFLGNLFTLD MEKSHLQLQQFVKKYGNLFCLDLAGKSIVIVTGLPLIKEVLVHMDQNFINRPVPPIRERS FKKNGLIMSSGQLWKEQRRFALMTLRNFGLGKKSLEERIQEEARHLTEAMEKEGGQPFDA HFKINNAVSNIICSITFGERFEYHDGQFQELLKLFDEVMYLEASMLCQLYNIFPWIMKFL PGAHQTLFSNWKKLELFVSRMLENHKKDWNPAETRDFIDAYLKEMSKYPGSATSSFNEEN LICSTLDLFLAGTETTSDMRWGLLFMALYPEIQEKVHAEIDSVIGQWQQPSMASRESLPY TNAVIHEVQRMGNILPLNVPREVTVDTTLAGYHLPKGTVVLTNLTALHKDPEEWATPDTF NPEHFLENGQFKKKEAFIPFSIGKRACLGEQLAKSELFIFFTSLMQKFTFKPPSDEKLTL NFRMGITLSPVKHRICAIPRA
O4RTPB A00176 A54251 A22363 A29298 S03854 A92255 I54796 18-Aug-1982 17-May-1996 03-Mar-2000
cytochrome P450 2B1 cytochrome P450 b cytochrome P450, phenobarbital-inducible unspecific monooxygenase (EC 1.14.14.1) rat Norway rat Rattus norvegicus Fujii-Kuriyama, Y. Mizukami, Y. Kawajiri, K. Sogawa, K. Muramatsu, M. Proc. Natl. Acad. Sci. U.S.A. 7919822793-2797 Primary structure of a cytochrome p-450: coding nucleotide sequence of phenobarbital-inducible cytochrome p450 cDNA from rat liver. MUID82222224 A00176 mRNA 6-491 EMBLJ00719 NIDg203752 PIDNAAA41024.1 PIDg203753 the authors translated the codon GAT for residue 166 as Glu, CTG for residue 292 as Pro, and CGA for residue 378 as Gln Fujii-Kuriyama, Y. Mizukami, Y. Kawajiri, K. Sogawa, K. Muramatsu, M. Proc. Natl. Acad. Sci. U.S.A. 7919825443 Primary structure of a cytochrome P450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver. annotation the mistranslations shown in reference A93912 are acknowledged Roberts, E.S. Hopkins, N.E. Zaluzec, E.J. Gage, D.A. Alworth, W.L. Hollenberg, P.F. Biochemistry 3319943766-3771 Identification of active-site peptides from (3)H-labeled 2-ethynylnaphthalene-inactivated P450 2B1 and 2B4 using amino acid sequencing and mass spectrometry. MUID94190899 A54251 protein 290-301,'X' Suwa, Y. Mizukami, Y. Sogawa, K. Fujii-Kuriyama, Y. J. Biol. Chem. 26019857980-7984 Gene structure of a major form of phenobarbital-inducible cytochrome P-450 in rat liver. MUID85234490 A22363 DNA 1-91,'P',93-204,'R',206-327,'V',329-356,'H',358-391,'R',393-415,'V',417-433,'H',435-491 GBL00320 NIDg203816 PIDNAAA41046.1 PIDg203818 the authors translated the codon CAG for residue 57 as Gly, CCT for residue 92 as Ala, ATT for residue 146 as Val, TCC for residue 181 as Thr, AGG for residue 205 as Thr, AGC for residue 214 as Glu, AAA for residue 236 as Leu, AGC for residue 259 as Asn, GTT for residue 328 as Ile, CAT for residue 357 as Gln, GAC for residue 398 as Tyr, GTT for residue 416 as Ala, and CAC for residue 434 as Arg Rangarajan, P.N. Ravishankar, H. Padmanaban, G. Biochem. Biophys. Res. Commun. 1441987258-263 Isolation of a cytochrome P-450e gene variant and characterization of its 5' flanking sequences. MUID87213174 A29298 not compared with conceptual translation DNA 1-57 Oesch, F. Waxman, D.J. Morrissey, J.J. Honscha, W. Kissel, W. Friedberg, T. Arch. Biochem. Biophys. 270198923-32 Antibodies targeted against hypervariable and constant regions of cytochromes P450IIB1 and P450IIB2. MUID89192373 S03854 not compared with conceptual translation mRNA 1-18;146-160,'E',162-165;166,330-361;362-380;402-423 Botelho, L.H. Ryan, D.E. Levin, W. J. Biol. Chem. 25419795635-5640 Amino acid compositions and partial amino acid sequences of three highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, or 3-methylcholanthrene. MUID79194111 A92255 protein 1-3,'T',5-22 Fujii-Kuriyama, Y. Mizukami, Y. Taniguchi, T. Muramatsu, M. Int. Symp. Princess Takamatsu Cancer Res. Fund 12198231-40 Molecular cloning and coding nucleotide sequence of complementary DNA of cytochrome P-450 involved in metabolic activation of carcinogenic substances. MUID83160754 I54796 preliminary translated from GB/EMBL/DDBJ mRNA 6-491 GBM37134 NIDg203784 PIDNAAC42028.1 PIDg203785 CYP2B1 57/3; 112/1; 162/1; 215/3; 274/3; 322/1; 384/3; 432/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase phosphoprotein transmembrane protein domain cytochrome P450 homology 295-458 active-site Thr 302 predicted binding-site heme iron (Cys) (axial ligand) 436 predicted 491 complete MEPSILLLLALLVGFLLLLVRGHPKSRGNFPPGPRPLPLLGNLLQLDRGGLLNSFMQLRE KYGDVFTVHLGPRPVVMLCGTDTIKEALVGQAEDFSGRGTIAVIEPIFKEYGVIFANGER WKALRRFSLATMRDFGMGKRSVEERIQEEAQCLVEELRKSQGAPLDPTFLFQCITANIIC SIVFGERFDYTDRQFLRLLELFYRTFSLLSSFSSQVFEFFSGFLKYFPGAHRQISKNLQE ILDYIGHIVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHENLMISLLSLFFAGT ETSSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRSKMPYTDAVIHEIQRFS DLVPIGVPHRVTKDTMFRGYLLPKNTEVYPILSSALHDPQYFDHPDSFNPEHFLDANGAL KKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVSSHLAPKDIDLTPKESGIGKI PPTYQICFSAR
O4RTP2 A21162 A00177 B00176 B92255 S15589 A21872 A32736 S03855 I59060 04-Dec-1986 17-May-1996 01-Dec-2000
cytochrome P450 2B2 cytochrome P450 PB-4 cytochrome P450, phenobarbital-inducible cytochrome P450e-L oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Mizukami, Y. Sogawa, K. Suwa, Y. Muramatsu, M. Fujii-Kuriyama, Y. Proc. Natl. Acad. Sci. U.S.A. 8019833958-3962 Gene structure of a phenobarbital-inducible cytochrome P-450 in rat liver. MUID83247397 A21162 DNA 1-472,'M',474-491 EMBLJ00728 NIDg203845 PIDNAAA41056.1 PIDg203847 the authors translated the codon AGT for residue 4 as Thr, and ATG for residue 376 as Ala Frey, A.B. Waxman, D.J. Kreibich, G. J. Biol. Chem. 260198515253-15265 The structure of phenobarbital-inducible rat liver cytochrome P-450 isoenzyme PB-4. Production and characterization of site-specific antibodies. MUID86059379 A00177 protein 1-291,'P',293-320,'AE',323-475,'D',477-491 Fujii-Kuriyama, Y. Mizukami, Y. Kawajiri, K. Sogawa, K. Muramatsu, M. Proc. Natl. Acad. Sci. U.S.A. 7919822793-2797 Primary structure of a cytochrome p-450: coding nucleotide sequence of phenobarbital-inducible cytochrome p450 cDNA from rat liver. MUID82222224 B00176 mRNA 6-359,'S',361-362,'V',364-366,'V',368-406,'S',408-416,'N',418,'A',420-477,'G',479-491 nucleotide sequence for residues 1-5 is not given the authors translated the codon GAT for residue 166 as Glu, CTG for residue 292 as Pro, and CGA for residue 378 as Gln Fujii-Kuriyama, Y. Mizukami, Y. Kawajiri, K. Sogawa, K. Muramatsu, M. Proc. Natl. Acad. Sci. U.S.A. 7919825443 Primary structure of a cytochrome P450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver. annotation revisions the mistranslations in reference A93912 are acknowledged Botelho, L.H. Ryan, D.E. Levin, W. J. Biol. Chem. 25419795635-5640 Amino acid compositions and partial amino acid sequences of three highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, or 3-methylcholanthrene. MUID79194111 B92255 protein 1-3,'T',5-22 Lacroix, D. Desrochers, M. Lambert, M. Anderson, A. Gene 861990201-207 Alternative splicing of mRNA encoding rat liver cytochrome P450e (P450IIB2). MUID90215299 S15589 mRNA 105-113,'F',115-274,'VSPAWMRE',275-321,'E',323-491 EMBLM34452 NIDg203679 PIDNAAA41004.1 PIDg203680 translation of the nucleotide sequence is not complete Philips, I.R. Shephard, E.A. Ashworth, A. Rabin, B.R. Gene 24198341-52 A21872 mRNA 168-321,'E',323-443,'K',445-491 Affolter, M. Anderson, A. Biochem. Biophys. Res. Commun. 1181984655-662 Segmental homologies in the coding and 3' non-coding sequences of rat liver cytochrome P-450e and P-450b cDNAs and cytochrome P-450e-like genes. MUID84153837 A32736 mRNA 385-491 GBK01626 NIDg203782 PIDNAAA41037.1 PIDg203783 Oesch, F. Waxman, D.J. Morrissey, J.J. Honscha, W. Kissel, W. Friedberg, T. Arch. Biochem. Biophys. 270198923-32 Antibodies targeted against hypervariable and constant regions of cytochromes P450IIB1 and P450IIB2. MUID89192373 S03855 not compared with conceptual translation mRNA 329-358,'AS',361;362,363-380;402-423 Atchison, M.L. Adesnik, M. Proc. Natl. Acad. Sci. U.S.A. 8319862300-2304 Gene conversion in a cytochrome P-450 gene family. MUID86205943 I59060 preliminary translated from GB/EMBL/DDBJ DNA 323-431 GBM13234 NIDg203848 PIDNAAA41057.1 PIDg554434 CYP2B2 384/3 human cytochrome P450 CYP2D6 cytochrome P450 homology alternative splicing chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase phosphoprotein transmembrane protein domain cytochrome P450 homology 295-458 binding-site heme iron (Cys) (axial ligand) 436 predicted 491 complete MEPSILLLLALLVGFLLLLVRGHPKSRGNFPPGPRPLPLLGNLLQLDRGGLLNSFMQLRE KYGDVFTVHLGPRPVVMLCGTDTIKEALVGQAEDFSGRGTIAVIEPIFKEYGVIFANGER WKALRRFSLATMRDFGMGKRSVEERIQEEAQCLVEELRKSQGAPLDPTFLFQCITANIIC SIVFGERFDYTDRQFLRLLELFYRTFSLLSSFSSQVFEFFSGFLKYFPGAHRQISKNLQE ILDYIGHIVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHENLMISLLSLFFAGT ETGSTTLRYGFLLMLKYPHVTVKVQKEIDQVIGSHRPPSLDDRTKMPYTDAVIHEIQRFA DLAPIGLPHRVTKDTMFRGYLLPKNTEVYPILSSALHDPQYFDHPDTFNPEHFLDADGTL KKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVSSHLAPKDIDLTPKESGIAKI PPTYQICFSAR
O4RBPC A00179 A61538 S31279 A00178 B27717 C27717 E27717 20-Sep-1984 20-Sep-1984 03-Mar-2000
cytochrome P450 2B4 cytochrome P450-LM2 oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Tarr, G.E. Black, S.D. Fujita, V.S. Coon, M.J. Proc. Natl. Acad. Sci. U.S.A. 8019836552-6556 Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes. MUID84042509 A00179 protein 1-491 Parandoosh, Z. Fujita, V.S. Coon, M.J. Philpot, R.M. Drug Metab. Dispos. 15198759-67 Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of structure and inducibility. MUID87161284 A61538 protein 1-24 Gasser, R. Negishi, M. Philpot, R.M. Mol. Pharmacol. 33[32]198822-30 Primary structures of multiple forms of cytochrome P-450 isozyme 2 derived from rabbit pulmonary and hepatic cDNAs. header on page 22 gives volume number as 32 S31279 mRNA 1-491 EMBLM20856 NIDg164958 PIDNAAA65840.1 PIDg164959 Heinemann, F.S. Ozols, J. J. Biol. Chem. 25819834195-4201 The complete amino acid sequence of rabbit phenobarbital-induced liver microsomal cytochrome P-450. MUID83160983 A00178 protein 1-90,'E',92-94,96,95,97-98,101-134,'GY',137-140,'G',142-192,'K',194-220,'S',222-302,'A',304-460,'GNLSL',466-491 Komori, M. Imai, Y. Tsunasawa, S. Sato, R. Biochemistry 27198873-80 Microheterogeneity in the major phenobarbital-inducible forms of rabbit liver microsomal cytochrome P-450 as revealed by nucleotide sequencing of cloned cDNAs. MUID88163620 B27717 mRNA 301-313,'L',315-419,'M',421-491 clone b14 C27717 mRNA 52-103,'M',105-173,'V',175-220,'S',222-313,'L',315-424,'C',426-491 clone b46 the authors translated the codon AAG for residue 191 as Arg E27717 mRNA 297-479,'L',481-491 clone b54 Cytochromes P450 are a group of membrane-bound hemoprotein monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway and oxidizes a wide variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. CYP2B4 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase phosphoprotein transmembrane protein domain cytochrome P450 homology 295-458 binding-site heme iron (Cys) (axial ligand) 436 predicted 491 complete MEFSLLLLLAFLAGLLLLLFRGHPKAHGRLPPGPSPLPVLGNLLQMDRKGLLRSFLRLRE KYGDVFTVYLGSRPVVVLCGTDAIREALVDQAEAFSGRGKIAVVDPIFQGYGVIFANGER WRALRRFSLATMRDFGMGKRSVEERIQEEARCLVEELRKSKGALLDNTLLFHSITSNIIC SIVFGKRFDYKDPVFLRLLDLFFQSFSLISSFSSQVFELFPGFLKHFPGTHRQIYRNLQE INTFIGQSVEKHRATLDPSNPRDFIDVYLLRMEKDKSDPSSEFHHQNLILTVLSLFFAGT ETTSTTLRYGFLLMLKYPHVTERVQKEIEQVIGSHRPPALDDRAKMPYTDAVIHEIQRLG DLIPFGVPHTVTKDTQFRGYVIPKNTEVFPVLSSALHDPRYFETPNTFNPGHFLDANGAL KRNEGFMPFSLGKRICLGEGIARTELFLFFTTILQNFSIASPVPPEDIDLTPRESGVGNV PPSYQIRFLAR
O4RBC6 S12765 A27479 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome P450 2C16 cytochrome P450 1a, phenobarbital-inducible, hepatic oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Hassett, C. Omiecinski, C.J. Nucleic Acids Res. 1819901429-1434 Sequence and gene expression of rabbit cytochrome P450 IIC16: comparison to highly related family members. MUID90221865 S12765 mRNA 1-487 EMBLM29968 NIDg164966 PIDNAAA31226.1 PIDg164967 strain New Zealand White the authors translated the codon AGG for residue 330 as His Hassett, C. Omiecinski, C.J. Biochem. Biophys. Res. Commun. 1491987326-333 Use of a conserved consensus oligomer in the identification of cytochrome P-450 mRNAs. MUID88106440 A27479 mRNA 414-487 GBM18376 NIDg164922 PIDNAAA31215.1 PIDg164923 CYP2C16 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 1-20 predicted domain cytochrome P450 homology 291-454 binding-site heme iron (Cys) (axial ligand) 432 predicted 487 complete MDPVVVLVLGLCCLLLLSHWKQNSGRGKLPPGPTPFPIIGNILQIDAKDISKSLTKFSER YGPVFTVYLGMKPAVVLHGYQAVKEALVDLGEEFAGRGSFPMLDKVSKGLGIVFTNGKRW KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICS IIFHNRFDYKDEEFLKLLEKFNENVRILSSPWLQVCNNFPALIDYLPGSHKTLLKNSDYV KNFIMEKVKEHQKFLDVNNPRDFIDCFLIKMEQENHLEFTLESLVTTVFDLFGAGTETTS TTLRYSLLLLLKHPEVADKVQEEIERVIGRHRSPCMQDRSRMPYTDAVIHEIQRFIDLVP NNLPHTVTRDIKFRNYFIPKGTDIMTSLTSVLHDEKAFPNPKVFDPGHFLDESGNFKKSD YFMPFSAGKRICVGEALARMELFLFLTSILQNFKLQSLVEPKDLDITAVLNGFVSVPPSF QLCFIPV
O4RBP4 A00180 A37828 28-Feb-1986 28-Feb-1986 03-Mar-2000
progesterone monooxygenase (EC 1.14.99.4) cytochrome P450 2C5 cytochrome P450 form 1 progesterone 21-hydroxylase rabbit domestic rabbit Oryctolagus cuniculus Tukey, R.H. Okino, S. Barnes, H. Griffin, K.J. Johnson, E.F. J. Biol. Chem. 260198513347-13354 Multiple gene-like sequences related to the rabbit hepatic progesterone 21-hydroxylase cytochrome P-450 1. MUID86033780 A00180 mRNA 1-487 EMBLM11299 Pendurthi, U.R. Lamb, J.G. Nguyen, N. Johnson, E.F. Tukey, R.H. J. Biol. Chem. 265199014662-14668 Characterization of the CYP2C5 gene in 21L III/J rabbits. Allelic variation affects the expression of P450IIC5. MUID90354466 A37828 DNA 1-96,'R',98-487 GBM55664 GBJ05575 NIDg164968 PIDNAAA63461.1 PIDg164969 CYP2C5 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 291-454 binding-site heme iron (Cys) (axial ligand) 432 predicted 487 complete MDPVVVLVLGLCCLLLLSIWKQNSGRGKLPPGPTPFPIIGNILQIDAKDISKSLTKFSEC YGPVFTVYLGMKPTVVLHGYEAVKEALVDLGEEFAGTGSVPILEKVSKGLGIAFSNAKTW KEMRRFSLMTLRNFGMGKRSIEDRIQEEARCLVEELRKTNASPCDPTFILGCAPCNVICS VIFHNRFDYKDEEFLKLMESLNENVRILSSPWLQVYNNFPALLDYFPGIHKTLLKNADYI KNFIMEKVKEHQKLLDVNNPRDFIDCFLIKMEQENNLEFTLESLVIAVSDLFGAGTETTS TTLRYSLLLLLKHPEVAARVQEEIERVIGRHRSPCMQDRSRMPYTDAVIHEIQRFIDLLP TNLPHAVTRDVRFRNYFIPKGTDIITSLTSVLHDEKAFPNPKVFDPGHFLDESGNFKKSD YFMPFSAGKRMCVGEGLARMELFLFLTSILQNFKLQSLVEPKDLDITAVVNGFVSVPPSY QLCFIPI
O4RBP1 A00181 A34257 20-Sep-1984 16-Feb-1996 03-Mar-2000
cytochrome P450 2C1 oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Leighton, J.K. DeBrunner-Vossbrinck, B.A. Kemper, B. Biochemistry 231984204-210 Isolation and sequence analysis of three cloned cDNAs for rabbit liver proteins that are related to rabbit cytochrome P-450 (form 2), the major phenobarbital-inducible form. MUID84128536 A00181 mRNA 11-490 EMBLK01522 NIDg164914 PIDNAAA31211.1 PIDg164915 the authors translated the codon CAA for residue 48 as Lys, GAT for residue 133 as Asn, CTG for residue 291 as Val, AGT for residue 292 as Thr, GTG for residue 439 as Ala, and GCC for residue 441 as Val Zhao, J. Chan, G. Govind, S. Bell, P. Kemper, B. DNA Cell Biol. 9199037-48 Structure of 5' regions and expression of phenobarbital-inducible rabbit cytochrome P450IIC genes. MUID90197893 A34257 DNA 1-24 GBM74199 CYP2C1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 294-457 binding-site heme iron (Cys) (axial ligand) 435 predicted 490 complete MDPVVVLGLCLSCLLLLSLWKQSYGGGKLPPGPTPFPILGNILQIGIQDISKSFTKLSEV YGPVFTVYLGMKPTVVIHGYDAVKEALVDLGEEFSGRIVFPLTAKINKGYGIVFSNGKRW KETRRFSLMTLRDFGMGKRSIEDRVQEEARCLVEELRKTNGSPCNPTFILGAAPCNVICS VIFQNRFDYTDQDFLSLMGKLNENFKILNSPWVQMCNNFPILIDYLPGSHNKILRNNIYI RNYVLEKIKEHQETLDINNPRDFIDCFLIKMEQEKDNQQSEFTIENLMTTLSDVFGAGTE TTSTTLRYGLLLLMKHPEVIAKVQEEIERVIGRHRSPCMQDRSRMPYTDATVHEIQRYIN LIPNNVPRATTCNVKFRSYLIPKGTAVITSLTSMLYNDKEFPNPDRFDPGHFLDASGKFR KSDYFMPFSTGKRVCVGEVLARMELFLFLTAILQNFTPKPLVDPKDIDTTPLVSGLGRVP PLYQLSFIPA
O4RBP2 A27718 A00182 S15587 20-Sep-1984 16-Feb-1996 03-Mar-2000
laurate omega-minus-1 hydroxylase (EC 1.14.14.-) cytochrome P450 2C2 cytochrome P450 PBc2 rabbit domestic rabbit Oryctolagus cuniculus Imai, Y. Komori, M. Sato, R. Biochemistry 27198880-88 Comparison of primary structures deduced from cDNA nucleotide sequences for various forms of liver microsomal cytochrome P-450 from phenobarbital-treated rabbits. MUID88163622 A27718 mRNA 1-490 clone HP2 Leighton, J.K. DeBrunner-Vossbrinck, B.A. Kemper, B. Biochemistry 231984204-210 Isolation and sequence analysis of three cloned cDNAs for rabbit liver proteins that are related to rabbit cytochrome P-450 (form 2), the major phenobarbital-inducible form. MUID84128536 A00182 mRNA 12-470,'L',472-490 EMBLK01521 NIDg164912 PIDNAAA31210.1 PIDg164913 Govind, S. Bell, P.A. Kemper, B. DNA 51986371-382 Structure of genes in the cytochrome P-450PBc subfamily: conservation of intron locations in the phenobarbital-inducible family. MUID87053173 S15587 preliminary DNA 1-22 EMBLM14955 NIDg164908 PIDNAAA31208.1 PIDg164909 CYP2C2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 294-457 binding-site heme iron (Cys) (axial ligand) 435 predicted 490 complete MDLVVVLGLCLSCLLLLSLWKQSHGGGKLPPGPTPFPILGNVLQLDFKDLSKSLTNLSKV YGPVFTVYLGMKPTVVVHGYEAVKEALVDLGHELSGRSRFLVTAKLNKGFGVIFSNGKRW TETRRFSLMTLRNFGMGKRSIEERVQEEAHCLVEELRKTNASPCDPTFILGAAPCNVICS VIFQNRFDYTDQDFLSLMGKFNENFKILNSPWVQFCNCFPILFDYFPGSHRKAVKNIFYV KNYITEQIKEHQKSLDINNPRDFIDCFLIKMEQEKCNQQSEFTIENLLTTVSDVFMAGTE TTSTTLRYGLLLLMKHPEVIAKVQEEIERVIGRHRSPCMQDRSRMPYTDATVHEIQRYIN LIPNNVPHTTICNLKFRNYLIPKGTDVLTSLSSVLHDDKEFPNPDRFDPGHFLDASGNFR KSDYFMPFSTGKRVCVGEALARMELFLFLTAILQNFTPKPLVNPNNVDENPFSSGIVRVP PLYRVSFIPV
O4RBP3 A00183 A34534 A22606 20-Sep-1984 16-Feb-1996 03-Mar-2000
progesterone 16alpha-hydroxylase (EC 1.14.-.-) cytochrome P450 2C3 cytochrome P450 form 3b progesterone 6beta-hydroxylase rabbit domestic rabbit Oryctolagus cuniculus Leighton, J.K. DeBrunner-Vossbrinck, B.A. Kemper, B. Biochemistry 231984204-210 Isolation and sequence analysis of three cloned cDNAs for rabbit liver proteins that are related to rabbit cytochrome P-450 (form 2), the major phenobarbital-inducible form. MUID84128536 A00183 mRNA 87-489 EMBLK01523 the authors translated the codon AGC for residue 216 as Tyr, TGG for residue 360 as Leu, TTC for residue 361 as Val, and CTG for residue 471 as Val. An extra Phe between residues 222 and 223 and the codon given for residue 299 (TAG) are inconsistent with the codon usage table and the authors' translation Chan, G. Kemper, B. Biochemistry 2919903743-3750 Structure of the rabbit cytochrome P450IIC3 gene, a constitutive member of the P450IIC subfamily. MUID90254101 A34534 DNA 1-110 GBM31245 GBJ02901 GBM31246 GBM31247 Ozols, J. Heinemann, F.S. Johnson, E.F. J. Biol. Chem. 26019855427-5434 The complete amino acid sequence of a constitutive form of liver microsomal cytochrome P-450. MUID85182688 A22606 protein 1-48,'D',50-81,'G',83,'I',85-88,'Y',90-215,'Y',217-222,'G',223-337,'S',339-341,'S',343-359,'LV',362-428,'T',430-470,'V',472-489 CYP2C3 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 293-456 binding-site heme iron (Cys) (axial ligand) 434 predicted 489 complete MDLLIILGICLSCVVLLSLWKKTHGKGKLPPGPTPLPVVGNLLQLETKNINKSLSMLAKE YGSIFTLYFGMKPAVVLYGYETVKEALIDRGEEFSGRGIFPVFDRVTKGLGIVFSSGEKW KETRRFSLTVLRNLGMGKKTIEERIQEEALCLIQALRKTNASPCDPTFLLFCVPCNVICS VIFQNRFDYDDEKFKTLIKYFHENFELLGTPWIQLSNIFPILHYLPGSHRQLFKNIDGQI KFILEKVQEHQESLDSNNPRDFVDHFLIKMEKEKHKKQSEFTMDNLITTIWDVFSAGTDT TSNTLKFALLLLLKHPEITAKVQEEIEHVIGRHRSPCMQDRTRMPYTDAVMHEIQRYVDW FPTSLPHAVTQDIEFNGYLIPKGTDIIPSLTSVLYDDKEFPNPEKFDPGHFLDESGNFKK SDYFMPFSAGKRACVGEGLARMELFLLLTTILQHFTLKPLVDPKDIDPTPLENGFVSVPP SYELCFVPV
O4HUPB A00190 27-Nov-1985 27-Nov-1985 03-Mar-2000
cytochrome P450 2A3, hepatic cytochrome P450-LM2 unspecific monooxygenase (EC 1.14.14.1) human man Homo sapiens Phillips, I.R. Shephard, E.A. Ashworth, A. Rabin, B.R. Proc. Natl. Acad. Sci. U.S.A. 821985983-987 Isolation and sequence of a human cytochrome P-450 cDNA clone. MUID85140280 A00190 mRNA 1-331 GBK03192 NIDg181321 PIDNAAA52147.1 PIDg181322 Cytochromes P450 are a group of membrane-bound hemoprotein monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway and oxidizes a wide variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. GDBCYP2A3 GDB377635 19q13.2-19q13.2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 135-298 binding-site heme iron (Cys) (axial ligand) 276 predicted 331 fragment /RLRANIDPTLFLIRTFSNVISSIVFGDRFDYKDRELLSLFRIMLVIVPVHVNSTGQLYE MFSSVMKQLPGPQQQAFQLLQGLEDFIAKKVEHNTPLDPNSPRDFIDSFLIRMQEEEKNP NTEFYLEKLVMTSLNLFIGGTETVSTTLRYGFLLLIKHPGVEAKVHEEIDRVIGKNRQPK FEDRAKMPYMEAMIHEIQRFGDVIPMIWPGRVKKDTKFRDFFLPKGTEVYPMLGSVLRDP IFLSKPQDFNPQHFTELEGAPKKSDAFVPFSIGQPNCFGEGLARMELFLFFTTVMQNFRL KSSQSPKDIDVSPKHVGFPRFPRNYTMSFLPR
O4HUA6 S04698 S04581 A61272 S05946 A34271 B34271 S17220 S09329 31-Mar-1992 31-Mar-1992 03-Mar-2000
coumarin 7-hydroxylase (EC 1.14.14.-) cytochrome P450 2A6 CYP450 2A3 CYP450 2A3v CYP450 2A4 cytochrome P450MP81 human man Homo sapiens Yamano, S. Nagata, K. Yamazoe, Y. Kato, R. Gelboin, H.V. Gonzalez, F.J. Nucleic Acids Res. 1719894888 cDNA and deduced amino acid sequences of human P450 IIA3 (CYP2A3). MUID89315238 S04698 mRNA 1-494 EMBLX13929 the authors identified this protein as cytochrome P450IIA3 Miles, J.S. Bickmore, W. Brook, J.D. McLaren, A.W. Meehan, R. Wolf, C.R. Nucleic Acids Res. 1719892907-2917 Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity. MUID89263705 S04581 mRNA 6-28,'N',30-254,'K',256-325,'Q',327-494 EMBLX13897 NIDg29546 PIDNCAA32097.1 PIDg29547 326-Lys and 386-Leu were also found Yun, C.H. Shimada, T. Guengerich, F.P. Mol. Pharmacol. 401991679-685 Purification and characterization of human liver microsomal cytochrome P-450 2A6. MUID92049260 A61272 protein 1-13 liver Landsman, D. submitted to the EMBL Data Library January1989 S05946 mRNA 1-159,'H',161-494 EMBLX13930 NIDg30331 PIDNCAA32118.1 PIDg30332 Yamano, S. Tatsuno, J. Gonzalez, F.J. Biochemistry 2919901322-1329 The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. MUID90212623 A34271 mRNA 1-494 GBM33318 NIDg180986 PIDNAAA52067.1 PIDg180987 GBM33316 this allele was designated cytochrome P450 2A3 B34271 mRNA 1-159,'H',161-494 GBM33318 GBM33316 this allele was designated cytochrome P450 2A3v Maurice, M. Emiliani, S. Dalet-Beluche, I. Derancourt, J. Lange, R. Eur. J. Biochem. 2001991511-517 Isolation and characterization of a cytochrome P450 of the IIA subfamily from human liver microsomes. MUID91364703 S17220 protein 1-13,'X',15,'X',17-20 GDBCYP2A6 GDB377803 19q13.2-19q13.2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 298-461 binding-site heme iron (Cys) (axial ligand) 439 predicted 494 complete MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSN VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEK GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF ATIPRNYTMSFLPR
S45644 S45644 S62858 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 2K1 oxidoreductase (EC 1.-.-.-) rainbow trout rainbow trout Oncorhynchus mykiss Buhler, D.R. Yang, Y.H. Dreher, T.W. Miranda, C.L. Wang, J.L. Arch. Biochem. Biophys. 312199445-51 Cloning and sequencing of the major rainbow trout constitutive cytochrome P450 (CYP2K1): identification of a new cytochrome P450 gene subfamily and its expression in mature rainbow trout liver and trunk kidney. MUID94304231 S45644 mRNA 1-504 EMBLL11528 NIDg309631 PIDNAAA52078.1 PIDg309632 S62858 protein 1-15 CYP2K1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 307-469 binding-site heme iron (Cys) (axial ligand) 447 predicted 504 complete MSLIEDILQTSSTVTLLGTVLFLLVLYLRSSGSSSEEQGKEPPGPRPLPLLGNMLQLDLK KPYCTLCELSKKYGSIFTVHFGPKKVVVLAGYKTVKQALVNQAEDFGDRDITPVFYDFNQ GHGILFANGDSWKEMRRFALTNLRDFGMGKKGSEEKILEEIPYLIEVFEKHEGKAFDTTQ SVLYAVSNIISAIVYGSRFEYTDPLFTGMADRAKESIHLTGSASIQMYNMFPWLGPWINN LTRLKKNIADMKMEVIELVRGLKETLNPHMCRGFVDSFLVRKQTLEESGHMDSFYHDDNL VFSVGNLFSAGTDTTGTTLRWGLLLMTKYPHIQDQVQEEISRVIGSRQTLVEDRKNLPYT DAVIHETQRLANIVPMSVPHTTSRDVTFQGYFIKKGTSVIPLLTSVLQDDSEWESPNTFN PSHFLDEQGGFVKRDAFMAFSAGRRVCLGEGLARMELFLFFTSLLQRFRFSPPPGVTEDD LDLTPLLGFTLNPSPHQLCAVSRV
S68856 S68856 S74194 10-Sep-1999 10-Sep-1999 19-May-2000
cytochrome P450 2L oxidoreductase (EC 1.-.-.-) spiny lobster spiny lobster Panulirus argus James, M.O. Boyle, S.M. Trapido-Rosenthal, H.G. Smith, W.C. Greenberg, R.M. Shiverick, K.T. Arch. Biochem. Biophys. 329199631-38 cDNA and protein sequence of a major form of P450, CYP2L, in the hepatopancreas of the spiny lobster, Panulirus argus. MUID96201120 S68856 mRNA 1-492 EMBLU44826 NIDg1304739 PIDNAAB03106.1 PIDg1304740 hepatopancreas S74194 protein 1-10,'X',12-39 CYP2L1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase phosphoprotein transmembrane protein domain cytochrome P450 homology 295-458 binding-site heme iron (Cys) (axial ligand) 436 predicted 492 complete MLTGALLLLLLVVIVYLLDKKPSGLPPGIWGWPLVGRMPSRSKHLADQVKQLRKKYGDII TWRIGTRVNVFLCNFKLVKTALSKFECSDRPDFYTFKLFGEGNDVGVVFSNGVMWQTHRR FILRQLRDLGMGKSRLEAAIQHEAACLVQELKKHTDQPMPLPKSINLAVLNVIWKLVADH RYSLQDQEGQYFTQLLTTTTDNMQGFALNLFNYLPWLLMITPDFVKNWMGVRVLRDGVCE LKDYMKTFIKEHQATLDPSNPKDLLDAYLIDLQERKEDPLSTMNIETVRAVIMDLFGAGT ETTSTMIRWTILYLMKYPEVQAKIQREIDAAVPRGTLPSLEHKDKLAYFEATIHEVHRIV SLVPLGVSHYTNQDTELAGYRLPKGTVVMSHLECCHRDPSYWEKPNEFYPEHFLDDQGKF VKREHLVNFSVGRRVCVGESLARMELFVFLSAILQNFTFSAPKGEVLHTEKDPQQMLFSF PKPYQVIIRERE
O4HU6 A24797 S15803 S16714 B23585 S19336 28-Dec-1987 01-Mar-1996 03-Mar-2000
aryl hydrocarbon (benzo[a]pyrene) hydroxylase (EC 1.14.14.-) cytochrome P450 1A1 cytochrome P450c human man Homo sapiens Kawajiri, K. Watanabe, J. Gotoh, O. Tagashira, Y. Sogawa, K. Fujii-Kuriyama, Y. Eur. J. Biochem. 1591986219-225 Structure and drug inducibility of the human cytochrome P-450c gene. MUID87004629 A24797 DNA 1-512 EMBLX04300 NIDg30346 PIDNCAA27843.1 PIDg30347 Jaiswal, A.K. Gonzalez, F.J. Nebert, D.W. Nucleic Acids Res. 1319854503-4520 Human P(1)-450 gene sequence and correlation of mRNA with genetic differences in benzo[a]pyrene metabolism. MUID85242117 S15803 DNA 1-380,'L',382-461,'V',463-512 EMBLX02612 NIDg30340 PIDNCAA26458.1 PIDg30341 Jaiswal, A.K. Gonzalez, F.J. Nebert, D.W. Science 228198580-83 Human dioxin-inducible cytochrome P(1)-450: complementary DNA and amino acid sequence. MUID85142181 S16714 mRNA 1-461,'V',463-512 EMBLK03191 Quattrochi, L.C. Okino, S.T. Pendurthi, U.R. Tukey, R.H. DNA 41985395-400 Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. MUID86081170 B23585 mRNA 295-461,'V',463-484 GDBCYP1A1 GDB120604 OMIM108330 15q22-15q24 275/3; 318/1; 348/1; 389/2; 418/2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 314-479 binding-site heme iron (Cys) (axial ligand) 457 predicted 512 complete MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
O4MSM1 A23923 S15588 A00184 A45955 A24953 C24406 17-May-1985 01-Mar-1996 03-Mar-2000
aryl hydrocarbon (benzo[a]pyrene) hydroxylase (EC 1.14.14.-) cytochrome P450 1A1 cytochrome P1 450 cytochrome P450-P1 mouse house mouse Mus musculus Gonzalez, F.J. Kimura, S. Nebert, D.W. J. Biol. Chem. 26019855040-5049 Comparison of the flanking regions and introns of the mouse 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450 genes. MUID85182627 A23923 DNA 1-524 EMBLM10021 NIDg192887 PIDNAAA37507.1 PIDg387138 Kimura, S. Smith, H.H. Hankinson, O. Nebert, D.W. EMBO J. 619871929-1933 Analysis of two benzo[a]pyrene-resistant mutants of the mouse hepatoma Hepa-1 P(1)450 gene via cDNA expression in yeast. MUID88004400 S15588 mRNA 1-524 EMBLY00071 NIDg50625 PIDNCAA68277.1 PIDg50626 Kimura, S. Gonzalez, F.J. Nebert, D.W. J. Biol. Chem. 259198410705-10713 The murine Ah locus. Comparison of the complete cytochrome P-1-450 and P-3-450 cDNA nucleotide and amino acid sequences. MUID84289486 A00184 mRNA 4-524 EMBLK02588 NIDg192885 PIDNAAA37506.1 PIDg309204 Peterson, T.C. Gonzalez, F.J. Nebert, D.W. Biochem. Pharmacol. 3519862107-2114 Methylation differences in the murine P-1-450 and P-3-450 genes in wild-type and mutant hepatoma cell culture. MUID86269072 A45955 DNA 280-321 GBM25623 NIDg200175 PIDNAAA39868.1 PIDg554249 Gonzalez, F.J. Mackenzie, P.I. Kimura, S. Nebert, D.W. Gene 291984281-292 Isolation and characterization of full-length mouse cDNA and genomic clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-450. MUID85028449 A24953 mRNA 4-33 EMBLM10021 Cheng, K.C. Park, S.S. Krutzsch, H.C. Grantham, P.H. Gelboin, H.V. Friedman, F.K. Biochemistry 2519862397-2402 Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450. MUID86243357 C24406 protein 2-23,'X',25 strain C57BL/6 Gonzalez, F.J. Kimura, S. Nebert, D.W. J. Biol. Chem. 260198511884-11889 annotation Cyp1a1 9 279/3; 322/1; 352/1; 393/2; 422/2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 318-483 binding-site heme iron (Cys) (axial ligand) 461 predicted 524 complete MPSMYGLPAFVSATELLLAVTVFCLGFWVVRATRTWVPKGLKTPPGPWGLPFIGHMLTVG KNPHLSLTRLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVRQGDDFKGRPDLYSFTLIT NGKSMTFNPDSGPVWAARRRLAQNALKSFSIASDPTSASSCYLEEHVSKEANYLVSKLQK VMAEVGHFDPYKYLVVSVANVICAICFGQRYDHDDQELLSIVNLSNEFGEVTGSGYPADF IPVLRYLPNSSLDAFKDLNDKFYSFMKKLIKEHYRTFEKGHIRDITDSLIEHCQDRKLDE NANVQLSDDKVITIVLDLFGAGFDTVTTAISWSLMYLVTNPRVQRKIQEELDTVIGRDRQ PRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTTRDTSLNGFYIPKGCCVFVNQWQVNH DRELWGDPNEFRPERFLTPSGTLDKRLSEKVTLFGLGKRKCIGETIGRSEVFLFLAILLQ QIEFKVSPGEKVDMTPTYGLTLKHARCEHFQVQMRSSGPQHLQA
O4RTMC A00185 A93513 A24406 D60822 S15584 S69265 S09617 17-May-1985 27-Nov-1985 03-Mar-2000
unspecific monooxygenase (EC 1.14.14.1) cytochrome P450 1A1, hepatic cytochrome P450 MC2 cytochrome P450, 57K, 3-methylcholanthrene-inducible cytochrome P450c rat Norway rat Rattus norvegicus Sogawa, K. Gotoh, O. Kawajiri, K. Fujii-Kuriyama, Y. Proc. Natl. Acad. Sci. U.S.A. 8119845066-5070 Distinct organization of methylcholanthrene- and phenobarbital- inducible cytochrome P-450 genes in the rat. MUID84298082 A00185 DNA 1-524 GBK02246 NIDg203760 PIDNAAA41027.1 PIDg203761 Yabusaki, Y. Shimizu, M. Murakami, H. Nakamura, K. Oeda, K. Ohkawa, H. Nucleic Acids Res. 1219842929-2938 Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC. MUID84169583 A93513 mRNA 1-52,'M',54-524 GBX00469 NIDg56043 PIDNCAA25153.1 PIDg56044 Cheng, K.C. Park, S.S. Krutzsch, H.C. Grantham, P.H. Gelboin, H.V. Friedman, F.K. Biochemistry 2519862397-2402 Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450. MUID86243357 A24406 protein 2-23,'X',25-26 Amelizad, Z. Narbonne, J.F. Wolf, C.R. Robertson, L.W. Oesch, F. Biochem. Pharmacol. 3719883245-3249 Effect of nutritional imbalances on cytochrome P-450 isozymes in rat liver. MUID88293549 D60822 protein 2-20,'VV' Hines, R.N. Levy, J.B. Conrad, R.D. Iversen, P.L. Shen, M.L. Renli, A.M. Bresnick, E. Arch. Biochem. Biophys. 2371985465-476 Gene structure and nucleotide sequence for rat cytochrome P-450c. MUID85147736 S15584 DNA 1-493,'S',495-524 EMBLM26129 NIDg203754 PIDNAAA41025.1 PIDg203755 the authors translated the codon GAG for residue 278 as Gly, GAG for residue 291 as Gly, and AGT for residue 494 as Ser Cvrk, T. Hodek, P. Strobel, H.W. Arch. Biochem. Biophys. 3301996142-152 Identification and characterization of cytochrome P4501A1 amino acid residues interacting with a radiolabeled photoaffinity diazido-benzphetamine analogue. MUID96230251 S69265 protein 118-119;122-123,'X';'I',258-260;276-278;436-444;'X',462;469-470,'X',472-473;492-500 CYP1A1 279/3; 322/1; 352/1; 393/1; 422/2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 11-30 predicted domain cytochrome P450 homology 318-483 binding-site heme iron (Cys) (axial ligand) 461 predicted 524 complete MPSVYGFPAFTSATELLLAVTTFCLGFWVVRVTRTWVPKGLKSPPGPWGLPFIGHVLTLG KNPHLSLTKLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVKQGDDFKGRPDLYSFTLIA NGQSMTFNPDSGPLWAARRRLAQNALKSFSIASDPTLASSCYLEEHVSKEAEYLISKFQK LMAEVGHFDPFKYLVVSVANVICAICFGRRYDHDDQELLSIVNLSNEFGEVTGSGYPADF IPILRYLPNSSLDAFKDLNKKFYSFMKKLIKEHYRTFEKGHIRDITDSLIEHCQDRRLDE NANVQLSDDKVITIVFDLFGAGFDTITTAISWSLMYLVTNPRIQRKIQEELDTVIGRDRQ PRLSDRPQLPYLEAFILETFRHSSFVPFTIPHSTIRDTSLNGFYIPKGHCVFVNQWQVNH DQELWGDPNEFRPERFLTSSGTLDKHLSEKVILFGLGKRKCIGETIGRLEVFLFLAILLQ QMEFNVSPGEKVDMTPAYGLTLKHARCEHFQVQMRSSGPQHLQA
O4MSM3 B92495 B23923 A00186 A26373 B45955 A93512 B24953 E24406 D24406 28-Aug-1985 28-Aug-1985 03-Mar-2000
acetanilide 4-hydroxylase (EC 1.14.14.-) cytochrome P450 1A2 cytochrome P450-P3 mouse house mouse Mus musculus Gonzalez, F.J. Kimura, S. Nebert, D.W. J. Biol. Chem. 260198511884-11889 erratum B92495 DNA 1-513 Gonzalez, F.J. Kimura, S. Nebert, D.W. J. Biol. Chem. 26019855040-5049 Comparison of the flanking regions and introns of the mouse 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450 genes. MUID85182627 B23923 DNA 1-513 EMBLM10022 NIDg192892 PIDNAAA37508.1 PIDg387139 Kimura, S. Gonzalez, F.J. Nebert, D.W. J. Biol. Chem. 259198410705-10713 The murine Ah locus. Comparison of the complete cytochrome P-1-450 and P-3-450 cDNA nucleotide and amino acid sequences. MUID84289486 A00186 mRNA 1-513 EMBLK02589 Kimura, S. Nebert, D.W. Nucleic Acids Res. 1419866765-6766 cDNA and complete amino acid sequence of mouse P2-450: allelic variant of mouse P3-450 gene. MUID86312932 A26373 mRNA 1-383,'M',385-513 EMBLX04283 NIDg50627 PIDNCAA27832.1 PIDg50628 Peterson, T.C. Gonzalez, F.J. Nebert, D.W. Biochem. Pharmacol. 3519862107-2114 Methylation differences in the murine P-1-450 and P-3-450 genes in wild-type and mutant hepatoma cell culture. MUID86269072 B45955 preliminary DNA 277-315 GBM25624 NIDg200188 PIDNAAA39873.1 PIDg554250 Kimura, S. Gonzalez, F.J. Nebert, D.W. Nucleic Acids Res. 1219842917-2928 Mouse cytochrome P-3-450: complete cDNA and amino acid sequence. MUID84169582 A93512 mRNA 1-27,'QSLKDPGSQRPEESTRTL',46-513 EMBLX00479 the sequences from references A92443 and A93512 differ due to frameshifts in the reported nucleotide sequences Gonzalez, F.J. Mackenzie, P.I. Kimura, S. Nebert, D.W. Gene 291984281-292 Isolation and characterization of full-length mouse cDNA and genomic clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-450. MUID85028449 B24953 mRNA 1-27,'QSL' EMBLM10022 Cheng, K.C. Park, S.S. Krutzsch, H.C. Grantham, P.H. Gelboin, H.V. Friedman, F.K. Biochemistry 2519862397-2402 Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450. MUID86243357 E24406 mRNA 2-20,'X',22-26 strain DBA/2 D24406 protein 2-20,'X',22-24,'X',26 strain C57BL/6 Cyp1a2 position 9 276/3; 316/1; 346/1; 387/2; 416/2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 312-478 binding-site heme iron (Cys) (axial ligand) 456 predicted 513 complete MAFSQYISLAPELLLATAIFCLVFWMVRASRTQVPKGLKNPPGPWGLPFIGHMLTVGKNP HLSLTRLSQQYGDVLQIRIGSTPVVVLSGLNTIKQALVRQGDDFKGRPDLYSFTLITNGK SMTFNPDSGPVWAARRRLAQDALKSFSIASDPTSASSCYLEEHVSKEANHLVSKLQKAMA EVGHFEPVSQVVESVANVIGAMCFGKNFPRKSEEMLNIVNNSKDFVENVTSGNAVDFFPV LRYLPNPALKRFKTFNDNFVLFLQKTVQEHYQDFNKNSIQDITSALFKHSENYKDNGGLI PEEKIVNIVNDIFGAGFDTVTTAITWSILLLVTWPNVQRKIHEELDTVVGRDRQPRLSDR PQLPYLEAFILEIYRYTSFVPFTIPHSTTRDTSLNGFHIPKERCIYINQWQVNHDEKQWK DPFVFRPERFLTNNNSAIDKTQSEKVMLFGLGKRRCIGEIPAKWEVFLFLAILLQHLEFS VPPGVKVDLTPNYGLTMKPGTCEHVQAWPRFSK
O4RBBN B27821 S02038 B25143 A00187 A00188 A44250 28-May-1986 24-Feb-1994 03-Mar-2000
cytochrome P450 1A2 acetanilide 4-hydroxylase (EC 1.14.14.-) cytochrome P450 LM4 cytochrome P450-4 rabbit domestic rabbit Oryctolagus cuniculus Kagawa, N. Mihara, K. Sato, R. J. Biochem. 10119871471-1479 Structural analysis of cloned cDNAs for polycyclic hydrocarbon-inducible forms of rabbit liver microsomal cytochrome P-450. MUID88032911 B27821 mRNA 1-120,'H',122-516 EMBLX05686 NIDg1540 PIDNCAA29171.1 PIDg1541 Pompon, D. Eur. J. Biochem. 1771988285-293 cDNA cloning and functional expression in yeast Saccharomyces cerevisiae of beta-naphthoflavone-induced rabbit liver P-450 LM4 and LM6. MUID89052697 S02038 mRNA 1-173,'S',175-207,'H',209-232,'S',234-298,'G',300-353,'PG',356-516 EMBLX13853 NIDg1532 PIDNCAA32066.1 PIDg1533 the authors translated the codon GAC for residue 276 as Gln and CCC for residue 354 as Ala Okino, S.T. Quattrochi, L.C. Barnes, H.J. Osanto, S. Griffin, K.J. Johnson, E.F. Tukey, R.H. Proc. Natl. Acad. Sci. U.S.A. 8219855310-5314 Cloning and characterization of cDNAs encoding 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible rabbit mRNAs for cytochrome P-450 isozymes 4 and 6. MUID85270514 B25143 mRNA 'H',94-207,'H',209-287,'I',289-290,'N',292,'MD',295,'MDDGAHV',303-308,'T',310-357,'L',359-461,'I',463-516 EMBLM11728 NIDg165578 PIDNAAA31433.1 PIDg165579 Ozols, J. J. Biol. Chem. 26119863965-3979 Complete amino acid sequence of a cytochrome P-450 isolated from beta-naphthoflavone-induced rabbit liver microsomes. Comparison with phenobarbital-induced and constitutive isozymes and identification of invariant residues. MUID86140205 A00187 protein 2-21,'S',23-69,'Q',71-91,'N',93-171,'F',173-193,'S',195-207,'FPQGM',213-246,'QPN',250,'R',252-289,'SH',292-294;296-298,'G',300-493,'T',495-516 233-Ser and 247-Asn were also found Fujita, V.S. Black, S.D. Tarr, G.E. Koop, D.R. Coon, M.J. Proc. Natl. Acad. Sci. U.S.A. 8119844260-4264 On the amino acid sequence of cytochrome P-450 isozyme 4 from rabbit liver microsomes. MUID84272618 A00188 protein 2-45,'S',47,'V',49;107-118;133-173,'S',175-197,'X',199-206;217-232,'S',234-241,'V',243-246;255-264;267-274;297-298,'G',300-341;362-376,'XX',379-381;394-444,'A',446-477,'X',479-486;500-511,'S',513;'K' Yun, C.H. Hammons, G.J. Jones, G. Martin, M.V. Hopkins, N.E. Alworth, W.L. Guengerich, F.P. Biochemistry 31199210556-10563 Modification of cytochrome P450 1A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl. MUID93041749 A44250 protein 176-185 only this tryptic peptide was photoaffinify labeled by 4-azidobenphenyl, a substrate analog There are three forms of this protein that differ only in the absence or presence of the first one or two residues. CYP1A2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 314-480 binding-site heme iron (Cys) (axial ligand) 458 predicted 516 complete MAMSPAAPLSVTELLLVSAVFCLVFWAVRASRPKVPKGLKRLPGPWGWPLLGHLLTLGKN PHVALARLSRRYGDVFQIRLGSTPVVVLSGLDTIKQALVRQGDDFKGRPDLYSSSFITEG QSMTFSPDSGPVWAARRRLAQDSLKSFSIASNPASSSSCYLEEHVSQEAENLIGRFQELM AAVGRFDPYSQLVVSAARVIGAMCFGRRFPQGSEEMLDVVRNSSKFVETASSGSPVDFFP ILRYLPNRPLQRFKDFNQRFLRFLQKTVREHYEDFDRNSIQDITGALFKHSEKNSKANSG LIPQEKIVNLVNDIFGAGFDTITTALSWSLMYLVTNPRRQRKIQEELDAVVGRARQPRLS DRPQLPYLEAFILELFRHTSFVPFTIPHSTTRDTTLNGFHIPKECCIFINQWQINHDPQL WGDPEEFRPERFLTADGAAINKPLSEKVTLFGLGKRRCIGETLARWEVFLFLAILLQRLE FSVPPGVPVDLTPIYGLTMKHPRCEHVQARPRFSDQ
O4HU4 S16718 A25892 A23585 S07373 S22433 A60881 28-Dec-1987 31-Mar-1992 03-Mar-2000
cytochrome P450 1A2 cytochrome P450 HLd cytochrome P450-4 cytochrome P450-P3 oxidoreductase (EC 1.-.-.-) human man Homo sapiens Ikeya, K. Jaiswal, A.K. Owens, R.A. Jones, J.E. Nebert, D.W. Kimura, S. Mol. Endocrinol. 319891399-1408 Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. MUID90114205 S16718 DNA 1-515 EMBLM31664 NIDg181377 EMBLM31665 NIDg181378 EMBLM31666 NIDg181379 EMBLM31667 NIDg181380 PIDNAAA52163.1 PIDg181382 Quattrochi, L.C. Pendurthi, U.R. Okino, S.T. Potenza, C. Tukey, R.H. Proc. Natl. Acad. Sci. U.S.A. 8319866731-6735 Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA. MUID86313652 A25892 DNA 1-78,'S',80-510,'LP',512-515 EMBLL00388 GBL00389 EMBLM14337 NIDg181315 PIDNAAA35738.1 PIDg181317 Quattrochi, L.C. Okino, S.T. Pendurthi, U.R. Tukey, R.H. DNA 41985395-400 Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. MUID86081170 A23585 mRNA 295-310,'L',312-449,'M',450,'V',452-485 GBM12078 NIDg181351 PIDNAAA52154.1 PIDg553246 Jaiswal, A.K. Nebert, D.W. Gonzalez, F.J. Nucleic Acids Res. 1419866773-6774 Human P(3)450: cDNA and complete amino acid sequence. MUID86312938 S07373 translation not shown mRNA 1-515 EMBLZ00036 NIDg30338 PIDNCAA77335.1 PIDg30339 Jaiswal, A.K. Nebert, D.W. McBride, O.W. Gonzalez, F.J. J. Exp. Pathol. 319871-17 Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15. MUID88061719 S22433 preliminary mRNA 1-515 EMBLM55053 NIDg181307 PIDNAAA52146.1 PIDg181308 Wrighton, S.A. Campanile, C. Thomas, P.E. Maines, S.L. Watkins, P.B. Parker, G. Mendez-Picon, G. Haniu, M. Shively, J.E. Levin, W. Guzelian, P.S. Mol. Pharmacol. 291986405-410 Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat. MUID86203234 A60881 protein 2-19 GDBCYP1A2 GDB118780 OMIM124060 15q22-15qter 277/3; 318/1; 348/1; 389/2; 418/2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein microsome monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 314-480 binding-site heme iron (Cys) (axial ligand) 458 predicted 515 complete MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
A54116 A54116 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 1B1 oxidoreductase (EC 1.-.-.-) human man Homo sapiens Sutter, T.R. Tang, Y.M. Hayes, C.L. Wo, Y.Y.P. Jabs, E.W. Li, X. Yin, H. Cody, C.W. Greenlee, W.F. J. Biol. Chem. 269199413092-13099 Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. MUID94230403 A54116 preliminary mRNA 1-543 GBU03688 NIDg501030 PIDNAAA19567.1 PIDg501031 GDBCYP1B1 GDB353515 OMIM601771 2pter-2qter human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 327-492 binding-site heme iron (Cys) (axial ligand) 470 predicted 543 complete MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV FVNQWSVNHDPVKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE TCQ
O4CHC7 JT0318 30-Jun-1989 30-Jun-1989 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 cytochrome P450(c17) steroid 17alpha-hydroxylase chicken chicken Gallus gallus Ono, H. Iwasaki, M. Sakamoto, N. Mizuno, S. Gene 66198877-85 cDNA cloning and sequence analysis of a chicken gene expressed during the gonadal development and homologous to mammalian cytochrome P-450c17. MUID88329730 JT0318 mRNA 1-508 GBM21406 NIDg212492 PIDNAAA48997.1 PIDg212493 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein monooxygenase ovary oxidoreductase steroid biosynthesis testis domain cytochrome P450 homology 302-467 binding-site heme iron (Cys) (axial ligand) 445 predicted 508 complete MPPLAVLLLALALLCAWRLSYSQGPTGTGTGRPRSLPALPLVGSLLQLAGHPQLHLRLWR LQGRYGSLYGLWMGSHYVVVVNSYQHAREVLLKKGKAFAGRPRTVTTDLLSRGGKDIAFA SYGPLWKFQRKLVHAALSMFGEGSVALEKIICREAASLCETLGAAQDMALDMAPELTRAV TNVVCSLCFNSSYRRGDPEFEAMLEYSQGIVDTVAKESLVDIFPWLQIFPNRDLALLKRC LKVRDQLLQQKFTEHKEAFCGDTVRDLMDALLQVRLNAENNSPLEPGLELTDDHLLMTVG DIFGAGVETTTTVLKWAVLYLLHYPEVQKKIQEEMDQKIGLARHPHLSDRPLLPYLEATI SEGLRIRPVSPLLIPHVSLADTSIGEYSIPKGARVVINLWSVHHDEKEWDKPEEFNPGRF LDEQGQHIHSPSPSYLPFGAGIRVCLGEVLAKMELFLFLAWVLQRFTLECPQDQPLPSLE GKFGVVLQVQKFRVKARLREAWRGEMVR
S21125 S21125 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 cytochrome P450 c17 steroid 17,20-lyase rainbow trout rainbow trout Oncorhynchus mykiss Sakai, N. Tanaka, M. Adachi, S. Miller, W.L. Nagahama, Y. FEBS Lett. 301199260-64 Rainbow trout cytochrome P-450(c17) (17alpha-hydroxylase/17,20-lyase). cDNA cloning, enzymatic properties and temporal pattern of ovarian P-450(c17) mRNA expression during oogenesis. MUID93083625 S21125 preliminary mRNA 1-514 EMBLZ14246 EMBLX65800 NIDg64316 PIDNCAA46675.1 PIDg64317 CYP17 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron membrane protein metalloprotein microsome monooxygenase oxidoreductase domain cytochrome P450 homology 306-471 binding-site heme iron (Cys) (axial ligand) 449 predicted 514 complete MAWFLCMCVFSVVGLGLLLLQVKLRRSLETRGGPPSLPVFPLIGSLLSLRSNQAPHVLFQ KLQQKYGHTYSLMMGPHTVILVNHHQHAKEVLLKKGKIFAGRPRTVTTDLLTRDGKDIAF ADYGATWRFHRKTVHGALCMFGEGSASIEKIICREALSLCDTLRESGSASLDLSPELTRA VTNVVCSLCFSSSYCRGDPEFEAMLQFSQGIVDTVAKDSLVDIFPWLQVFPNADLRLLKQ CVSIRDKLLQKKYEEHKSDYSDHEQRDLLDALLRAKRSAENNNTAEITMETVGLSEDHLL MTVGDIFGAGVETTSTVLKWAIAYLIHHPQVQQRIQEELDSVVGGDRTPQLSDRGSLPYL EATIREVLRIRPVAPLLIPHVAQTDTSIGKFTVRKGARIIINLWSLHHDEKEWKNPEMFD PGRFLNEEGTGLCIPSPSYLPFGAGVRVCLGEALAKMEIFLFLSWILQRLTMTVSPGQPL PSLEGKFGVVLQPVKYKVNATPRAGWEKSHLQTS
I51281 I51281 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 c17 spiny dogfish spiny dogfish Squalus acanthias Trant, J.M. J. Exp. Zool. 272199525-33 Isolation and characterization of the cDNA encoding the spiny dogfish shark (Squalus acanthias) form of cytochrome P450c17. MUID95256824 I51281 preliminary translated from GB/EMBL/DDBJ mRNA 1-509 GBS77384 NIDg999087 PIDNAAB34256.1 PIDg999088 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron membrane protein metalloprotein microsome monooxygenase oxidoreductase domain cytochrome P450 homology 302-467 binding-site heme iron (Cys) (axial ligand) 445 predicted 509 complete MSLMLAALILTVAFVICSLTGFTQRKLSGGRLPKCLPSFPLIGSLLSLRSDLPPHLLFQK LQKTYGNLFSLMMGPHYAVVINNHQHAKEVLLKKGKIFAGRPSMVTTDLLSRGGKDIAFG KYGPAWKFHRKLVLSALHLFGDGSAGIEKMICQEATSMCSTFERLNNAAHDMMPDVTRAV TNVICLLCFNSTYEKEDPEFQTMRKYSQGIVNTVAKDSLIDIFPWLQFFPNENLHTLKQC IATRDSILQKKFEDHKANYSSDSANDLFNILLKAKMNAENNNSSVHEAGLTDDHMVMTVA DIFGAGVETSSTAFAWMIIYLIHHPEVQKKIQEEIDSNIGFERTPKMSDKGNMNFLNATI HEILRIQPVSPLLIPHVALADSSIGDYTIPKGTRVIINLWAIHHDEKEWKNPDAFDPGRF LDEDGKYVCSSSESYLPFGAGTRVCLGEMLARMELFLFTSWILQRFTVQVPPGYPPPDKE GKFGIVLQPLKFKVQLKLRKAWENRGLHD
A26366 A40921 A40908 A26366 A29587 S16717 S16903 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 cytochrome P450(17alpha) steroid 17alpha-hydroxylase human man Homo sapiens Kagimoto, M. Winter, J.S.D. Kagimoto, K. Simpson, E.R. Waterman, M.R. Mol. Endocrinol. 21988564-570 Structural characterization of normal and mutant human steroid 17alpha-hydroxylase genes: molecular basis of one example of combined 17alpha-hydroxylase/17,20 lyase deficiency. MUID88334559 A40921 DNA 1-508 GBM31146 GBM31153 NIDg181284 the authors translated the codon TCT for residue 154 as Cys Bradshaw, K.D. Waterman, M.R. Couch, R.T. Simpson, E.R. Zuber, M.X. Mol. Endocrinol. 11987348-354 Characterization of complementary deoxyribonucleic acid for human adrenocortical 17alpha-hydroxylase: a probe for analysis of 17alpha-hydroxylase deficiency. MUID90331926 A40908 not compared with conceptual translation mRNA 1-508 Chung, B.C. Picado-Leonard, J. Haniu, M. Bienkowski, M. Hall, P.F. Shively, J.E. Miller, W.L. Proc. Natl. Acad. Sci. U.S.A. 841987407-411 Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. MUID87092418 A26366 mRNA 1-508 GBM14564 NIDg181341 PIDNAAA52151.1 PIDg181342 adrenal gland Picado-Leonard, J. Miller, W.L. DNA 61987439-448 Cloning and sequence of the human gene for P450c17 (steroid 17-alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21. MUID88054468 A29587 DNA 1-21,'W',23-508 GBM19489 NIDg189442 PIDNAAA36405.1 PIDg386992 GBM63871 NIDg189444 PIDNAAA59984.1 PIDg189445 the authors translated the codon TGG for residue 22 as Cys GDBCYP17 GDB119829 OMIM202110 10q24.3-10q24.3 99/3; 146/1; 222/3; 251/3; 323/3; 380/2; 415/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 299-464 binding-site heme iron (Cys) (axial ligand) 442 predicted 508 complete MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKY GPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAH WQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRN DLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIF GAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREV LRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNP AGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP KVVFLIDSFKVKIKVRQAWREAQAEGST
S22339 S22339 S24233 B26366 S30074 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 cytochrome P450(C17) steroid 17alpha-hydroxylase pig domestic pig Sus scrofa domestica Conley, A.J. Graham-Lorence, S.E. Kagimoto, M. Lorence, M.C. Murry, B.A. Oka, K. Sanders, D. Mason, J.I. Biochim. Biophys. Acta 1130199275-77 Nucleotide sequence of a cDNA encoding porcine testis 17alpha-hydroxylase cytochrome P-450. MUID92182016 S22339 preliminary mRNA 1-509 EMBLM63507 NIDg164396 PIDNAAA31008.1 PIDg164397 Zhang, P. Nason, T.F. Han, X.G. Hall, P.F. Biochim. Biophys. Acta 11311992345-348 Gene for 17-alpha-hydroxylase/C(17-20) lyase P-450: complete nucleotide sequence of the porcine gene and 5' upstream sequence of the rat gene. MUID92329554 S24233 DNA 1-50,'I',52-107,117-291,'S',293-318,'ATLC',322-329,'E',331-332,'E',334-406,'H',408-509 EMBLZ11854 GBS40340 NIDg1855 PIDNCAA77878.1 PIDg833797 the authors translated the codon TCC for residue 94 as Glu Chung, B.C. Picado-Leonard, J. Haniu, M. Bienkowski, M. Hall, P.F. Shively, J.E. Miller, W.L. Proc. Natl. Acad. Sci. U.S.A. 841987407-411 Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues. MUID87092418 B26366 protein 1-45,'F','L',54-69,'D',71-97,'K',99-116,'E',118-125,'S',127,'F',141-160,'VIQNA',183,'EMDRL',189,'EI',192-195,'D',197-200,'IEE',204,'E',206,'T',211-237,'E',239-256,265,'L',267-270,286-290,302,'C',304-307,'V',309-310,'FI',313-314,329,'E',331-332,'E',334-388,'A',390-394,'S',396,'F',398-406,'H',408-509 adrenal gland, testis CYP17 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 299-464 binding-site heme iron (Cys) (axial ligand) 442 predicted 509 complete MWVLLVFFLLTLTYLFWPKTKGSGAKYPRSLPVLPVVGSLPFLPRRGHQHMNFFKLQDKY GPIFSFRLGSKTTVVIGDHQLAKEVLLKKGKEFSGRPRVMTLDILSDNQKGIAFADHGTS WQLHRKLALSTFSLFKGGNLKLENIINQEIKVLCDFLATRNGESIDLAQPLSLAMTNIVS FICFNFSFKKGDPALQAIVNFNDGILDAVGKEILYDMFPGIRILPSQTLENMKQCVRMRN ELLREILENRKENYSRNSITNLLDIMIQAKTNAESNTGGPDHNLKLLSDRHMLATVADIF GAGVETSASVVKWIVAFLLHYPLLRKKIQDAIDQNIGFNRAPSISDRNQLVLLEATIREV LRFRPVSPTLIPHRAIIDSSIGEFTIDKDTDVVVNLWALHHNEKEWLRPDLFMPERFLDP TGTQLISPSLSYLPFGAGPRSCVGEMLARQELFLFTAGLLQRFDLELPDDGQLPCLVGNP SLVLQIDPFKVKIKERQAWKEAHTEGSTS
S04346 S04346 A26289 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 precursor cytochrome P450(C17) bovine cattle Bos primigenius taurus Bhasker, C.R. Adler, B.S. Dee, A. John, M.E. Kagimoto, M. Zuber, M.X. Ahlgren, R. Wang, X. Simpson, E.R. Waterman, M.R. Arch. Biochem. Biophys. 2711989479-487 Structural characterization of the bovine CYP17 (17-alpha--hydroxylase) gene. MUID89271931 S04346 not compared with conceptual translation DNA 1-509 Zuber, M.X. John, M.E. Okamura, T. Simpson, E.R. Waterman, M.R. J. Biol. Chem. 26119862475-2482 Bovine adrenocortical cytochrome P-450-17-alpha. Regulation of gene expression by ACTH and elucidation of primary sequence. MUID86111956 A26289 mRNA 1-422,'T',424-457,'R',459-508,'P' GBM12547 NIDg162942 PIDNAAA30485.1 PIDg162943 CYP17 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain signal sequence 1-25 predicted product steroid 17alpha-monooxygenase cytochrome P450 17 26-509 predicted domain cytochrome P450 homology 299-464 binding-site heme iron (Cys) (axial ligand) 442 predicted 509 complete MWLLLAVFLLTLAYLFWPKTKHSGAKYPRSLPSLPLVGSLPFLPRRGQQHKNFFKLQEKY GPIYSFRLGSKTTVMIGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFADHGAH WQLHRKLALNAFALFKDGNLKLEKIINQEANVLCDFLATQHGEAIDLSEPLSLAVTNIIS FICFNFSFKNEDPALKAIQNVNDGILEVLSKEVLLDIFPVLKIFPSKAMEKMKGCVQTRN ELLNEILEKCQENFSSDSITNLLHILIQAKVNADNNNAGPDQDSKLLSNRHMLATIGDIF GAGVETTTSVIKWIVAYLLHHPSLKKRIQDDIDQIIGFNRTPTISDRNRLVLLEATIREV LRIRPVAPTLIPHKAVIDSSIGDLTIDKGTDVVVNLWALHHSEKEWQHPDLFMPERFLDP TGAQLISPSLSYLPFGAGPRSCVGEMLARQELFLFMSWLLQRFNLEIPDDGKLPSLEGHA SLVLQIKPFKVKIEVRQAWKEAQAEGSTS
A30828 A31359 S16719 S24316 A33980 A27659 D41425 I60207 A30828 S20655 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 cytochrome P450 17-alpha cytochrome P450 IF-5, hepatic steroid 17,20-lyase steroid 17alpha-hydroxylase rat Norway rat Rattus norvegicus Namiki, M. Kitamura, M. Buczko, E. Dufau, M.L. Biochem. Biophys. Res. Commun. 1571988705-712 Rat testis P-450-17-alpha cDNA: the deduced amino acid sequence, expression and secondary structural configuration. MUID89076306 A31359 mRNA 1-507 GBM22204 NIDg205921 PIDNAAA41783.1 PIDg205922 GBX14086 NIDg56051 PIDNCAA32248.1 PIDg56052 Fevold, H.R. Lorence, M.C. McCarthy, J.L. Trant, J.M. Kagimoto, M. Waterman, M.R. Mason, J.I. Mol. Endocrinol. 31989968-975 Rat P450(17-alpha) from testis: characterization of a full-length cDNA encoding a unique steroid hydroxylase capable of catalyzing both Delta(4)- and Delta(5)-steroid-17,20-lyase reactions. MUID89295447 S16719 preliminary mRNA 1-507 EMBLM31681 NIDg205909 PIDNAAA41777.1 PIDg205910 Zhang, P. Nason, T.F. Han, X.G. Hall, P.F. Biochim. Biophys. Acta 11311992345-348 Gene for 17-alpha-hydroxylase/C(17-20) lyase P-450: complete nucleotide sequence of the porcine gene and 5' upstream sequence of the rat gene. MUID92329554 S24316 DNA 1-97 EMBLZ11902 NIDg56031 PIDNCAA77954.1 PIDg56032 Mellon, S.H. Vaisse, C. Proc. Natl. Acad. Sci. U.S.A. 8619897775-7779 cAMP regulates P450scc gene expression by a cycloheximide-insensitive mechanism in cultured mouse Leydig MA-10 cells. MUID90046678 A33980 mRNA 273-507 GBM27282 NIDg205913 PIDNAAA41779.1 PIDg205914 Nishihara, M. Winters, C.A. Buzko, E. Waterman, M.R. Dufau, M.L. Biochem. Biophys. Res. Commun. 1541988151-158 Hormonal regulation of rat Leydig cell cytochrome P-450-17-alpha mRNA levels and characterization of a partial length rat P-450-17-alpha cDNA. MUID88280759 A27659 mRNA 271-507 GBM21208 NIDg203825 the authors translated the codon GAT for residues 288, 401, and 478 as Glu, Asn, and Asn respectively Imaoka, S. Kamataki, T. Funae, Y. J. Biochem. 1021987843-851 Purification and characterization of six cytochromes P-450 from hepatic microsomes of immature female rats. MUID88139237 D41425 protein 'XXXE',5-16 Givens, C.R. Zhang, P. Bair, S.R. Mellon, S.H. DNA Cell Biol. 1319941087-1098 Transcriptional regulation of rat cytochrome P450c17 expression in mouse Leydig MA-10 and adrenal Y-1 cells: identification of a single protein that mediates both basal and cAMP-induced activities. MUID95217329 I60207 preliminary translated from GB/EMBL/DDBJ DNA 1-507 EMBLX69816 NIDg619900 PIDNCAA49470.1 PIDg940818 CYP17 99/3; 145/1; 221/3; 250/3; 322/3; 379/2; 414/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron liver metalloprotein microsome monooxygenase oxidoreductase transmembrane protein domain transmembrane 2-21 predicted domain transmembrane 169-186 predicted domain cytochrome P450 homology 298-463 binding-site heme iron (Cys) (axial ligand) 441 predicted 507 complete MWELVGLLLLILAYFFWVKSKTPGAKLPRSLPSLPLVGSLPFLPRRGHMHVNFFKLQEKY GPIYSLRLGTTTTVIIGHYQLAREVLIKKGKEFSGRPQMVTQSLLSDQGKGVAFADAGSS WHLHRKLVFSTFSLFKDGQKLEKLICQEAKSLCDMMLAHDKESIDLSTPIFMSVTNIICA ICFNISYEKNDPKLTAIKTFTEGIVDATGDRNLVDIFPWLTIFPNKGLEVIKGYAKVRNE VLTGIFEKCREKFDSQSISSLTDILIQAKMNSDNNNSCEGRDPDVFSDRHILATVGDIFG AGIETTTTVLKWILAFLVHNPEVKKKIQKEIDQYVGFSRTPTFNDRSHLLMLEATIREVL RIRPVAPMLIPHKANVDSSIGEFTVPKDTHVVVNLWALHHDENEWDQPDQFMPERFLDPT GSHLITPTQSYLPFGAGPRSCIGEALARQELFVFTALLLQRFDLDVSDDKQLPRLEGDPK VVFLIDPFKVKITVRQAWMDAQAEVST
A39072 A39072 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 17alpha-monooxygenase (EC 1.14.99.9) cytochrome P450 17 mouse house mouse Mus musculus Youngblood, G.L. Sartorius, C. Taylor, B.A. Payne, A.H. Genomics 101991270-275 Isolation, characterization, and chromosomal mapping of mouse P450 17alpha-hydroxylase/C-17-20 lyase. MUID91257840 A39072 preliminary mRNA 1-507 GBM64863 NIDg200192 PIDNAAA39877.1 PIDg200193 the authors translated the codon AAG for residue 126 as Arg Cyp17 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 298-463 binding-site heme iron (Cys) (axial ligand) 441 predicted 507 complete MWELVGLLLLILAYFFWPKSKTPNAKFPRSLPFLPLVGSLPFLPRRGHMHANFFKLQEKY GPIYSLRLGTTTAVIVGHYQLAREVLVKKGKEFSGRPQMVTLGLLSDQGKGVAFADSSSS WQLHRKLVFSTFSLFRDDQKLEKMICQEANSLCDLILTYDGESRDLSTLIFKSVINIICT ICFNISFENKDPILTTIQTFTEGIVDVLGHSDLVDIFPWLKIFPNKNLEMIKEHTKIREK TLVEMFEKCKEKFNSESLSSLTDILIQAKMNAENNNTGEGQDPSVFSDKHILVTVGDIFG AGIETTSSVLNWILAFLVHNPEVKRKIQKEIDQYVGFSRTPSFNDRTHLLMLEATIREVL RIRPVAPLLIPHKANIDSSIGEFAIPKDTHVIINLWALHHDKNEWDQPDRFMPERFLDPT GSHLITPTPSYLPFGAGPRSCIGEALARQELFIFMALLLQRFDFDVSDDKQLPCLVGDPK VVFLIDPFKVKITVRQAWKDAQVEVST
O4HUC2 A25446 A00191 A27865 A32715 A21889 S26484 S29670 S29671 S26584 S29673 I55547 I59109 I58113 A29406 04-Dec-1986 08-Feb-1996 03-Mar-2000
steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21 cytochrome P450(C21B) steroid 21-hydroxylase cytochrome P450 21A2 human man Homo sapiens White, P.C. New, M.I. Dupont, B. Proc. Natl. Acad. Sci. U.S.A. 8319865111-5115 Structure of human steroid 21-hydroxylase genes. MUID86259742 A25446 DNA 1-494 GBM13936 NIDg187899 PIDNAAA59695.1 PIDg386910 Higashi, Y. Yoshioka, H. Yamane, M. Gotoh, O. Fujii-Kuriyama, Y. Proc. Natl. Acad. Sci. U.S.A. 8319862841-2845 Complete nucleotide sequence of two steroid 21-hydroxylase genes tandemly arranged in human chromosome: a pseudogene and a genuine gene. MUID86206051 A00191 mRNA 1-425,'P',427-494 Rodrigues, N.R. Dunham, I. Yu, C.Y. Carroll, M.C. Porter, R.R. Campbell, R.D. EMBO J. 619871653-1661 Molecular characterization of the HLA-linked steroid 21-hydroxylase B gene from an individual with congenital adrenal hyperplasia. MUID87275858 A27865 not compared with conceptual translation DNA 1-9,'L',10-101,'R',103-372,'S',373-494 Matteson, K.J. Phillips III, J.A. Miller, W.L. Chung, B. Orlando, P.J. Frisch, H. Ferrandez, A. Burr, I.M. Proc. Natl. Acad. Sci. U.S.A. 8419875858-5862 P450XXI (steroid 21-hydroxylase) gene deletions are not found in family studies of congenital adrenal hyperplasia. MUID87289701 A32715 mRNA 265-310,'L',312-345,'I',347-494 GBM17252 NIDg189446 PIDNAAA59985.1 PIDg386993 the authors translated the codon ATT for residue 346 as Asn Carroll, M.C. Campbell, R.D. Porter, R.R. Proc. Natl. Acad. Sci. U.S.A. 821985521-525 Mapping of steroid 21-hydroxylase genes adjacent to complement component C4 genes in HLA, the major histocompatibility complex in man. MUID85113228 A21889 DNA 149-171,'N',173-182 GBK02771 NIDg187928 PIDNAAA59706.1 PIDg443672 Helmberg, A. Kofler, R. submitted to the EMBL Data Library March1991 S26484 DNA 1-101,'R',103-371 EMBLX58904 NIDg30319 PIDNCAA41707.1 PIDg30320 S29670 DNA 1-9,'L',10-101,'R',103-338,'H',340-452,'S',454-492,'S',494 EMBLX58906 NIDg30321 PIDNCAA41709.1 PIDg30322 S29671 DNA 1-9,'L',10-101,'R',103-371 EMBLX58902 NIDg30325 PIDNCAA41706.1 PIDg30326 Helmberg, A. Tabarelli, M. Dobler, G. Kofler, R. submitted to the EMBL Data Library March1991 Identification of molecular defects causing congenital adrenal Hyperplasia by cloning of PCR-amplified 21-hydroxylase genes. S26584 DNA 1-171,'N',173-371 EMBLX58898 NIDg30316 PIDNCAA41702.1 PIDg30317 S29673 DNA 1-9,'L',10-101,'R',103-371 EMBLX58900 NIDg30328 PIDNCAA41704.1 PIDg30329 Globerman, H. Amor, M. Parker, K.L. New, M.I. White, P.C. J. Clin. Invest. 821988139-144 Nonsense mutation causing steroid 21-hydroxylase deficiency. MUID88273565 I55547 preliminary translated from GB/EMBL/DDBJ DNA 1-9,'L',10-280,'L',282-494 GBM21550 NIDg180960 PIDNAAA52063.1 PIDg180962 Amor, M. Parker, K.L. Globerman, H. New, M.I. White, P.C. Proc. Natl. Acad. Sci. U.S.A. 8519881600-1604 Mutation in the CYP21B gene (Ile-172----Asn) causes steroid 21-hydroxylase deficiency. MUID88144483 I59109 preliminary translated from GB/EMBL/DDBJ DNA 149-182 GBM19711 NIDg181289 PIDNAAA83248.1 PIDg181290 Collier, S. Tassabehji, M. Strachan, T. Nature Genet. 31993260-265 A de novo pathological point mutation at the 21-hydroxylase locus: implications for gene conversion in the human genome. MUID93251047 I58113 translated from GB/EMBL/DDBJ DNA 109-171,'N',173-185 GBS60612 NIDg300314 Deficiency of this enzyme (21-hydroxylase deficiency) causes about 90 % of cases of congenital adrenal hyperplasia, an inborn error of cortisol biosynthesis. GDBCYP21 GDBCYP21B GDB120605 OMIM201910 6p21.3-6p21.3 67/1; 97/1; 148/3; 182/3; 216/3; 245/3; 312/3; 372/2; 407/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 288-450 binding-site heme iron (Cys) (axial ligand) 428 predicted 494 complete MLLLGLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYR LHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSKNYPDLSLGDYSLLWKAHK KLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDK IKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQ LRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANTL SWAVVFLLHHPEIQQRLQEELDHELGPGASSSRVPYKDRARLPLLNATIAEVLRLRPVVP LALPHRTTRPSSISGYDIPEGTVIIPNLQGAHLDETVWERPHEFWPDRFLEPGKNSRALA FGCGARVCLGEPLARLELFVVLTRLLQAFTLLPSGDALPSLQPLPHCSVILKMQPFQVRL QPRGMGAHSPGQNQ
O4BOC2 A27555 A00192 A24101 C28860 A21181 28-May-1986 05-Apr-1995 03-Mar-2000
steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 cytochrome P450 (C21) steroid 21-hydroxylase bovine cattle Bos primigenius taurus Chung, B. Matteson, K.J. Miller, W.L. Proc. Natl. Acad. Sci. U.S.A. 8319864243-4247 Structure of a bovine gene for P-450c21 (steroid 21-hydroxylase) defines a novel cytochrome P-450 gene family. MUID86233409 A27555 DNA 1-496 GBM11267 NIDg163468 PIDNAAA83247.1 PIDg163469 Yoshioka, H. Morohashi, K. Sogawa, K. Yamane, M. Kominami, S. Takemori, S. Okada, Y. Omura, T. Fujii-Kuriyama, Y. J. Biol. Chem. 26119864106-4109 Structural analysis of cloned cDNA for mRNA of microsomal cytochrome P-450(C21) which catalyzes steroid 21-hydroxylation in bovine adrenal cortex. MUID86140226 A00192 mRNA 1-13,'S',15-400,'Y',402-496 GBM12918 NIDg162947 PIDNAAA30487.1 PIDg162948 adrenal cortex microsomes John, M.E. Okamura, T. Dee, A. Adler, B. John, M.C. White, P.C. Simpson, E.R. Waterman, M.R. Biochemistry 2519862846-2853 Bovine steroid 21-hydroxylase: regulation of biosynthesis. MUID86243279 A24101 mRNA 121-430,'C',432-496 GBK01333 NIDg162944 PIDNAAA30486.1 PIDg162945 Ogishima, T. Okada, Y. Kominami, S. Takemori, S. Omura, T. J. Biochem. 9419831711-1714 Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex. MUID84087829 C28860 protein 1-12,'K',14-15,248-250,'S' adrenal cortex microsomes White, P.C. New, M.I. Dupont, B. Proc. Natl. Acad. Sci. U.S.A. 8119841986-1990 Cloning and expression of cDNA encoding a bovine adrenal cytochrome P-450 specific for steroid 21-hydroxylation. MUID84193940 annotation sequence report this sequence differs substantially from that in reference A24101 68/1; 98/1; 149/3; 181/3; 215/3; 244/3; 311/3; 371/2; 406/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 287-449 binding-site heme iron (Cys) (axial ligand) 427 predicted 496 complete MVLAGLLLLLTLLAGAHLLWGRWKLRNLHLPPLVPGFLHLLQPNLPIHLLSLTQKLGPVY RLRLGLQEVVVLNSKRTIEEAMIRKWVDFAGRPQIPSYKLVSQRCQDISLGDYSLLWKAH KKLTRSALLLGTRSSMEPWVDQLTQEFCERMRVQAGAPVTIQKEFSLLTCSIICYLTFGN KEDTLVHAFHDCVQDLMKTWDHWSIQILDMVPFLRFFPNPGLWRLKQAIENRDHMVEKQL TRHKESMVAGQWRDMTDYMLQGVGRQRVEEGPGQLLEGHVHMSVVDLFIGGTETTASTLS WAVAFLLHHPEIQRRLQEELDRELGPGASCSRVTYKDRARLPLLNATIAEVLRLRPVVPL ALPHRTTRPSSIFGYDIPEGMVVIPNLQGAHLDETVWEQPHEFRPDRFLEPGANPSALAF GCGARVCLGESLARLELFVVLLRLLQAFTLLPPPVGALPSLQPDPYCGVNLKVQPFQVRL QPRGVEAGAWESASAQ
A43349 A43349 B43349 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 cytochrome P450(C21) sheep domestic sheep Ovis orientalis aries, Ovis ammon aries Crawford, R.J. Hammond, V.E. Connell, J.M. Coghlan, J.P. J. Biol. Chem. 267199216212-16218 The structure and activity of two cytochrome P450c21 proteins encoded in the ovine adrenal cortex. MUID92355577 A43349 mRNA 1-497 GBM92836 NIDg165851 adrenal cortex sequence extracted from NCBI backbone (NCBIN:110514, NCBIP:110515) B43349 mRNA 1-478,'D' GBM92837 NIDg165852 sequence extracted from NCBI backbone (NCBIN:111338, NCBIP:111339) human cytochrome P450 CYP2D6 cytochrome P450 homology alternative splicing chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 288-450 binding-site heme iron (Cys) (axial ligand) 428 predicted 497 complete MVLAGLLLLLLTLLAGAHLLWGRWKLRNLHLPPLVPGFLHLLQPNLPIHLLSLTQKLGPV YRLRLGLQEVVVLNSKRTIEEAMIRKWVDFAGRPQIPSYKLVSQRCQDISLGDYSLLWKA HKKLTRSALLLGTRSSMEPWVEQLTQEFCERMRVQAGAPVTIQKEFSLLTCSIICYLTFG DKEDTLVHAFHDCVQDLMKTWDHWSIQILDMVPFLRLFPNPGLWRLKKAIENRDHMVEKQ LRRHKESMVAGQWRDMMDYMLQGVGRQRVEEGPGQLLEGHVHMSVVDLFIGGTETKASTL SWAVAFLLHHPEIQRRLQEELDRELGPGASCSGVTYKDRARLPLLNATIAEVLRLRPVVP LALPHRTTRPSSIFGYDIPEGMVVIPNLQGAHLDETVWEQPHEFRPDRFLEPGANTSALA FGCGARVCLGESLARLELFVVLLRLLQAFTLLPPPGGALPSLQPDPYCGVNLKVQPFQVR LQPRGVEAGAWESTSAQ
A32525 S28169 A32525 A60677 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 cytochrome P450(C21) steroid 21-hydroxylase pig domestic pig Sus scrofa domestica Burghelle-Mayeur, C. Geffrotin, C. Vaiman, M. Biochim. Biophys. Acta 11711992153-161 Sequences of the swine 21-hydroxylase gene (CYP21) and a portion of the opposite-strand overlapping gene of unknown function previously described in human. MUID93129614 S28169 DNA 1-492 EMBLM83939 NIDg164559 PIDNAAA31080.1 PIDg164560 Haniu, M. Yanagibashi, K. Hall, P.F. Shively, J.E. Arch. Biochem. Biophys. 2541987380-384 Complete amino acid sequence of 21-hydroxylase cytochrome P-450 from porcine adrenal microsomes. MUID87212013 A32525 protein 1-9,'T',11-12,'K',14-54,'K',56-140,'C',142-200,'D',202-390,'I',392-462,'V',464,'Y',466-492 adrenal glands Geffrotin, C. Chardon, P. De Andres-Cara, D.F. Feil, R. Renard, C. Vaiman, M. Anim. Genet. 2119901-13 The swine steroid 21-hydroxylase gene (CYP21): cloning and mapping within the swine leucocyte antigen complex. MUID90233515 A60677 DNA 1-99 CYP21A1 68/1; 98/1; 149/3; 181/3; 215/3; 244/3; 311/3; 371/2; 406/1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein microsome monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 287-449 binding-site heme iron (Cys) (axial ligand) 427 predicted 492 complete MVLVWLLLLLTLLAGARLLWGQWKLRNLHLPPLVPGFLHLLQPNLPIYLLGLTQRLGPIY RLRLGLQDVVVLNSKRTIEEALVRKWVDFAGRPQIPSYKLASQHCPDISLGDYSLFWKAH KKLTRSALLLGVRSSMEPRVEQLTQEFCERMRAQAGTPVTIQKEFSVLTCSIICCLTFGD KEDTLVHALHDCVQDLMKTWEHWSIQILDMVPFLRFFPSPGLRRLKQAIENRDHLVEKQL RRHKESMVAGQWRDMLDYMLQEAGRQRVEEGQGQLLEGHVHMSVVDLFIGGTETTANTLS WAVVYLLHHPEIQWRLQEELDRELGPGAAGSRVPYKDRARLPLLNATIAEVLRLRPVVPL ALPHRATRPSSIFGYDIPEGTVVIPNLQGAHLDETVWEQPHEFRPDRFLAPGANPSALAF GCGARVCLGEPLARLELFVVLVQLLQAFTLLPPEGALPSLQPHPHSGINLKVQPFQVRLQ PRGGRGEGPGPR
A26660 A26660 A00193 10-Sep-1999 10-Sep-1999 03-Mar-2000
steroid 21-monooxygenase (EC 1.14.99.10) cytochrome P450 21A1 cytochrome P450(C21) steroid 21-hydroxylase mouse house mouse Mus musculus Chaplin, D.D. Galbraith, L.J. Seidman, J.G. White, P.C. Parker, K.L. Proc. Natl. Acad. Sci. U.S.A. 8319869601-9605 Nucleotide sequence analysis of murine 21-hydroxylase genes: mutations affecting gene expression. MUID87092295 A26660 DNA 1-487 GBM15009 the authors translated the codon CGC for residue 63 as His, TTC for residue 163 as Pro, AAG for residue 177 as Leu, GAC for residue 178 as Asn, CGG for residue 270 as Gln, and GCC for residue 314 as Glu Amor, M. Tosi, M. Duponchel, C. Steinmetz, M. Meo, T. Proc. Natl. Acad. Sci. U.S.A. 8219854453-4457 Liver mRNA probes disclose two cytochrome P-450 genes duplicated in tandem with the complement C4 loci of the mouse H-2S region. MUID85242702 A00193 DNA 'RPLLGQTSLALHLLPT',399-487 GBK03234 NIDg199331 this translation includes a region likely to represent an intron Cyp21 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 283-442 binding-site heme iron (Cys) (axial ligand) 420 predicted 487 complete MLLPGLLLLLLLLAGTRWLWGQWKLRKLHLPRLAPGFLHFLQPNLPIYLLGLTQKLGPIY RIRLGMQDVVVLNSNRTIEEALIQKWVDFAGRPHMLNGKMDLDLSLGDYSLMWKAHKKLS RSALMLGMRDSMEPLIEQLTQEFCERMRAQAGTPVAIHKEFSFLTCSIISCLTFGDNDST LVQTLHDCVQDLLQAWNHWSIQILTIIPLLRFLPNPGLQKLKQIQESRDHIVKQQLKQHK ESLVAGQWKDMIDYMLQGVEKQRDGKDEERLHEGHVHMSVVDLFIGGTETTATTLSWAVA FLLHHPEIQKRLQAELDLKLGPGSQLLYRNRMQLPLLMATIAEVLRLRPVVPLALPHRAT RASSISGYDIPKDMVIIPNIQGANLDEMVWELPSKFWPDRFLEPGKNPRTPSFGCGARVC LGEPLARLELFVVLARLLQAFTLLPPPDGTLPSLQPQPYAGINLPIPPFQVRLQPRNLAP QDQGERP
S36878 S36878 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 oxidoreductase (EC 1.-.-.-) alfalfa alfalfa Medicago sativa Fahrendorf, T. Dixon, R.A. Arch. Biochem. Biophys. 3051993509-515 Stress responses in alfalfa (Medicago sativa L.). XVIII: Molecular cloning and expression of the elicitor-inducible cinnamic acid 4-hydroxylase cytochrome P450. MUID93384309 S36878 preliminary mRNA 1-506 EMBLL11046 CYP73A3 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 304-470 binding-site heme iron (Cys) (axial ligand) 448 predicted 506 complete MDLLLLEKTLLALFIAATIAVTISKLRGKRFKLPPGPIPVPIFGYWLQVGDDLNHRNLTD YAKRFGEIFLLRMGQRNLVVVSSPELAKEVLHTQCVEFGSRTRNVVFDIFTGKGQDMVFT VYGEHWRKMRRIMTVPFFTNKVVQQYRYGWESEAESVVNDVKNNAEASVGGIVIRKRLQL MMYNIMYRIMFDRRFESEEDPLFVKLKALNGERSRLAQSFEYNYGDFIPILRPFLKGYLK VCKEVKDRRLQLFKDYFVDERKKLESTKSTTSNDGLKCAIDHILDAQKKGEINDDNVLYI VENINVAAIETTLWSIEWGIAELVNHQDIQNKVREEMDRVLGPGHQVTEPDLHKLPYLQA VIKETLRLRMAIPLLVPHMNLHDPKLNGFDIPAESKILVNAWWLPNNPAHWKKPEEFRPE RFLEEESHVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNVELLPPPGQSKI DTSEKGGQFSLHILKHSTIVAKPRSF
A35867 A35867 A44973 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 71A1 oxidoreductase (EC 1.-.-.-) avocado avocado Persea americana Bozak, K.R. Yu, H. Sirevag, R. Christoffersen, R.E. Proc. Natl. Acad. Sci. U.S.A. 8719903904-3908 Sequence analysis of ripening-related cytochrome P-450 cDNAs from avocado fruit. MUID90251665 A35867 mRNA 1-471 GBM32885 O'Keefe, D.P. Leto, K.J. Plant Physiol. 8919891141-1149 Cytochrome P-450 from the mesocarp of avocado (Persea americana). A44973 protein 1-40 a second sequence was identical except for the lack of the lack of Met-1 CYP71A1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 301-465 binding-site heme iron (Cys) (axial ligand) 443 predicted 471 complete MAILVSLLFLAIALTFFLLKLNEKREKKPNLPPSPPNLPIIGNLHQLGNLPHRSLRSLAN ELGPLILLHLGHIPTLIVSTAEIAEEILKTHDLIFASRPSTTAARRIFYDCTDVAFSPYG EYWRQVRKICVLELLSIKRVNSYRSIREEEVGLMMERISQSCSTGEAVNLSELLLLLSSG TITRVAFGKKYEGEEERKNKFADLATELTTLMGAFFVGDYFPSFAWVDVLTGMDARLKRN HGELDAFVDHVIDDHLLSRKANGSDGVEQKDLVDVLLHLQKDSSLGVHLNRNNLKAVILD MFSGGTDTTAVTLEWAMAELIKHPDVMEKAQQEVRRVVGKKAKVEEEDLHQLHYLKLIIK ETLRLHPVAPLLVPRESTRDVVIRGYHIPAKTRVFINAWAIGRDPKSWENAEEFLPERFV NNSVDFKGQDFQLIPFGAGRRGCPGIAFGISSVEISLANLLYWFNWELPGI
S36805 S36805 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 71A4 oxidoreductase (EC 1.-.-.-) eggplant eggplant, aubergine Solanum melongena Umemoto, N. Kobayashi, O. Ishizaki-Nishizawa, O. Toguri, T. FEBS Lett. 3301993169-173 cDNAs sequences encoding cytochrome P450 (CYP71 family) from eggplant seedlings. MUID93374057 S36805 preliminary mRNA 1-507 EMBLX70981 NIDg402223 PIDNCAA50312.1 PIDg402224 CYP71A4 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 305-470 binding-site heme iron (Cys) (axial ligand) 448 predicted 507 complete MDVPCLWYSLLILLLLFIFLLIHHCFTTSKTQNMFLPPSPRKLPIIGNLHQLGSHPHRSL RKLSQKYGPVMLLHLGSKPVIVASSVDAARDILKTHDHVWATRPKYSIADSLLYGSKDVG FSPFGEYWWQVRSIVVLHLLSNKRVQSYRDVREEETANMIEKIRQGCDASVINLGEHLCF LTNNITSRVALGRTYDERESGIDAKDILEQFLQLLDTFNVGDYIPWLKWVNKITGLDTKV EKIAKKLDTFLDSVIEEHIIRNKKEEYAITDEAKDFVDVLLEIQNGKETDFPLQRDSLKA ILLDAFAAGTDTIYTNLDWTMADVLRQPRAMKTLQNEVRGLAQGKSEITEDDLKNMQYLR AVIKESLRLHPPNSLLVPRESMEDVKLLGYYHIPARTQALINVWAIGRDPLSWENPEEFC PERFLNNDIDMKGLKFELLPFGSGRRGCPGSSFAIAVIELALARLVHKFNFALPKGTKPE DLDMTECTGIATRRKSPLPVVATPFSG
S45039 S45039 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 oxidoreductase (EC 1.-.-.-) Mentha piperita (peppermint) peppermint Mentha piperita Kang, M.H. Choi, Y.D. submitted to the EMBL Data Library May1994 Molecular cloning of a genomic DNA for cytochrome P-450 oxidase from Mentha piperita. S45039 DNA 1-502 EMBLZ33875 NIDg493474 PIDNCAA83941.1 PIDg493475 303/3 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 305-469 binding-site heme iron (Cys) (axial ligand) 447 predicted 502 complete MYSIAFMLVLRKMDEIISHTLAFQALVSLILLISITKWLSNSPKNKNSSPPSPRKLPILG NLLQLGSLPHHNLRSMARKHGPIMLLHLGSVRPVSSRRRPRGNHENSRSRLRRPRGSRSA ALQLQGRVGGYGEYWRQLKTICVVQLLSNKRVQSFRSVREEETELLMKKIGDSSGNVNLS HMFTQLTNDVVCRSAIGRKYGAGDENGEKFLEILREFLELLGAISIGDFVPSLWWINRIN GFDRRVDRIAKEMDEFLEKVIHERLENPAAKAEENFVDILLEIYRNNSAGVSIDRDSIKA IILDVFAAGTDTTAVVLEWAMTELLRHPEIMKKLQSEVRQVVKDKHNITDDDIEKMHYLK AVMKETMRFHTPIPLLVPRVARNDVEVMGYDVPVGTMVMINAWAIGRDPTSWDEPEKFRP ERFLNSSVDFKGLDFELIPFGAGRRGCPGTTFPMATLEFTLANLMQKFDWELPHECRELD MSERPGVAIRRVIPLLAIGTKM
S62899 S62899 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 (CYP93 A1) oxidoreductase (EC 1.-.-.-) soybean soybean Glycine max Suzuki, G. Ohta, H. Kato, T. Igarashi, T. Sakai, F. Shibata, D. Takano, A. Masuda, T. Shioi, Y. Takamiya, K. FEBS Lett. 383199683-86 Induction of a novel cytochrome P450 (CYP93 family) by methyl jasmonate in soybean suspension-cultured cells. MUID96184393 S62899 preliminary not compared with conceptual translation mRNA 1-509 GBD83968 NIDg1435059 PIDNBAA12159.1 PIDg1232111 cyp93A1 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 303-469 binding-site heme iron (Cys) (axial ligand) 447 predicted 509 complete MAYQVLLICLVSTIVFAYILWRKQSKKNLPPSPKALPIIGHLHLVSPIPHQDFYKLSTRH GPIMQLFLGSVPCVVASTAEAAKEFLKTHEINFSNRPGQNVAVKGLAYDSQDFLFAFAPF GPYWKFMKKLCMSELLSGRMMDQFLPVRQQETKRFISRVFRKGVAGEAVDFGDELMTLSN NIVSRMTLSQKTSENDNQAEEMKKLVSNIAELMGKFNVSDFIWYLKPFDLQGFNRKIKET RDRFDVVVDGIIKQRQEERRKNKETGTAKQFKDMLDVLLDMHEDENAEIKLDKKNIKAFI MDIFVAGTDTSAVSIEWAMAELINNPDVLEKARQEIDAVVGKSRMVEESDIANLPYLQAI VRETLRLHPGGPLVVRESSKSAVVCGYDIPAKTRLFVNVWAIGRDPNHWEKPFEFRPERF IRDGQNQLDVRGQHYHFIPFGSGRRTCPGASLAWQVVPVNLAIIIQCFQWKLVGGNGKVD MEEKSGITLPRANPIICVPVPRINPFPTI
A71418 A71418 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 d13725w oxidoreductase (EC 1.-.-.-) Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana columbia Bevan, M. Bancroft, I. Bent, E. Love, K. Goodman, H. Dean, C. Bergkamp, R. Dirkse, W. Van Staveren, M. Stiekema, W. Drost, L. Ridley, P. Hudson, S.A. Patel, K. Murphy, G. Piffanelli, P. Wedler, H. Wedler, E. Wambutt, R. Weitzenegger, T. Pohl, T.M. Terryn, N. Gielen, J. Villarroel, R. De Clerck, R. Van Montagu, M. Lecharny, A. Auborg, S. Gy, I. Kreis, M. Lao, N. Kavanagh, T. Hempel, S. Kotter, P. Entian, K.D. Rieger, M. Schaeffer, M. Funk, B. Mueller-Auer, S. Silvey, M. James, R. Montfort, A. Pons, A. Puigdomenech, P. Douka, A. Voukelatou, E. Milioni, D. Hatzopoulos, P. Piravandi, E. Obermaier, B. Hilbert, H. Duesterhoft, A. Moores, T. Jones, J.D.G. Eneva, T. Palme, K. Benes, V. Rechman, S. Ansorge, W. Cooke, R. Berger, C. Delseny, M. Voet, M. Volckaert, G. Mewes, H.W. Klosterman, S. Schueller, C. Chalwatzis, N. Nature 3911998485-488 Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. MUID98121113 A71418 preliminary nucleic acid sequence not shown translation not shown DNA 1-527 GBZ97338 NIDg2244870 PIDNCAB10315.1 PIDg2244893 d13725w 4COP9-4G3845 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 308-473 binding-site heme iron (Cys) (axial ligand) 451 predicted 527 complete MIAIIVEFQNFFIFILLCLFSLLCHSLFFKKPKDSRSFVLPSSPPSLPIIGHLHLLLSVL THKSLQKLSSKYGPLLLIRIFYVPIILVSSSSMAYEIFKAHDVNVSSRGIIALDESLMFG ASGILNAPYGDYWKFMKKLMATKLLRPQVLERSRGVRVEELHRFYRSILDKATKNESVEI GKEAMKLMNNTLCKLIMGRSFSEDNGESNRVRGLVDETYALSEKIFLAAILRRPLAKLRI SLFKKEIMGVSNKFDELLERILQERKENLEEKNNEGMDMMDVLLEAYGDENAEYKITWKH IKAFFVEFFIGGTDTSVQTTQWAMAEMINNANVLERLREEIVSVVGETRLIQETDLPNLP YLQAVVKEVLRLHPPSPVLIRKFQEKCEVKGFYIPEKTTLIVNVYAIMRDSDSWEDPEKF KPERFLTSSRSGEEDEKELKFLPFGSGRRGCPGANLGSIFVGTAIGVMVQCFDWKIKEDK VNMEETFEGMTLKMVHPLTCTPFFEPNLYLLLLISKFPCLILSFGAC
S38534 S38534 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 76A2 oxidoreductase (EC 1.-.-.-) eggplant eggplant, aubergine Solanum melongena Toguri, T. Kobayashi, O. Umemoto, N. Biochim. Biophys. Acta 12161993165-169 The cloning of eggplant seedling cDNAs encoding proteins from a novel cytochrome P-450 family (CYP76). MUID94032483 S38534 preliminary mRNA 1-505 EMBLX71657 NIDg415910 PIDNCAA50648.1 PIDg415911 CYP76A2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 306-470 binding-site heme iron (Cys) (axial ligand) 448 predicted 505 complete MEWEWSYVFFSAIIILPAFILFFSQKNTTKSSYKFPPGPPGLPIFGNMFELGTEPYKKMA VLRQKYGPVLWLKLGSTYTMVVQTAQASEELFKNHDISFANRVIPDVNQAHSYYQGSLAI APYGPFWRFQRRICTIEMFVHKKISETEPVRRKCVDNMLKWIEKEANSAEKGSGIEVTRF VFLASFNMLGNLILSKDLADLESEEASEFFIAMKRINEWSGIANVSDIFPFLKKFDLQSL RKKMARDMGKAVEIMSMFLKEREEERKKGTEKGKDFLDVLLEFQGTGKDEPAKLSEHEIK IFVLEMFLAGTETTSSSVEWALTELLRHPEAMAKVKTEISQAIEPNRKFEDSDIENLPYM QAVLKESLRLHPPLPFLIPRETIQDTKFMGYDVPKDTQVLVNAWAIGRDPECWDDPMSFK PERFLGSKIDVKGQHYGLIPFGAGRRMCVGLPLGHRMMHFALGSLLREFEWELPDGVSPK SINMDGSMGVTARKRDSLKVIPKKA
S43342 S43342 10-Sep-1999 10-Sep-1999 03-Mar-2000
flavonoid 3',5'-hydroxylase (EC 1.14.-.-) cytochrome P450 eggplant eggplant, aubergine Solanum melongena Toguri, T. Umemoto, N. Kobayashi, O. Ohtani, T. Plant Mol. Biol. 231993933-946 Activation of anthocyanin synthesis genes by white light in eggplant hypocotyl tissues, and identification of an inducible P-450 cDNA. MUID94083564 S43342 preliminary mRNA 1-513 EMBLX70824 NIDg395260 PIDNCAA50155.1 PIDg395261 CYP75A2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 301-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 513 complete MVILPSELIGATIIYIIVYIIIQKLIATGSWRRRRLPPGPEGWPVIGALPLLGGMPHVAL AKMAKKYGPIMYLKVGTCGMVVASTPNAAKAFLKTLDINFSNRPPNAGATHMAYNAQDMV FAPYGPRWKLLRKLSNLHMLGGKALENWANVRANELGHMLKSMFDASHVGERIVVADMLT FAMANMIGQVMLSKRVFVEKGKEVNEFKNMVVELMTVAGYFNIGDFIPQIAWMDLQGIEK GMKKLHKKFDDLLTKMFEEHEATSNERKGKPDFLDFIMANRDNSEGERLSITNIKALLLN LFTAGTDTSSSVIEWALTEMMKNPTIFKKAQQEMDQIIGKNRRFIESDIPNLPYLRAICK EAFRKHPSTPLNLPRVSSDACTIDGYYIPKNTRLSVNIWAIGRDPDVWENPLEFIPERFL SEKNAKIEHRGNDFELIPFGAGRRICAGTRMGIVMVEYILGTLIHSFDWKLPNDVVDINM EETFGLALQKAVPLEAIVTPRLSFDIYQSSEPF
S41598 S41598 S40266 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 77A2 oxidoreductase (EC 1.-.-.-) eggplant eggplant, aubergine Solanum melongena Toguri, T. Tokugawa, K. FEBS Lett. 3381994290-294 Cloning of eggplant hypocotyl cDNAs encoding cytochromes P450 belonging to a novel family (CYP77). MUID94139942 S41598 mRNA 1-511 EMBLX71655 NIDg438240 PIDNCAA50646.1 PIDg438241 clone cyp77A2 CYP77A2 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 312-478 binding-site heme iron (Cys) (axial ligand) 456 predicted 511 complete MDFFSTSSLSSYYHLIFTILAFVISSIIYFLSKKAESKKLKLPPGPPGWPVVGNLLQVAR SGKPFFQIMRELRQKYGPIFTLRMGTRTMIILSNADLVHEALILKGQVFATRPRENPTRT VFSCDKFTVNAAVYGPVWRSLRKNMVQNGLSSIRLKEFRAVRKSAMDKMIEKIRAEADAN EGVVWVLKNARFAVFCILLAMCFGVEMDEKTIEKIDQMMKSVLIALDPRLDDYLPILSPF FSKQRKHAMDVRKQQIKTIVPFIEQRKKILESPEIDKTAASFSYLDTLFDLKIEGRNSTP TYPELVTLCSEFLNGGTDTTATAIEWAIGRLIENPNIQSQLYEEIKKTVGENKIDEKDIE KMPYLNAVVKELLRKHPPTYMSLTHAVTEPAKLGGYDIPTGVNVEIFLPGISDDPNLWSE PEKFDPDRFYLGKEDADITGVSGVKMIPFGMGRRICPGLNMATVHVSLMLARLVQEFEWA DPENTRVDFTEKLEFTVVMKNTLRAKIKPRM
S68203 S68203 10-Sep-1999 10-Sep-1999 03-Mar-2000
tyrosine N-monooxygenase (EC 1.14.13.41) cytochrome P450tyr tyrosine N-hydroxylase sorghum sorghum Sorghum bicolor Koch, B.M. Sibbesen, O. Halkier, B.A. Svendsen, I. Moller, B.L. Arch. Biochem. Biophys. 3231995177-186 The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. MUID96019962 S68203 preliminary mRNA 1-558 EMBLU32624 NIDg984542 PIDNAAA85440.1 PIDg984543 CYP79 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 348-515 binding-site heme iron (Cys) (axial ligand) 493 predicted 558 complete MATMEVEAAAATVLAAPLLSSSAILKLLLFVVTLSYLARALRRPRKSTTKCSSTTCASPP AGVGNPPLPPGPVPWPVVGNLPEMLLNKPAFRWIHQMMREMGTDIACVKLGGVHVVSITC PEIAREVLRKQDANFISRPLTFASETFSGGYRNAVLSPYGDQWKKMRRVLTSEIICPSRH AWLHDKRTDEADNLTRYVYNLATKAATGDVAVDVRHVARHYCGNVIRRLMFNRRYFGEPQ ADGGPGPMEVLHMDAVFTSLGLLYAFCVSDYLPWLRGLDLDGHEKIVKEANVAVNRLHDT VIDDRWRQWKSGERQEMEDFLDVLITLKDAQGNPLLTIEEVKAQSQDITFAAVDNPSNAV EWALAEMVNNPEVMAKAMEELDRVVGRERLVQESDIPKLNYVKACIREAFRLHPVAPFNV PHVALADTTIAGYRVPKGSHVILSRTGLGRNPRVWDEPLRFYPDRHLATAASDVALTEND LRFISFSTGRRGCIAASLGTAMSVMLFGRLLQGFTWSKPAGVEAVDLSESKSDTFMATPL VLHAEPRLPAHLYPSISI
S51475 S51475 S46317 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 cyp78 maize maize Zea mays Larkin, J.C. submitted to the EMBL Data Library August1993 Isolation of a cytochrome P450 homologue preferentially expressed in developing inflorescences of Zea mays L. S51475 preliminary mRNA 1-547 EMBLL23209 NIDg349717 PIDNAAA61607.1 PIDg349718 Larkin, J.C. Plant Mol. Biol. 251994343-353 Isolation of a cytochrome P450 homologue preferentially expressed in developing inflorescences of Zea mays. MUID94325460 S46317 preliminary mRNA 1-174,'N',176-547 EMBLL23209 NIDg349717 cyp78 human cytochrome P450 CYP2D6 cytochrome P450 homology chromoprotein heme iron metalloprotein domain cytochrome P450 homology 342-512 binding-site heme iron (Cys) (axial ligand) 490 predicted 547 complete MAMASAACSCTDGTWWVYALPALLGSDTLCAHPALLAGLIFLATVSVALLAWATSPGGPA WTNGRGASASLLSWDPVVCPCSAASSRCPGAAAPRPRRDGPRRRPRAKELMAFSVGDTPA VVSSCPATAREVLAHPSFADRPVKRSARELMFARAIGFAPNGEYWRRLRRVASTHLFSPR RVASHEPGRQGDAEAMLRSIAAEQSASGAVALRPHLQAAALNNIMGSVFGTRYDVTSGAG AAEAEHLKSMVREGFELLGAFNWSDHLPWLAHLYDPSNVTRRCAALVPRVQTFVRGVIDE HRRRRQNSAALNDNADFVDVLLSLEGDEKLGDDDMVAILWEMVFRGTDTTALLTEWCMAE LVRHPAVQARVRAEVDAAVGAGGCPTDADVARMPYLQAVVKETLRAHPPGPLLSWARLAT ADVPLCNGMVVPAGTTAMVNMWAITHDAAVWADPDAFAPERFLPSEGGADVDVRGVDLRL APFGAGRRVCPGKNLGLTTVGLWVARLVHAFQWALPDGAAAVCLDEVLKLSLEMKTPLVA AAIPRTA
S11338 S11338 S29068 A34181 B40223 10-Sep-1999 10-Sep-1999 21-Jul-2000
steroid 11beta-monooxygenase (EC 1.14.15.4) cytochrome P450 11B1 precursor cytochrome P450(11beta) steroid 11beta-hydroxylase human man Homo sapiens Kawamoto, T. Mitsuuchi, Y. Toda, K. Miyahara, K. Yokoyama, Y. Nakao, K. Hosoda, K. Yamamoto, Y. Imura, H. Shizuta, Y. FEBS Lett. 2691990345-349 Cloning of cDNA and genomic DNA for human cytochrome P-450(11-beta). MUID90382577 S11338 mRNA 1-503 EMBLX55764 NIDg30183 PIDNCAA39290.1 PIDg30184 S29068 DNA 1-30 EMBLX55765 NIDg30362 PIDNCAA39291.1 PIDg30363 Mornet, E. Dupont, J. Vitek, A. White, P.C. J. Biol. Chem. 264198920961-20967 Characterization of two genes encoding human steroid 11beta-hydroxylase (P-450-11beta). MUID90078185 A34181 DNA 1-42,'R',44-373,375-385,'A',387-431,'K',433-457,'V',459-493,'C',495-503 GBM32863 GBM32878 GBM32879 GBJ05140 Kawamoto, T. Mitsuuchi, Y. Toda, K. Yokoyama, Y. Miyahara, K. Miura, S. Ohnishi, T. Ichikawa, Y. Nakao, K. Imura, H. Ulick, S. Shizuta, Y. Proc. Natl. Acad. Sci. U.S.A. 8919921458-1462 Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the biosynthesis of glucocorticoids and mineralocorticoids in humans. MUID92159068 B40223 DNA 1-30 GBD10169 GBD90428 NIDg219561 PIDNBAA01039.1 PIDg219562 sequence extracted from NCBI backbone (NCBIN:82634, NCBIP:82638) GDBCYP11B1 GDBCYP11B GDB120603 OMIM202010 8q21-8q22 80/2; 132/2; 198/3; 266/3; 318/3; 373/3; 400/3; 466/3 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain transit peptide (mitochondrion) 1-24 predicted product steroid 11beta-monooxygenase 25-503 predicted domain cytochrome P450 homology 311-472 binding-site heme iron (Cys) (axial ligand) 450 predicted 503 complete MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPQRPGNRWLRLLQIWREQG YEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYR QHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNA RGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFM PRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELS PDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATT ELPLLRAALKETLRLYPVGLFLERVVSSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRP ERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQED IKMVYSFILRPSMFPLLTFRAIN
O4BOM A00189 S15865 A24067 A42033 A28860 S29644 S04947 27-Nov-1985 27-Nov-1985 03-Mar-2000
cholesterol monooxygenase (side-chain-cleaving) (EC 1.14.15.6) cytochrome P450 11A1 precursor, mitochondrial cytochrome P450(SCC) bovine cattle Bos primigenius taurus Morohashi, K. Fujii-Kuriyama, Y. Okada, Y. Sogawa, K. Hirose, T. Inayama, S. Omura, T. Proc. Natl. Acad. Sci. U.S.A. 8119844647-4651 Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex. MUID84272690 A00189 DNA 1-520 GBK02130 NIDg162950 PIDNAAA30488.1 PIDg162951 Ahlgren, R. Simpson, E.R. Waterman, M.R. Lund, J. J. Biol. Chem. 26519903313-3319 Characterization of the promoter/regulatory region of the bovine CYP11A (P-450(scc)) gene. Basal and cAMP-dependent expression. MUID90153984 S15865 DNA 1-21,'S',23-90 EMBLJ05245 Chashchin, V.L. Lapko, V.N. Adamovich, T.B. Lapko, A.G. Kuprina, N.S. Akhrem, A.A. Biochim. Biophys. Acta 8711986217-223 Primary structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria and some aspects of its functioning on a structural level. MUID86216225 A24067 protein 40-56,'D',58-105,'N',107-196,'N',198-520 Pikuleva, I.A. Lapko, A.G. Chashchin, V.L. J. Biol. Chem. 26719921438-1442 Functional reconstitution of cytochrome P-450-scc with hemin activated with Woodward's reagent K. Formation of a hemeprotein cross-link. MUID92112852 A42033 protein 216-233 Ogishima, T. Okada, Y. Kominami, S. Takemori, S. Omura, T. J. Biochem. 9419831711-1714 Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex. MUID84087829 A28860 protein 40-54 Tsujita, M. Ichikawa, Y. Biochim. Biophys. Acta 11611993124-130 Substrate-binding region of cytochrome P-450(scc) (P-450 XIA1). Identification and primary structure of the cholesterol binding region in cytochrome P-450(scc). MUID93160229 S29644 protein 47-67 Adamovich, T.B. Pikuleva, I.A. Chashchin, V.L. Usanov, S.A. Biochim. Biophys. Acta 9961989247-253 Selective chemical modification of cytochrome P-450(SCC) lysine residues. Identification of lysines involved in the interaction with adrenodoxin. MUID89323202 S04947 protein 112-117;142-161;183-194;306-309;377-384 This cytochrome P450 catalyzes the side-chain cleavage reaction of cholesterol in bovine adrenal cortex mitochondria. human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain transit peptide (mitochondrion) 1-39 predicted product cholesterol monooxygenase (side-chain-cleaving) cytochrome P450 11A1, mitochondrial 40-520 experimental region substrate binding 47-67 domain cytochrome P450 homology 322-483 binding-site heme iron (Cys) (axial ligand) 461 predicted 520 complete MLARGLPLRSALVKACPPILSTVGEGWGHHRVGTGEGAGISTKTPRPYSEIPSPGDNGWL NLYHFWREKGSQRIHFRHIENFQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPER YDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAPEAIKNFIPLLNPVSQDFVS LLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKM FHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGI LYCLLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARR QAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYA MGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILE NFKVEMQHIGDVDTIFNLILTPDKPIFLVFRPFNQDPPQA
S03188 S03188 PN0018 A54723 A30825 10-Sep-1999 10-Sep-1999 03-Mar-2000
cholesterol monooxygenase (side-chain-cleaving) (EC 1.14.15.6) cytochrome P450 11A1 precursor, mitochondrial cytochrome P450(SCC) pig domestic pig Sus scrofa domestica Mulheron, G.W. Stone, R.T. Miller, W.L. Wise, T. Nucleic Acids Res. 1719891773 Nucleotide sequence of cytochrome P-450 cholesterol side-chain cleavage cDNA isolated from porcine testis. MUID89160344 S03188 translation not shown mRNA 1-520 EMBLX13768 NIDg2024 PIDNCAA32018.1 PIDg2025 Kuwada, M. Kitajima, R. Suzuki, H. Horie, S. Biochem. Biophys. Res. Commun. 17619911501-1508 Purification and properties of cytochrome P-450(SCC) from pig testis mitochondria. MUID91248248 PN0018 protein 41-58,'X',60-61 testis mitochondria Iwahashi, K. Tsubaki, M. Miyatake, A. Ichikawa, Y. Int. J. Biochem. 231991901-909 Purification and comparative characterization of cytochrome P-450scc from porcine adrenocortical mitochondria. MUID92128625 A54723 protein 40-45,'F',47-64 sequence extracted from NCBI backbone (NCBIP:79244) This protein catalyzes the conversion of cholesterol to pregnenolone. CYP11A1 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain transit peptide (mitochondrion) 1-40 predicted product cholesterol monooxygenase (side-chain-cleaving) 41-520 experimental domain cytochrome P450 homology 322-483 region steroid binding 369-392 predicted binding-site heme iron (Cys) (axial ligand) 461 predicted 520 complete MLARGLALRSVLVKGCQPFLSAPRECPGHPRVGTGEGACISTKTPRPFSEIPSPGDNGWI NLYRFWKEKGTQKIHYHHVQNFQKYGPIYREKLGNLESVYIIDPEDVALLFKFEGPNPER YNIPPWVAYHQHYQKPVGVLLKKSGAWKKDRLVLNTEVMAPEAIKNFIPLLDTVSQDFVG VLHRRIKQQGSGKFSGDIREDLFRFAFESITNVIFGERLGMLEEIVDPEAQKFIDAVYQM FHTSVPMLNLPPDLFRLFRTKTWRDHVAAWDTIFNKAEKYTQNFYWDLRRKREFNNYPGI LYRLLGNDKLLSEDVKANVTEMLAGGVDTTSMTLQWHLYEMARSLNVQEMLREEVLNARR QAQGDTSKMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAVYA MGRDPAFFSNPGQFDPTRWLGKERDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILE NFKVELQHFSDVDTIFNLILMPDKPIFLVFRPFNQDPLQA
A34164 A34164 A27321 A23688 10-Sep-1999 10-Sep-1999 03-Mar-2000
cholesterol monooxygenase (side-chain-cleaving) (EC 1.14.15.6) cytochrome P450 11A1 precursor, mitochondrial cytochrome P450 SCC rat Norway rat Rattus norvegicus Oonk, R.B. Krasnow, J.S. Beattie, W.G. Richards, J.S. J. Biol. Chem. 264198921934-21942 Cyclic AMP-dependent and -independent regulation of cholesterol side chain cleavage cytochrome P-450 (P-450-scc) in rat ovarian granulosa cells and corpora lutea. cDNA and deduced amino acid sequence of rat P-450-scc. MUID90094378 A34164 mRNA 1-526 GBJ05156 NIDg203638 PIDNAAA40989.1 PIDg203639 McMasters, K.M. Dickson, L.A. Shamy, R.V. Robischon, K. Macdonald, G.J. Moyle, W.R. Gene 5719871-9 Rat cholesterol side-chain cleavage enzyme (P-450scc): use of a cDNA probe to study the hormonal regulation of P-450scc mRNA levels in ovarian granulosa cells. MUID88112851 A27321 not compared with conceptual translation mRNA 344-526 GBM22615 NIDg666941 PIDNAAA62267.1 PIDg666942 Oonk, R.B. Parker, K.L. Gibson, J.L. Richards, J.S. J. Biol. Chem. 265199022392-22401 Rat cholesterol side-chain cleavage cytochrome P-450 (P-450-SCC) gene. Structure and regulation by cAMP in vitro. MUID91093084 A23688 preliminary DNA 1-526 GBM63133 NIDg203559 PIDNAAA40958.1 PIDg203561 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 320-481 binding-site heme iron (Cys) (axial ligand) 459 predicted 526 complete MLAKGLCLRSVLVKSCQPFLSPVWQGPGLATGNGAGISSTNSPRSFNEIPSPGDNGWINL YHFLRENGTHRIHYHHMQNFQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYL VPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAPDSIKNFVPLLEGVAQDFIKVL HRRIKQQNSGKFSGDISDDLFRFAFESITSVVFGERLGMLEEIVDPESQRFIDAVYQMFH TSVPMLNMPPDLFRLFRTKTWKDHAAAWDVIFSKADEYTQNFYWDLRQKRDFSKYPGVLY SLLGGNKLPFKNIQANITEMLAGGVDTTSMTLQWNLYEMAHNLKVQEMLRAEVLAARRQA QGDMAKMVQLVPLLKASIKETLRLHPISVTLQRYIVNDLVLRNYKIPAKTLVQVASYAMG RESSFFPNPNKFDPTRWLEKSQNTTHFRYLGFGWGVRQCLGRRIAELEMTIFLINVLENF RIEVQSIRDVGTKFNLILMPEKPIFFNFQPLKQDLGSTMPRKGDTV
A39740 A39740 I39233 I55588 10-Sep-1999 10-Sep-1999 03-Mar-2000
sterol 27-monooxygenase (EC 1.14.14.-) cytochrome P450 27, precursor sterol 27-hydroxylase vitamin D3 25-hydroxylase human man Homo sapiens Cali, J.J. Russell, D.W. J. Biol. Chem. 26619917774-7778 Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reactions in bile acid biosynthesis. MUID91210301 A39740 mRNA 1-531 GBM62401 NIDg181291 PIDNAAA52142.1 PIDg181292 Guo, Y.D. Strugnell, S. Back, D.W. Jones, G. Proc. Natl. Acad. Sci. U.S.A. 9019938668-8672 Transfected human liver cytochrome P-450 hydroxylates vitamin D analogs at different side-chain positions. MUID93391416 I39233 mRNA 1-19,'SA',22,'T',24,26-170,'R',172-531 EMBLX59812 NIDg414120 PIDNCAA42481.1 PIDg414121 HepG2 cells this enzyme, after transfection into transformed monkey kidney cells, was capable of 24-, 25-, and 26(27)-hydroxylation of vitamin D analogs Leitersdorf, E. Reshef, A. Meiner, V. Levitzki, R. Schwartz, S.P. Dann, E.J. Berkman, N. Cali, J.J. Klapholz, L. Berginer, V.M. J. Clin. Invest. 9119932488-2496 Frameshift and splice-junction mutations in the sterol 27-hydroxylase gene cause cerebrotendinous xanthomatosis in Jews or Moroccan origin. MUID93293982 I55588 preliminary translated from GB/EMBL/DDBJ DNA 1-15 GBS62709 NIDg386290 PIDNAAB27199.1 PIDg386291 GDBCYP27 GDB128129 OMIM213700 2q33-2qter human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 332-498 binding-site heme iron (Cys) (axial ligand) 476 predicted 531 complete MAALGCARLRWALRGAGRGLCPHGARAKAAIPAALPSDKATGAPGAGPGVRRRQRSLEEI PRLGQLRFFFQLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQ EGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAALYTDAFNE VIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTF VRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAA GPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEA LHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPK NTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSVPFGYGVRACLGRR IAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQFLQRQC
A33813 A33813 A90152 A90155 A30293 A32279 10-Sep-1999 10-Sep-1999 03-Mar-2000
sterol 26-monooxygenase (EC 1.14.14.-) cytochrome P450 26A1 precursor, mitochondrial cytochrome P450XXVIA1 sterol 26-hydroxylase rabbit domestic rabbit Oryctolagus cuniculus Andersson, S. Davis, D.L. Dahlbaeck, H. Joernvall, H. Russell, D.W. J. Biol. Chem. 26419898222-8229 Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. MUID89255259 A33813 mRNA 1-535 GBJ04717 NIDg164964 PIDNAAA31225.1 PIDg164965 parts of this sequence, including the amino and carboxyl ends of the mature protein, were confirmed by peptide sequencing Dahlbaeck, H. Biochem. Biophys. Res. Commun. 157198830-36 Characterization of the liver mitochondrial cytochrome P-450 catalyzing the 26-hydroxylation of 5beta-cholestane-3alpha,7alpha,12alpha-triol. MUID89061727 A90152 protein 37-44,'E',46-49,51-54,'GGV' Dahlbaeck, H. Biochem. Biophys. Res. Commun. 1591989370 A90155 protein 37-54,'GGV' CYP27 catalyzes the first step in the oxidation of the side chain of sterol intermediates for bile acid biosynthesis human cytochrome P450 CYP11B1 cytochrome P450 homology cholesterol metabolism chromoprotein electron transfer heme iron metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain transit peptide (mitochondrion) 1-36 predicted product cytochrome P450 27 37-535 experimental domain cytochrome P450 homology 335-502 binding-site heme iron (Cys) (axial ligand) 480 predicted 535 complete MAALGCARLRWALLGPRVAGCGLCPQGARAKAAIPTALPADEAAQAPGAGPGDRRRRRSL EELPRLGQLRFFYQAFVQGYLLHLHKLQVLNKARYGPMWVSYLGPQLFVNLASAPLVETV MRQEGKYPVRNDMQLWKEHRDHQDLAYGVFTTDGHDWYQLRQALNQRLLKPAEAALYTDA LNEVIDSFVVRLDQLRAESASGDQVPDMADLLYHFALEAICYILFEKRIGCLEASIPKDT ENFIRSVGLMFQNSVYVTFLPKWTRPLLPFWKRYLDGWDTIFSFGKNLIDQKLQEVVAQL QSAGSDGVQVSGYLHSLLTSGQLSPREALGSLPELLLAGVDTTSNTLTWALYHLSKNPEI QAALRKEVVGVVAAGQVPQHKDFAHMPLLKAVLKETLRLYPVIPANSRIIVDKEIEVGGF LFPKNTQFVFCHYVTSRDPSTFSEPDTFWPYRWLRKGQPETSKTQHPFGSVPFGYGVRAC LGRRIAELEMQLLLARLIQRYELMLAPETGEVQSVARIVLVPNKKVGLRFLPTQR
O4RTV3 S09198 A34558 A36239 A33406 A40291 31-Mar-1991 31-Mar-1991 03-Mar-2000
vitamin D3 25-monooxygenase (EC 1.14.14.-) cytochrome P450 27 precursor, mitochondrial cholesterol 26-hydroxylase cytochrome P450 CYP27 cytochrome P450c26/25 cytochrome P450mt3, phenobarbital-inducible vitamin D3 25-hydroxylase rat Norway rat Rattus norvegicus Usui, E. Noshiro, M. Okuda, K. FEBS Lett. 2621990135-138 Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat liver mitochondria. MUID90201359 S09198 mRNA 1-533 EMBLY07534 NIDg56033 PIDNCAA68822.1 PIDg56034 A34558 protein 33-37 Su, P. Rennert, H. Shayiq, R.M. Yamamoto, R. Zheng, Y.M. Addya, S. Strauss III, J.F. Avadhani, N.G. DNA Cell Biol. 91990657-665 A cDNA encoding a rat mitochondrial cytochrome P450 catalyzing both the 26-hydroxylation of cholesterol and 25-hydroxylation of vitamin D-3: gonadotropic regulation of the cognate mRNA in ovaries. MUID91083838 A36239 mRNA 1-430,'T',432-533 GBM38566 NIDg858743 PIDNAAB02287.1 PIDg1374714 Shayiq, R.M. Avadhani, N.G. Biochemistry 2819897546-7554 Purification and characterization of a hepatic mitochondrial cytochrome P-450 active in aflatoxin B-1 metabolism. MUID90122729 A33406 protein 33-39,'TD' Addya, S. Zheng, Y.M. Shayiq, R.M. Fan, J. Avadhani, N.G. Biochemistry 3019918323-8330 Characterization of a female-specific hepatic mitochondrial cytochrome P-450 whose steady-state level is modulated by testosterone. MUID91355184 A40291 protein 33-42 CYP27 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron liver metalloprotein mitochondrion monooxygenase oxidoreductase transmembrane protein domain transit peptide (mitochondrion) 1-32 predicted product vitamin D3 25-hydroxylase 33-533 experimental domain cytochrome P450 homology 334-501 binding-site heme iron (Cys) (axial ligand) 479 predicted 533 complete MAVLSRMRLRWALLDTRVMGHGLCPQGARAKAAIPAALRDHESTEGPGTGQDRPRLRSLA ELPGPGTLRFLFQLFLRGYVLHLHELQALNKAKYGPMWTTTFGTRTNVNLASAPLLEQVM RQEGKYPIRDSMEQWKEHRDHKGLSYGIFITQGQQWYHLRHSLNQRMLKPAEAALYTDAL NEVISDFIARLDQVRTESASGDQVPDVAHLLYHLALEAICYILFEKRVGCLEPSIPEDTA TFIRSVGLMFKNSVYVTFLPKWSRPLLPFWKRYMNNWDNIFSFGEKMIHQKVQEIEAQLQ AAGPDGVQVSGYLHFLLTKELLSPQETVGTFPELILAGVDTTSNTLTWALYHLSKNPEIQ EALHKEVTGVVPFGKVPQNKDFAHMPLLKAVIKETLRLYPVVPTNSRIITEKETEINGFL FPKNTQFVLCHYVVSRDPSVFPEPESFQPHRWLRKREDDNSGIQHPFGSVPFGYGVRSCL GRRIAELEMQLLLSRLIQKYEVVLSPGMGEVKSVSRIVLVPSKKVSLRFLQRQ
JC5713 JC5713 10-Sep-1999 10-Sep-1999 03-Mar-2000
25-hydroxyvitamin D3 1-alpha-hydroxylase (EC 1.14.-.-) precursor human man Homo sapiens Monkawa, T. Yoshida, T. Wakino, S. Shinki, T. Anazawa, H. DeLuca, H.F. Suda, T. Hayashi, M. Saruta, T. Biochem. Biophys. Res. Commun. 2391997527-533 Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1-alpha-hydroxylase. MUID98008873 JC5713 mRNA 1-508 DDBJAB005038 NIDg2626736 PIDNBAA23416.1 PIDg2626737 This enzyme catalyzes the conversion of 25-hydroxyvitamin D3 to 1-alpha,25-dihydroxyvitamin D3. It plays also a role in calcium homeostasis. GDBPDDR GDBVDR GDBVDD1 GDBCYP27B GDBCYP1ALPHA GDB120486 OMIM264700 12q12-12q13 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 314-477 domain heme-binding 450-470 predicted binding-site heme iron (Cys) (axial ligand) 455 predicted 508 complete MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSR LHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCR QRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPP ALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPH WLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFRE ELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPS ATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPA QFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQP EPGAAPVRPKTRTVLVPERSINLQFLDR
A47436 A47436 10-Sep-1999 10-Sep-1999 21-Jul-2000
1,25-dihydroxyvitamin D3 24-hydroxylase (EC 1.14.-.-) precursor human man Homo sapiens Chen, K.S. Prahl, J.M. DeLuca, H.F. Proc. Natl. Acad. Sci. U.S.A. 9019934543-4547 Isolation and expression of human 1,25-dihydroxyvitamin D-3 24-hydroxylase cDNA. MUID93281615 A47436 preliminary mRNA 1-513 GBL13286 NIDg306703 PIDNAAA62379.1 PIDg306704 GDBCYP24 GDB134534 OMIM600125 20q13.3-20q13.3 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain transit peptide (mitochondrion) 1-35 predicted product 1,25-dihydroxyvitamin D3 24-hydroxylase 36-513 predicted domain cytochrome P450 homology 322-483 binding-site heme iron (Cys) (axial ligand) 461 predicted 513 complete MSSPISKSRSLAAFLQQLRSPRQPPRLVTSTAYTSPQPREVPVCPLTAGGETQNAAALPG PTSWPLLASLLQILWKGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYR TESVPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINE VLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMA IKTMMSTFGRMMVTPVELHKSLNTKVWQGHTLAWDTIFKSVKACIDNRLEKYSQQPSADF LCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLP ENQRPREEDLRNMPYLKACLKESMRLTPGVPFTTRTLDKATVLGEYALPKGTVLMLNTQV LGSSEDNFEDSSQFRPERWLQEKEKINPFAHLPFGVGKRMCIGRRLAELQLHLALCWIVR KYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR
JX0225 JX0225 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 CYP10 oxidoreductase (EC 1.-.-.-) great pond snail great pond snail Lymnaea stagnalis Teunissen, Y. Geraerts, W.P.M. van Heerikhuizen, H. Planta, R.J. Joosse, J. J. Biochem. 1121992249-252 Molecular cloning of a cDNA encoding a member of a novel cytochrome P-450 family in the mollusc Lymnaea stagnalis. MUID93015787 JX0225 mRNA 1-545 GBS46130 NIDg257242 PIDNAAB23599.1 PIDg257243 CYP10 human cytochrome P450 CYP11B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 348-515 binding-site heme iron (Cys) (axial ligand) 493 predicted 545 complete MAIMKKFIHHSLKQLIKPNLTSTKRVVSTSPRKEQGVAAISLEPSEMAQCPFRKSIDTFT ETTNAVKAPGMTEVQPFERIPGPKGLPIVGTLFDYFKKDGPKFSKMFEVYRQRALEFGNI YYEKVGHFHCVVISSPGEYSRLVHAERQYPNRREMVPIAYYRKQKGFDLGVVNSQGEEWY RQRTVVSKKMLKLAEVSNFSTQMGEVSDDFVKRLSHVRDSHGEIPALERELFKWAMESIG TFLFEERIGCLGQETSPMAQTFIANLEGFFKTLQPLMYNLPTYKLWSTKLWKQFENYSDN VIDIGRSLVEKKWHPCKMEVTQNLHLISYLVNNGSMSTKEVTGLIVDLMLAAVETTSSAT VWCLYNLAKNPQVQEKLFQEITEAQAKNNGTISAEDLCKLPMVKAVVKETLRLYPITYST SRNIAEDMELGGYTIPAGTHVQANLYGMYRDPSLFPEPEGILPERWLRMNGSQMDATIKS TSQLVWGHGARMCLGRRIAEQEMHITLSKIIQNFTLSYNHDDVEPILNTMLTPDRPVRIE FKPRQ
JH0659 S29818 JH0659 S11051 A42201 A54310 30-Jun-1993 30-Jun-1993 03-Mar-2000
cholesterol 7alpha-monooxygenase (EC 1.14.13.17) chain 1 cholesterol 7alpha-hydroxylase cytochrome P450, subfamily VIIA human man Homo sapiens Nishimoto, M. Noshiro, M. Okuda, K. Biochim. Biophys. Acta 11721993147-150 Structure of the gene encoding human liver cholesterol 7alpha-hydroxylase. MUID93176797 S29818 preliminary DNA 1-504 EMBLL04633 Karam, W.G. Chiang, J.Y.L. Biochem. Biophys. Res. Commun. 1851992588-595 Polymorphisms of human cholesterol 7 alpha-hydroxylase. MUID92304280 JH0659 mRNA 1-504 GBM93133 NIDg181318 PIDNAAA58435.1 PIDg181319 liver 100-Ser was also found Noshiro, M. Okuda, K. FEBS Lett. 2681990137-140 Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7-alpha-hydroxylase. MUID90346120 S11051 mRNA 1-346,'N',348-384,'S',386-504 GBM93133 Molowa, D.T. Chen, W.S. Cimis, G.M. Tan, C.P. Biochemistry 3119922539-2544 Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene. MUID92190183 A42201 DNA 1-25 GBM89647 GBJ05363 NIDg180469 PIDNAAA58423.1 PIDg553228 sequence extracted from NCBI backbone (NCBIN:89078, NCBIP:89079) Wang, D.P. Chiang, J.Y. Genomics 201994320-323 Structure and nucleotide sequences of the human cholesterol 7 alpha-hydroxylase gene (CYP7). MUID94292222 A54310 translated from GB/EMBL/DDBJ DNA 1-140 GBL13460 NIDg499855 PIDNAAA61350.1 PIDg624966 This liver microsomal enzyme catalyzes the conversion of cholesterol to bile acid; this reaction is the first and rate-limiting step in bile acid synthesis in the liver. GDBCYP7A1 GDBCYP7 GDB132221 OMIM118455 8q11-8q12 27/2; 107/3; 303/2; 347/1; 405/3 human cytochrome P450 CYP7A1 cytochrome P450 homology cholesterol metabolism chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 282-466 binding-site heme iron (Cys) (axial ligand) 444 predicted 504 complete MMTTSLIWGIAIAACCCLWLILGIRRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQ RKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDWKKFHFATSAKAFGHRSIDPMDGN TTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYRVMF EAGYLTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAE SLRHENLQKRESISELISLRMFLNDTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQ MIRNPEAMKAATEEVKRTLENAGQKVSLEGNPICLSQAELNDLPVLDSIIKESLRLSSAS LNIRTAKEDFTLHLEDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENGKTK TTFYCNGLKLKYYYMPFGSGATICPGRLFAIHEIKQFLILMLSYFELELIEGQAKCPPLD QSRAGLGILPPLNDIEFKYKFKHL
A35376 A35376 A35609 A36450 S06632 A37071 A38736 S27206 30-Jun-1993 30-Jun-1993 21-Jul-2000
cholesterol 7alpha-monooxygenase (EC 1.14.13.17) cholesterol 7alpha-hydroxylase rat Norway rat Rattus norvegicus Jelinek, D.F. Andersson, S. Slaughter, C.A. Russell, D.W. J. Biol. Chem. 26519908190-8197 Cloning and regulation of cholesterol 7alpha-hydroxylase, the rate-limiting enzyme in bile acid biosynthesis. MUID90243699 A35376 mRNA 1-503 GBJ05430 NIDg203792 PIDNAAA41041.1 PIDg203793 Jelinek, D.F. Russell, D.W. Biochemistry 2919907781-7785 Structure of the rat gene encoding cholesterol 7alpha-hydroxylase. MUID91084435 A35609 DNA 1-26 GBJ02926 Noshiro, M. Nishimoto, M. Okuda, K. J. Biol. Chem. 265199010036-10041 Rat liver cholesterol 7alpha-hydroxylase. Pretranslational regulation for circadian rhythm. MUID90277612 A36450 mRNA 1-503 GBJ05460 NIDg203455 PIDNAAA03649.1 PIDg203456 Noshiro, M. Nishimoto, M. Morohashi, K.I. Okuda, K. FEBS Lett. 257198997-100 Molecular cloning of cDNA for cholesterol 7alpha-hydroxylase from rat liver microsomes. Nucleotide sequence and expression. MUID90033362 S06632 mRNA 1-503 GBX17595 NIDg57535 PIDNCAB57878.1 PIDg6018697 Li, Y.C. Wang, D.P. Chiang, J.Y.L. J. Biol. Chem. 265199012012-12019 Regulation of cholesterol 7alpha-hydroxylase in the liver. Cloning, sequencing, and regulation of cholesterol 7alpha-hydroxylase mRNA. MUID90307735 A37071 mRNA 1-503 GBJ05509 NIDg203204 PIDNAAA40839.1 PIDg203205 Nishimoto, M. Gotoh, O. Okuda, K. Noshiro, M. J. Biol. Chem. 26619916467-6471 Structural analysis of the gene encoding rat cholesterol alpha-hydroxylase, the key enzyme for bile acid biosynthesis. MUID91177904 A38736 DNA 1-370,'S',372-503 GBM59184 Chiang, J.Y.L. Yang, T.P. Wang, D.P. Biochim. Biophys. Acta 11321992337-339 Cloning and 5'-flanking sequence of a rat cholesterol 7alpha-hydroxylase gene. MUID93041942 S27206 DNA 1-26 GBZ14108 GBS48135 NIDg55835 PIDNCAA78481.1 PIDg55836 This liver microsomal enzyme catalyzes the conversion of cholesterol to bile acid; this reaction is the first and rate-limiting step in bile acid synthesis in the liver. 27/2; 107/3; 303/2; 347/1; 405/3 human cytochrome P450 CYP7A1 cytochrome P450 homology cholesterol metabolism chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 282-466 binding-site heme iron (Cys) (axial ligand) 444 predicted 503 complete MMTISLIWGIAVLVSCCIWFIVGIRRRKAGEPPLENGLIPYLGCALKFGSNPLEFLRANQ RKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSIDPNDGN TTENINNTFTKTLQGDALCSLSEAMMQNLQSVMRPPGLPKSKSNAWVTEGMYAFCYRVMF EAGYLTLFGRDISKTDTQKALILNNLDNFKQFDQVFPALVAGLPIHLFKTAHKAREKLAE GLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQ MIRSPEAMKAASEEVSGALQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSAS LNIRTAKEDFTLHLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAK TTFYSNGNKLKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLD QSRAGLGILPPLHDIEFKYKLKH
JC2231 JC2231 10-Sep-1999 10-Sep-1999 16-Jun-2000
prostaglandin-I synthase (EC 5.3.99.4) prostacyclin synthase human man Homo sapiens Miyata, A. Hara, S. Yokoyama, C. Inoue, H. Ullrich, V. Tanabe, T. Biochem. Biophys. Res. Commun. 20019941728-1734 Molecular cloning and expression of human prostacyclin synthase. MUID94242046 JC2231 mRNA 1-500 GBD38145 NIDg537948 PIDNBAA07343.1 PIDg537949 aortic endothelial cell This enzyme catalyzes the conversion of prostaglandin H2 to prostaglandin I2. GDBPTGIS GDBPGIS GDBCYP8 GDB362921 OMIM601699 20q13.11-20q13.13 human cytochrome P450 CYP7A1 cytochrome P450 homology intramolecular oxidoreductase isomerase 500 complete MAWAALLGLLAALLLLLLLSRRRTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEK HGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDE KARMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTL YGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSLSVGDKDHMCSVKSRLWKL LSPARLARRAHRSKWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLL KNPEALAAVRGELESILWQAEQPVSQTTTLPQKVLDSTPVLDSVLSESLRLTAAPFITRE VVVDLAMPMADGREFNLRRGDRLLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDF YKDGKRLKNYNMPWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSR YGFGLMQPEHDVPVRYRIRP
S68855 S68855 10-Sep-1999 10-Sep-1999 21-Jul-2000
lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 human man Homo sapiens Stroemstedt, M. Rozman, D. Waterman, M.R. Arch. Biochem. Biophys. 329199673-81 The ubiquitously expressed human CYP51 encodes lanosterol 14alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. MUID96201125 S68855 preliminary nucleic acid sequence not shown mRNA 1-509 EMBLU23942 GDBCYP51 GDB4073039 OMIM601637 7q21.2-7q21.3 human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 314-477 binding-site heme iron (Cys) (axial ligand) 455 predicted 509 complete MAAAAGMLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQL PAGVKSPPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAA ALLFNSKNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSI IEKETKEYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGF SHAAWLLPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGR PLTDDEVAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTY DQLKDLNLLDRCIRETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDS WVERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDL IDGYFPTVNYTTMIHTPENPVIRYKRRSK
O4CK51 S02713 31-Mar-1992 31-Mar-1992 03-Mar-2000
lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 cytochrome P450 LIA1 yeast (Candida albicans) Candida albicans Lai, M.H. Kirsch, D.R. Nucleic Acids Res. 171989804 Nucleotide sequence of cytochrome P450 L1A1 (lanosterol 14alpha-demethylase) from Candida albicans. MUID89128456 S02713 DNA 1-528 EMBLX13296 CYP51 human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 304-492 binding-site heme iron (Cys) (axial ligand) 470 predicted 528 complete MAIVETVIDGINYFLSLSVTQQISILLGVPFVYNLVWQYLYSLRKDRAPLVFYWIPWFGS AASYGQQPYEFFESCRQKYGDVFSFMLLGKIMTVYLGPKGHEFVFNAKLSDVSAEDAYKH LTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKRYVPKIREEILNYFVTDESFKLKE KTHGVANVMKTQPEITIFTASRSLFGDEMRRIFDRSFAQLYSDLDKGFTPINFVFPNLPL PHYWRRDAAQKKISATYMKEIKLRRERGDIDPNRDLIDSLLIHSTYKDGVKMTDQEIANL LIGILMGGQHTSASTSAWFLLHLGEKPHLQDVIYQEVVELLKEKGGDLNDLTYEDLQKLP SVNNTIKETLRMHMPLHSIFRKVTNPLRIPETNYIVPKGHYVLVSPGYAHTSERYFDNPE DFDPTRWDTAAAKANSVSFNSSDEVDYGFGKVSKGVSSPYLPFGGGRHRCIGEQFAYVQL GTILTTFVYNLRWTIDGYKVPDPDYSSMVVLPTEPAEIIWEKRETCMF
A31854 A31854 A26828 10-Sep-1999 10-Sep-1999 03-Mar-2000
lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 cytochrome P450 14DM yeast (Candida tropicalis) Candida tropicalis Chen, C. Kalb, V.F. Turi, T.G. Loper, J.C. DNA 71988617-626 Primary structure of the cytochrome P450 lanosterol 14alpha-demethylase gene from Candida tropicalis. MUID89152749 A31854 DNA 1-528 GBM23673 NIDg341007 PIDNAAA53284.1 PIDg576547 ATCC 750 Chen, C. Turi, T.G. Sanglard, D. Loper, J.C. Biochem. Biophys. Res. Commun. 14619871311-1317 Isolation of the Candida tropicalis gene for P450 lanosterol demethylase and its expression in Saccharomyces cerevisiae. MUID87298576 A26828 DNA 434-447,'V',449-499,'G',501-528 GBM17595 NIDg170811 PIDNAAA34316.1 PIDg170812 ATCC 750 the authors translated the codon GTT for residue 448 as Gly and GGT for residue 500 as Val CYP51 human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 304-492 binding-site heme iron (Cys) (axial ligand) 470 predicted 528 complete MAIVDTAIDGINYFLSLSLTQQITILVVFPFIYNIAWQLLYSLRKDRVPMVFYWIPWFGS AASYGMQPYEFFEKCRLKYGDVFSFMLLGKVMTVYLGPKGHEFIYNAKLSDVSAEEAYTH LTTPVFGKGVIYDCPNSRLMEQKKFAKFALTTDSFKTYVPKIREEVLNYFVNDVSFKTKE RDHGVASVMKTQPEITIFTASRCLFGDEMRKSFDRSFAQLYADLDKGFTPINFVFPNLPL PHYWRRDAAQRKISAHYMKEIKRRRESGDIDPKRDLIDSLLVNSTYKDGVKMTDQEIANL LIGVLMGGQHTSASTSAWFLLHLAEQPQLQDDLYEELTNLLKEKGGDLNDLTYEDLQKLP LVNNTIKETLRMHMPLHSIFRKVMNPLRVPNTKYVIPKGHYVLVSAGYAHTSDRWFEHPE HFNPRRWESDDTKASAVSFNSEDTVDYGFGKISKGVSSPYLPFGGGRHRCIGEQFAYVQL GTILTTYIYNFKWRLNGDKVPDVDYQSMVTLPLEPAEIVWEKRDTCMV
A27491 A27491 S46804 B31569 A25563 10-Sep-1999 10-Sep-1999 23-Mar-2001
lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 protein YHR007c yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Kalb, V.F. Woods, C.W. Turi, T.G. Dey, C.R. Sutter, T.R. Loper, J.C. DNA 61987529-537 Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae. MUID88111027 A27491 DNA 1-530 EMBLM18109 NIDg170945 PIDNAAA34379.1 PIDg170946 Favello, T. submitted to the EMBL Data Library June1994 The sequence of S. cerevisiae cosmid 9780. S46804 DNA 1-530 EMBLU10555 NIDg500813 PIDNAAB68433.1 PIDg500824 GSPDBGN00008 MIPSYHR007c Ishida, N. Aoyama, Y. Hatanaka, R. Oyama, Y. Imajo, S. Ishiguro, M. Oshima, T. Nakazato, H. Noguchi, T. Maitra, U.S. Mohan, V.P. Sprinson, D.B. Yoshida, Y. Biochem. Biophys. Res. Commun. 1551988317-323 A single amino acid substitution converts cytochrome P450-14DM to an inactive form, cytochrome P450-SG1: complete primary structures deduced from cloned DNAs. MUID88326319 B31569 DNA 1-432,'N',434-530 EMBLM21483 NIDg171353 PIDNAAA34546.1 PIDg171354 Kalb, V.F. Loper, J.C. Dey, C.R. Woods, C.W. Sutter, T.R. Gene 451986237-245 Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae. MUID87106820 A25563 DNA 444-530 EMBLM15663 SGDERG11 MIPSYHR007c SGDS0001049 MIPSYHR007c 8R human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 311-492 binding-site heme iron (Cys) (axial ligand) 470 predicted 530 complete MSATKSIVGEALEYVNIGLSHFLALPLAQRISLIIIIPFIYNIVWQLLYSLRKDRPPLVF YWIPWVGSAVVYGMKPYEFFEECQKKYGDIFSFVLLGRVMTVYLGPKGHEFVFNAKLADV SAEAAYAHLTTPVFGKGVIYDCPNSRLMEQKKFVKGALTKEAFKSYVPLIAEEVYKYFRD SKNFRLNERTTGTIDVMVTQPEMTIFTASRSLLGKEMRAKLDTDFAYLYSDLDKGFTPIN FVFPNLPLEHYRKRDHAQKAISGTYMSLIKERRKNNDIQDRDLIDSLMKNSTYKDGVKMT DQEIANLLIGVLMGGQHTSAATSAWILLHLAERPDVQQELYEEQMRVLDGGKKELTYDLL QEMPLLNQTIKETLRMHHPLHSLFRKVMKDMHVPNTSYVIPAGYHVLVSPGYTHLRDEYF PNAHQFNIHRWNKDSASSYSVGEEVDYGFGAISKGVSSPYLPFGGGRHRCIGEHFAYCQL GVLMSIFIRTLKWHYPEGKTVPPPDFTSMVTLPTGPAKIIWEKRNPEQKI
S52319 S52319 10-Sep-1999 10-Sep-1999 21-Jul-2000
unspecific monooxygenase (EC 1.14.14.1) smut fungus (Ustilago maydis) corn smut Ustilago maydis Hargreaves, J.A. Keon, J.P.R. submitted to the EMBL Data Library February1995 The sterol 14 alpha-demethylase (ERG11) gene from Ustilago maydis. S52319 preliminary DNA 1-561 EMBLZ48164 NIDg663266 PIDNCAA88176.1 PIDg663267 human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 322-523 binding-site heme iron (Cys) (axial ligand) 501 predicted 561 complete MVASSSSATASLLDQLFALTPLADSSAWIKTITVLVLLPLLAVVLNVASQLLLATPKNHP PVVFHFVPVIGSAIYYGIDPYKFFFECREKYGDVFTFVLLGRKITVALGPKGSNLVFNAK HQQVTAEDAYTHLTTPVFGKEVVYDVPNAVFMEQKKFVKVGLSIENFRVYVPQIVDEVRE YIKSDARFSALKTRKTITVDIFQAMSELIILTASRTLQGKEVRQGLDKSFAQLYHDLDSG FTPINFVIPNLPLPSNFKRDRAQKKMSQFYQDIVAKRRAAGASTSADDASGENDMIAALI EQKYKNGRALSGVEIAHMMIALLMAGQHTSSATSSWAFLRLASRPEIIEELYEEQLNVYS DGHGGLRELDYETQKTSVPLLDAVVKETLRLHPPLHSIMRYVKSDLAVPPTLSSPTSTKS EPDAHYVIPKGHYIMAAPGVSQVDPQIWKSSDQFDPHRWLDATTAAAMQDSGEDKQDFGF GMISTGANSPYLPFGAGRHRCIGEQFAYLQIGVILATFVRIFKWHLDSKFPDPDYQSMVV LPSKNGCAIVLTPRAESLHLD
S65578 S65578 S54836 10-Sep-1999 10-Sep-1999 21-Jul-2000
lanosterol 14alpha-demethylase (EC 1.14.14.-) cytochrome P450 51 Penicillium italicum Penicillium italicum van Nistelrooy, J.G.M. van den Brink, J.M. van Kan, J.A.L. van Gorcom, R.F.M. de Waard, M.A. Mol. Gen. Genet. 2501996725-733 Isolation and molecular characterisation of the gene encoding eburicol 14-alpha-demethylase (CYP51) from Penicillium italicum. MUID96204513 S65578 DNA 1-515 EMBLZ49750 NIDg836641 PIDNCAA89824.1 PIDg836642 CYP51 72/3; 138/3; 497/3 human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 301-481 binding-site heme iron (Cys) (axial ligand) 459 predicted 515 complete MDLVPLVTGQILGIAYYTTGLFLVSIVLNVIKQLIFYNRKEPPVVFHWIPFIGSTIAYGM DPYQFFFASRAKYGDIFTFILLGKKTTVYLGVEGNEFILNGKLKDVNAEEVYGKLTTPVF GSDVVYDCPNSKLMEQKKFIKYGLSQEALESYVPLIADETNAYIKSSPNFKGQSGTIDLA AAMAEITIFTAARTLQGEEVRSKLTSEFADLFHDLDLGFSPINFMLPWAPLPHNASAIKH TTYARDLSGNYPSATGSWRRRQRRRQDKSKGTDMISNLMRCVYRDGTPIPDKEIAHMMIT LLMAGQHSSSAISCWILLRLASQPEMAEKLHAEQIKNLGADLPPLQYKDMDKLPLLRNVI KETLRLHSSIHTLMRKVKNPMPVPGTDFVVPPSHTLLSSPGVTARDERHFRDPLRWDPHR WESRVEVEDSSDTVDYGYGAVSKGTRSPYLPFGAGRHRCIGEKFAYLNLEVIVATLVREF RFFNPEGMEGVPDTDYSSLFSRPVQPATVRWEVRS
G70706 G70706 10-Sep-1999 10-Sep-1999 21-Jul-2000
probable sterol demethylase (EC 1.14.-.-) Rv0764c Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 G70706 preliminary nucleic acid sequence not shown translation not shown DNA 1-451 GBZ80226 GBAL123456 NIDg3261638 PIDNCAB02394.1 PIDg1550642 strain H37Rv Rv0764c human cytochrome P450 CYP51 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 253-416 binding-site heme iron (Cys) (axial ligand) 394 predicted 451 complete MSAVALPRVSGGHDEHGHLEEFRTDPIGLMQRVRDECGDVGTFQLAGKQVVLLSGSHANE FFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQ VRRMIADWGEAGEIDLLDFFAELTIYTSSACLIGKKFRDQLDGRFAKLYHELERGTDPLA YVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPR FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHA LRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFP DPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA QPPESYRNDHSKMVVQLAQPACVRYRRRTGV
O4HU19 A34451 A40542 S03962 A31580 A31255 A40142 S22908 A48762 A29480 B29840 A42405 A24344 A23546 A38241 B24344 C24344 D24344 E24344 PC2041 31-Mar-1992 31-Mar-1992 03-Mar-2000
aromatase (EC 1.14.14.-) cytochrome P450 19 cytochrome P450 aromatase estrogen synthetase human man Homo sapiens Means, G.D. Mahendroo, M.S. Corbin, C.J. Mathis, J.M. Powell, F.E. Mendelson, C.R. Simpson, E.R. J. Biol. Chem. 264198919385-19391 Structural analysis of the gene encoding human aromatase cytochrome P-450, the enzyme responsible for estrogen biosynthesis. MUID90037080 A34451 DNA 1-503 EMBLM30803 the authors translated the codon ATC for residue 70 as Thr Mahendroo, M.S. Means, G.D. Mendelson, C.R. Simpson, E.R. J. Biol. Chem. 266199111276-11281 Tissue-specific expression of human P-450-AROM. The promoter responsible for expression in adipose tissue is different from that utilized in placenta. MUID91250444 A40542 preliminary DNA 1-48 GBM74174 Toda, K. Terashima, M. Mitsuuchi, Y. Yamasaki, Y. Yokoyama, Y. Nojima, S. Ushiro, H. Maeda, T. Yamamoto, Y. Sagara, Y. Shizuta, Y. FEBS Lett. 2471989371-376 Alternative usage of different poly(A) addition signals for two major species of mRNA encoding human aromatase P-450. MUID89232157 S03962 mRNA 1-503 EMBLY07508 NIDg28848 PIDNCAA68807.1 PIDg28849 14-Ser was also found Harada, N. Biochem. Biophys. Res. Commun. 1561988725-732 Cloning of a complete cDNA encoding human aromatase: immunochemical identification and sequence analysis. MUID89050098 A31580 mRNA 1-495,'S',497-503 EMBLM22246 NIDg179001 PIDNAAA35557.1 PIDg179002 Corbin, C.J. Graham-Lorence, S. McPhaul, M. Mason, J.I. Mendelson, C.R. Simpson, E.R. Proc. Natl. Acad. Sci. U.S.A. 8519888948-8952 Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells. MUID89057856 A31255 mRNA 1-263,'C',265-503 EMBLJ04127 NIDg181212 PIDNAAA52132.1 PIDg181213 Pompon, D. Liu, R.Y.K. Besman, M.J. Wang, P.L. Shively, J.E. Chen, S. Mol. Endocrinol. 319891477-1487 Expression of human placental aromatase in Saccharomyces cerevisiae. MUID90114215 A40142 preliminary not compared with conceptual translation mRNA 1-7,'Q',9-440,'V',442-503 placenta Simpson, E.R. Evans, C.T. Corbin, C.J. Powell, F.E. Ledesma, D.B. Mendelson, C.R. Mol. Cell. Endocrinol. 521987267-272 Sequencing of cDNA inserts encoding aromatase cytochrome P-450 (P-450(AROM)). MUID88005438 S22908 mRNA 85-263,'C',265-503 EMBLM28420 NIDg181287 PIDNAAA52141.1 PIDg181288 the authors translated the codon ATG for residue 219 as His Mahendroo, M.S. Mendelson, C.R. Simpson, E.R. J. Biol. Chem. 268199319463-19470 Tissue-specific and hormonally controlled alternative promoters regulate aromatase cytochrome P450 gene expression in human adipose tissue. MUID93374934 A48762 mRNA 1-48 different 5'-untranslated sequences were demonstrated in a variety of clones Chen, S. Besman, M.J. Sparkes, R.S. Zollman, S. Klisak, I. Mohandas, T. Hall, P.F. Shively, J.E. DNA 7198827-38 Human aromatase: cDNA cloning, southern blot analysis, and assignment of the gene to chromosome 15. MUID88166351 A29480 mRNA 85-503 EMBLM18856 NIDg178999 PIDNAAA35556.1 PIDg179000 B29840 protein 120-142;151-169;253-262;294-311;335-343;347-443;462-483;486-503 Harada, N. Ogawa, H. Shozu, M. Yamada, K. Suhara, K. Nishida, E. Takagi, Y. J. Biol. Chem. 26719924781-4785 Biochemical and molecular genetic analyses on placental aromatase (P-450AROM) deficiency. MUID92165841 A42405 mRNA 246-248,'QVIQLWKIYEYNWIGFFPLCLCCFSWPLS',249-258 GBS85075 NIDg246080 PIDNAAB21500.1 PIDg246081 placenta; placental aromatase deficiency patient sequence extracted from NCBI backbone (NCBIN:85075, NCBIP:85080) mutation of the splice donor for intron 6 and splicing instead at a cryptic splice donor causes an in-frame insertion in this patient with placental aromatase deficiency Chen, S. Shively, J.E. Nakajin, S. Shinoda, M. Hall, P.F. Biochem. Biophys. Res. Commun. 1351986713-719 Amino terminal sequence analysis of human placenta aromatase. MUID86186829 A24344 protein 2-11,'L',13,'LVL',17,'LP',20-21,'V';120-126,'HE',129-130;160-170;463-473;496-503 placenta Evans, C.T. Ledesma, D.B. Schulz, T.Z. Simpson, E.R. Mendelson, C.R. Proc. Natl. Acad. Sci. U.S.A. 8319866387-6391 Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA. MUID86313586 A23546 mRNA 458-476 Hagerman, D.D. submitted to the Protein Sequence Database July1992 A38241 protein 'XXX',8-11,'L',13-18,'Z',20-23,'L',25-27,'T',29 placenta Honda, S. Harada, N. Takagi, Y. Biochem. Biophys. Res. Commun. 19819941153-1160 Novel exon 1 of the aromatase gene specific for aromatase transcripts in human brain. MUID94161727 annotation alternative exons 1 (coding region begins in exon 2) GDBCYP19 GDB119830 OMIM107910 15q21.1-15q21.1 49/1; 99/2; 151/1; 210/1; 248/2; 286/3; 341/1; 421/3 human cytochrome P450 CYP19 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase polymorphism steroid biosynthesis transmembrane protein domain cytochrome P450 homology 303-459 binding-site heme iron (Cys) (axial ligand) 437 predicted 503 complete MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLI SHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL GLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTN ESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWL YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCI LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFI YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAK NVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLH PDETKNMLEMIFTPRNSDRCLEH
A36121 A36121 S16901 S26817 10-Sep-1999 10-Sep-1999 03-Mar-2000
aromatase (EC 1.14.14.-) cytochrome P450 19 cytochrome P450 arom rat Norway rat Rattus norvegicus Hickey, G.J. Krasnow, J.S. Beattie, W.G. Richards, J.S. Mol. Endocrinol. 419903-12 Aromatase cytochrome P450 in rat ovarian granulosa cells before and after luteinization: adenosine 3',5'-monophosphate-dependent and independent regulation. Cloning and sequencing of rat aromatase cDNA and 5' genomic DNA. MUID90220647 A36121 mRNA 1-508 EMBLM33986 NIDg203804 PIDNAAA41044.1 PIDg203805 Lephart, E.D. Peterson, K.G. Noble, J.F. George, F.W. McPhaul, M.J. Mol. Cell. Endocrinol. 70199031-40 The structure of cDNA clones encoding the aromatase P-450 isolated from a rat Leydig cell tumor line demonstrates differential processing of aromatase mRNA in rat ovary and a neoplastic cell line. MUID90255798 S16901 preliminary mRNA 1-2,'FQ',5-9,'Q',11-87,'C',89-100,'L',102-122,'VVH',126,'HAR',130-187,'L',189-209,'G',211-327,'WKQ',332-341,'A',343-363,'CGIS',368,'F',370-421,'L',423-424,'T',426-448,'I',450-465,'K',467-492,'SPRNS' CYP19 human cytochrome P450 CYP19 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein microsome monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 303-459 binding-site heme iron (Cys) (axial ligand) 437 predicted 508 complete MFLEMLNPMHYNVTIMVPETVPVSAMPLLLIMGLLLLIRNCESSSSIPGPGYCLGIGPLI SHGRFLWMGIGSACNYYNKMYGEFMRVWISGEETLIISKSSSMVHVMKHSNYISRFGSKR GLQCIGMHENGIIFNNNPSLWRTVRPFFMKALTGPGLIRMVEVCVESIKQHLDRLGDVTD NSGYVDVVTLMRHIMLDTSNTLFLGIPLDESSIVKKIQGYFNAWQALLIKPNIFFKISWL YRKYERSVKDLKDEIEILVEKKRQKVSSAEKLEDCMDFATDLIFAERRGDLTKENVNQCI LEMLIAAPDTMSVTLYVMLLLIAEYPEVETAILKEIHTVVGDRDIRIGDVQNLKVVENFI NESLRYQPVVDLVMRRALEDDVIDGYPVKKGTNIILNIGRMHRLEYFPKPNEFTLENFEK NVPYRYFQPFGFGPRSCAGKYIAMVMMKVVLVTLLKRFHVKTLQKRCIENMPKNNDLSLH LDEDSPIVEIIFRHIFNTPFLQCLYISL
A31916 A31916 20-Apr-2000 20-Apr-2000 21-Jul-2000
aromatase (EC 1.14.14.-) cytochrome P450 19 (version 1) cytochrome P450 arom chicken chicken Gallus gallus McPhaul, M.J. Noble, J.F. Simpson, E.R. Mendelson, C.R. Wilson, J.D. J. Biol. Chem. 263198816358-16363 The expression of a functional cDNA encoding the chicken cytochrome P-450-arom (aromatase) that catalyzes the formation of estrogen from androgen. MUID89034107 A31916 mRNA 1-507 EMBLJ04047 NIDg211703 PIDNAAA48738.1 PIDg211704 it is uncertain whether Met-1 or Met-20 is the initiator CYP19 human cytochrome P450 CYP19 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 302-458 binding-site heme iron (Cys) (axial ligand) 436 predicted 507 complete MIPETLNPLNYFTSLVPDLMPVATVPIIILICFLFLIWNHEETSSIPGPGYCMGIGPLIS HGRFLWMGVGNACNYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNYVSRFGSKLG LQCIGMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTTE VGNVNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQNYFDAWQALLLKPDIFFKISWLC KKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVL EMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIY ESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLEFFPKPNEFSLENFEKN VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNDLSMHP IERQPLLEMVFTQEAQTRIRVTKVDQH
O4HUB1 S07765 S17971 A33414 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome P450 4B1 cytochrome P450-HP oxidoreductase (EC 1.-.-.-) human man Homo sapiens Yokotani, N. Sogawa, K. Matsubara, S. Gotoh, O. Kusunose, E. Kusunose, M. Fujii-Kuriyama, Y. Eur. J. Biochem. 187199023-29 cDNA cloning of cytochrome P-450 related to P-450(p-2) from the cDNA library of human placenta. Gene structure and expression. MUID90126824 S07765 DNA 1-511 GBX16699 NIDg35204 PIDNCAA34672.1 PIDg35205 S17971 mRNA 9-511 EMBLX16699 Nhamburo, P.T. Gonzalez, F.J. McBride, O.W. Gelboin, H.V. Kimura, S. Biochemistry 2819898060-8066 Identification of a new P450 expressed in human lung: complete cDNA sequence, cDNA-directed expression, and chromosome mapping. MUID90105307 A33414 DNA 1-36,'R',38-511 EMBLJ02871 NIDg180968 PIDNAAA35712.1 PIDg180969 GDBCYP4B1 GDB125372 OMIM124075 1p34-1p12 60/3; 108/1; 123/1; 165/3; 258/1; 293/3; 357/2; 402/1; 423/3; 451/2 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 312-475 binding-site heme iron (Cys) (axial ligand) 453 predicted 511 complete MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALE IQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQ WIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDI FCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLT PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKL SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDL GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWP DPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP SRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK
A40164 A40164 B61538 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 4B1 cytochrome P450 isoform 5 oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Gasser, R. Philpot, R.M. Mol. Pharmacol. 351989617-625 Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: identification of cytochrome P-450 gene subfamily IVB. MUID89261667 A40164 mRNA 1-506 GBM29852 NIDg164920 PIDNAAA31214.1 PIDg164921 the authors translated the codon CAG for residue 57 as Gly Parandoosh, Z. Fujita, V.S. Coon, M.J. Philpot, R.M. Drug Metab. Dispos. 15198759-67 Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of structure and inducibility. MUID87161284 B61538 protein 1-21 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 307-470 binding-site heme iron (Cys) (axial ligand) 448 predicted 506 complete MLGFLSRLGLWASGLILILGFLKLLRLLLRRQRLARAMDSFPGPPTHWLFGHALEIQKTG SLDKVVTWTQQFPYAHPLWVGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQWIGKG LLVLDGPKWFQHRKLLTPGFHYDVLKPYVAIFADSTRIMLEKWEKKACEGKSFDIFSDVG HMALDTLMKCTFGKGDSGLNHRDSSYYVAVSELTLLMQQRIDSFQYHNDFIYWLTPHGRR FLRACRAAHDHTDRVIRQRKAALQDEKEREKIQNRRHLDFLDILLDVRGESGVQLSDTDL RAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQQRCREEVREILGDQDSFQWEDLAKMTY LTMCMKECFRLYPPVPQVYRQLSKPVSFVDGRSLPAGSLISLHIYALHRNSDVWPDPEVF DPLRFSPENSSGRHPYAFIPFSAGPRNCIGQQFAMNEMKVVTALCLLRFEFSVDPLRLPI KLPQLVLRSKNGIHLYLKPLGPKAEK
B40164 B40164 PQ0092 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 4B1 cytochrome P450 L-2 P450 isozyme 5 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Gasser, R. Philpot, R.M. Mol. Pharmacol. 351989617-625 Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: identification of cytochrome P-450 gene subfamily IVB. MUID89261667 B40164 mRNA 1-511 GBM29853 NIDg205911 PIDNAAA41778.1 PIDg205912 the authors translated the codon CAG for residue 62 as Gly Imaoka, S. Funae, Y. J. Biochem. 108199033-36 Purification and characterization of rat pulmonary cytochrome P-450. MUID91035323 PQ0092 protein 2-6,'X',8,'X',10,'X' lung microsomes CYP4B1 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron lung metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 312-475 binding-site heme iron (Cys) (axial ligand) 453 predicted 511 complete MVLNFLSPSLSRLGLWASVVILMVIVLKLFSLLLRRQKLARAMDSFPGPPTHWLFGHALE IQKLGSLDKVVSWAQQFPHAHPLWFGQFVGFLNIYEPDYAKAVYSRGDPKAADVYDFFLQ WIGKGLLVLDGPKWFQHRKLLTPGFHYDVLKPYVAIFAESTRMMLDKWEKKASENKSFDI FCDVGHMALDTLMKCTFGKGDSGLGHRDNSYYLAVSDLTLLMQQRIDSFQYHNDFIYWLT PHGRRFLRACKIAHDHTDEVIRQRKAALQDEKERKKIQQRRHLDFLDILLGVRDESGIKL SDAELRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQQLCREEVRGILGDQDSFQWDDL AKMTYLTMCMKECFRLYPPVPQVYRQLNKPVTFVDGRSLPAGSLISLHIYALHRNSTVWP DPEVFDPLRFSPENAAGRHPFAFMPFSAGPRNCIGQQFAMNEMKVVTALCLLRFEFSLDP SKMPIKVPQLILRSKNGIHLYLKPLASRSGK
A29368 S32315 S32423 A29368 JN0089 03-Dec-1999 03-Dec-1999 03-Mar-2000
prostaglandin omega-hydroxylase (EC 1.14.15.-) cytochrome P450 4A4 cytochrome P450-P2 cytochrome P450kd rabbit domestic rabbit Oryctolagus cuniculus Palmer, C.N.A. Griffin, K.J. Johnson, E.F. Arch. Biochem. Biophys. 3001993670-676 Rabbit prostaglandin omega-hydroxylase (CYP4A4): gene structure and expression. MUID93167855 S32315 DNA 1-510 Palmer, C.N.A. Griffin, K.J. Johnson, E.F. submitted to the EMBL Data Library May1993 Rabbit prostaglandin omega-hydroxylase (CYP4A4): gene structure and expression. S32423 DNA 1-26,'CSCCCSRQLSSTCTASGCSERSSSSRARPSTGSWGTAE' EMBLL04758 NIDg164972 PIDNAAA31228.1 PIDg552372 the difference at the amino end is due to a frameshift error Matsubara, S. Yamamoto, S. Sogawa, K. Yokotani, N. Fujii-Kuriyama, Y. Haniu, M. Shively, J.E. Gotoh, O. Kusunose, E. Kusunose, M. J. Biol. Chem. 262198713366-13371 cDNA cloning and inducible expression during pregnancy of the mRNA for rabbit pulmonary prostaglandin omega-hydroxylase (cytochrome P-450-p-2). MUID88007548 A29368 mRNA 5-475,'V',477-486,'I',488-510 portions of this protein, including residues 5-29, were determined by protein sequencing Yoshimura, R. Kusunose, E. Yokotani, N. Yamamoto, S. Kubota, I. Kusunose, M. J. Biochem. 1081990544-548 Purification and characterization of two forms of fatty acid omega-hydroxylase cytochrome P-450 from rabbit kidney cortex microsomes. MUID91154157 JN0089 protein 5-24 kidney This protein catalyzes the omega- and (omega-1)-hydroxylation of fatty acids. CYP4A4 65/3; 113/1; 128/1; 170/3; 212/2; 264/1; 299/3; 363/2; 408/1; 429/3; 455/2 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 318-479 binding-site heme iron (Cys) (axial ligand) 457 predicted 510 complete MSVSALSPTRLPGSLSGLLQVAALLGLLLLLLKAAQLYLHRQWLLRALQQFPCPPFHWLL GHSREFQNDQELERIQKWVEKFPGACPWWLSGNKARLLVYDPDYLKVILGRSDPKAPRNY KLMTPWIGYGLLLLDGQTWFQHRRMLTPAFHYDILKPYVGLMVDSVQIMLDRWEQLISQD SSLEIFQHVSLMTLDTIMKCAFSYQGSVQLDRNSHSYIQAINDLNNLVFYRARNVFHQSD FLYRLSPEGRLFHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAKM ENGSSLSDQDLRAEVDTFMFEGHDTTASGVSWIFYALATHPEHQHRCREEIQGLLGDGAS ITWEHLDQMPYTTMCIKEALRLYPPVPSVTRQLSKPVTFPDGRSLPKGVILFLSIYGLHY NPKVWQNPEVFDPFRFAPDSAYHSHAFLPFSGGARNCIGKQFAMRELKVAVALTLLRFEL LPDPTRVPIPIARVVLKSKNGIHLRLRKLH
B34160 B34160 C34260 JN0090 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 4A7 cytochrome P450ka-2 cytochrome P450kc oxidoreductase (EC 1.-.-.-) rabbit domestic rabbit Oryctolagus cuniculus Yokotani, N. Bernhardt, R. Sogawa, K. Kusunose, E. Gotoh, O. Kusunose, M. Fujii-Kuriyama, Y. J. Biol. Chem. 264198921665-21669 Two forms of omega-hydroxylase toward prostaglandin A and laurate. cDNA cloning and their expression. MUID90094341 B34160 mRNA 1-511 GBM29530 NIDg164984 PIDNAAA31233.1 PIDg164985 GBJ05150 Johnson, E.F. Walker, D.L. Griffin, K.J. Clark, J.E. Okita, R.T. Muerhoff, A.S. Masters, B.S. Biochemistry 291990873-879 Cloning and expression of three rabbit kidney cDNAs encoding lauric acid omega-hydroxylases. MUID90254128 C34260 mRNA 1-98,'C',100-149,'F',151-391,'SK',394-476,'V',478-511 GBM28657 NIDg164978 PIDNAAA31231.1 PIDg164979 Yoshimura, R. Kusunose, E. Yokotani, N. Yamamoto, S. Kubota, I. Kusunose, M. J. Biochem. 1081990544-548 Purification and characterization of two forms of fatty acid omega-hydroxylase cytochrome P-450 from rabbit kidney cortex microsomes. MUID91154157 JN0090 protein 5-7,'X',9-15,'X',17-22,'X',24 kidney This protein catalyzes the omega- and (omega-1)-hydroxylation of fatty acids. human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 319-480 binding-site heme iron (Cys) (axial ligand) 458 predicted 511 complete MSVSALSSTRLPGSFSGFLQAAALLGLLLLLLKAAQLYLRRQWLLRALQQFPCPPSHWLL GHSREFPIDSELQQVLKRVEKFPSACPRWLWGSELFLIVYDPDYMKTILGRSDPKARVSY SFLAPWIGYGLLLLEGQTWFQHRRMLTPASHYDILKPYVGLMVDSVQVMLDKLEKLARKD APLEIYEHVSLMTLETIMKCAFSHQGSVQLESRTSKSYIQAVRELSDLALQRVRNVFHQS DFLYRLSPEGRLSHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAK MENGSSLSDQDLRAEVDTFMFEGHDTTASGISWIFYALATHPEHQHRCREEIQGLLGDGA SITWEHLDKMPYTTMCIKEALRLYPPVPGVGRQLSSPVTFPDGRSLPKGIIITLSIYGLH HNPKVWPNPEVFDPSRFAPGSARHSHAFLPFSGGSRNCIGKQFAMNELKVAVALTLLRFE LLPDPTRVPIPITRLVLKSKNGIHLRLRKLH
A34160 A34160 B34260 PQ0047 S23949 03-Dec-1999 03-Dec-1999 03-Mar-2000
laurate omega-hydroxylase (EC 1.14.15.3) cytochrome P450 4A6 cytochrome P450ka-1 cytochrome P450LPGA omega 1 rabbit domestic rabbit Oryctolagus cuniculus Yokotani, N. Bernhardt, R. Sogawa, K. Kusunose, E. Gotoh, O. Kusunose, M. Fujii-Kuriyama, Y. J. Biol. Chem. 264198921665-21669 Two forms of omega-hydroxylase toward prostaglandin A and laurate. cDNA cloning and their expression. MUID90094341 A34160 mRNA 1-510 GBM29531 NIDg164986 PIDNAAA31234.1 PIDg164987 GBJ05150 Johnson, E.F. Walker, D.L. Griffin, K.J. Clark, J.E. Okita, R.T. Muerhoff, A.S. Masters, B.S. Biochemistry 291990873-879 Cloning and expression of three rabbit kidney cDNAs encoding lauric acid omega-hydroxylases. MUID90254128 B34260 mRNA 1-423,'VW',426-434,'R',436-475,'V',477-510 GBM28656 Kikuta, Y. Kusunose, E. Okumoto, T. Kubota, I. Kusunose, M. J. Biochem. 1071990280-286 Purification and characterization of two forms of cytochrome P-450 with omega-hydroxylase activities toward prostaglandin A and fatty acids from rabbit liver microsomes. MUID90299866 PQ0047 protein 5-24 liver amino-terminal sequence Muerhoff, A.S. Griffin, K.J. Johnson, E.F. Arch. Biochem. Biophys. 296199266-72 Characterization of a rabbit gene encoding a clofibrate-inducible fatty acid omega-hydroxylase: CYP4A6. MUID92296782 S23949 DNA 1-26,'C',28-379,'M',381-423,'VW',426-434,'R',436-475,'V',477-510 This enzyme catalyzes the omega-hydroxylation of prostaglandin A1 and A2, as well as the omega- and (omega-1)-hydroxylation of fatty acid. CYP4A6 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 318-479 binding-site heme iron (Cys) (axial ligand) 457 predicted 510 complete MSVSALNPTRLPGSLSGLLQVAGLLGLLLLLLKAAQLYLHRQWLLRALQQFPCPPFHWLL GHSREFQNGHELQVMLKWVEKFPSACPRWLWGSRAHLLIYDPDYMKVILGRSDPKAQGSY RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVQIMLDKWEQLVSQD SSLEVFQDISLMTLDTIMKCAFSHQGSVQLDRNSQSYIQAVGDLNNLFFSRVRNVFHQSD TIYRLSPEGRLSHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAKM ENGSSLSDQDLRAEVDTFMFEGHDTTASGISWIFYALATHPEHQHRCREEIQGLLGDGAS ITWEHLDQMPYTTMCIKEALRLYPPVPGVGRQLSSPVTFPDGRSLPKGVIVTLSIYALHH NPKCGPNPEVFDPSPFAPGSARHSHAFLPFSGGPRNCIGKQFAMNELKVAVALTLLRFEL LPDPKRVPDQKPRLVLKSSNGIHLRLRKLR
A34260 A34260 S14761 03-Dec-1999 03-Dec-1999 03-Mar-2000
laurate omega-hydroxylase (EC 1.14.15.3) cytochrome P450 4A5 cytochrome P450kd rabbit domestic rabbit Oryctolagus cuniculus Johnson, E.F. Walker, D.L. Griffin, K.J. Clark, J.E. Okita, R.T. Muerhoff, A.S. Masters, B.S. Biochemistry 291990873-879 Cloning and expression of three rabbit kidney cDNAs encoding lauric acid omega-hydroxylases. MUID90254128 A34260 mRNA 1-511 GBM28655 Yokotani, N. Kusunose, E. Sogawa, K. Kawashima, H. Kinosaki, M. Kusunose, M. Fujii-Kuriyama, Y. Eur. J. Biochem. 1961991531-536 cDNA cloning and expression of the mRNA for cytochrome P-450(kd) which shows a fatty acid omega-hydroxylating activity. MUID91192021 S14761 mRNA 1-476,'L',478-511 EMBLX57209 NIDg1655 PIDNCAA40493.1 PIDg1656 CYP4A5 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein microsome monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 319-480 binding-site heme iron (Cys) (axial ligand) 458 predicted 511 complete MSVSALSPTRLPGSLSGLLQVAALLGLLLLLLKAAQLYLRRQWLLRALQQFPCPPFHWLL GHSREFQMNQELQQILKWVEKFPRACPHWIGGNKVRVQLYDPDYMKVILGRSDPKSRGSY TFVAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVGLMVDSVQIMLDKWEQLVSQD SSLEVFQDISLMTLDTIMKCAFSYQGSVQLDSRNSQSYIQAVGDLNNLVFARVRNIFHQS DTIYRLSPEGRLSHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAK MENGSSLSDQDLRAEVDTFMFEGHDTTASGVSWIFYALATHPEHQHRCREEIQGLLGDGA SITWEHLDQMPYTTMCIKEAMRLYPPVPAISRDLSSPVTFPDGRSLPKGFTVTLSIYGLH HNPNVWPNPEVFDPSRFTPGSARHSHAFLPFSGGARNCIGKQFAMNELKVAVALTLVRFE LLPDPTRIPKPTARLVLKSNNGIHLRLRKLQ
A36304 A36304 S08300 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 4A8 cytochrome P450 KP1 cytochrome P450K-4 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Stroemstedt, M. Hayashi, S.I. Zaphiropoulos, P.G. Gustafsson, J.A. DNA Cell Biol. 91990569-577 Cloning and characterization of a novel member of the cytochrome P450 subfamily IVA in rat prostate. MUID91103877 A36304 mRNA 1-508 GBM37828 NIDg203756 PIDNAAA63485.1 PIDg203757 kidney, prostate Imaoka, S. Nagashima, K. Funae, Y. Arch. Biochem. Biophys. 2761990473-480 Characterization of three cytochrome P450s purified from renal microsomes of untreated male rats and comparison with human renal cytochrome P450. MUID90165442 S08300 protein 8-12,'X',14-22 CYP4A8 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 316-477 binding-site heme iron (Cys) (axial ligand) 455 predicted 508 complete MSGSALSFTIFPGSILGFLQIATVLTVLLLLLKTAQFYLHRRWLLRATQQFPSPPSHWFF GHKIPKDQDFQDILTRVKNFPSACPQWLWGSNVRIQVYDPEYMKLILGRSDPKAHGSYRF LAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDTLKPYVGIMADSVRIMLDKWEQIVGQDST LEIFQHITLMTLDTIMKCAFSQEGSVQLDRKYKSYIKAVEDLNNLFFFRVQNMFHQNDFI YSLSSNGRKAHNAWQLAHDYTDQVIKSRKAQLQDEEELQKVKQKRRLDFLDILLFARIEN GSSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQGCRKEIQSLLGDGASIT WDDLDKMPYTTMCIKEALRIYPPVTAVSRMLSTPVTFPDGRSLPKGITVMLSFYGLHHNP TVWPNPEVFDPYRFAPESSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLP DPTRIPIPIPRLVLKSKNGIYLRLKKLQ
JE0361 JE0361 03-Dec-1999 03-Dec-1999 19-May-2000
cytochromes P450, CYP4T2 oxidoreductase (EC 1.-.-.-) European sea bass European sea bass Dicentrarchus labrax Sabourault, C. Berge, J.B. Lafaurie, M. Girard, J.P. Amichot, M. Biochem. Biophys. Res. Commun. 2511998213-219 Molecular cloning of a phthalate-inducible CYP4 gene (CYP4T2) in kidney from the sea bass, Dicentrarchus labrax. MUID99009248 JE0361 mRNA 1-515 GBAF045468 NIDg4091077 PIDNAAC98961.1 PIDg4091078 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 318-481 binding-site heme iron (Cys) (axial ligand) 459 predicted 515 complete MELTEAFLTLHWGLPRLHHLLALLCLVAVVYKLATLLAKRRDVFRSYEDFPGPPTHWLFG HVLEFKQDGTDFDTLMAWTKQYPYAFPLWFGPFFCVLNIHHPDYVKTILASTEPKDDVSY RFILSWIGEGLLVSSGQKWFRHRRFLTPGFHYDVLKPYVKLMSDSTKTMLDKWGSYANSN ESFELFQHVSLMTLDSILKCAFSYNSNCQTESGTNVYIKAVYELSDLINLRLRTFPYHSD LIFYLSPHGYRYRKAIKVAQSHTEEVIKKRKEALKEEKELDRIQAKKNLDFLNILLLARD EKQQGLSDEDIRAEVDTFMFEGHDTTASGISFILYSLACHPEHQKICRDEIMQVLDGKDT MDWEDLSKIPYTTMCIKESLRIYPPVPGMSRKITKPITFCDGRTLPEGSYIGTSVFGIHR NGIVWENPDVFDHWRFLPENVSKRSPHAFVPFSAGPRNCIGQNFAMNEMKVVIALTLKKY HLIEDPNWKPKIIPRLVLRSLNGIHIKIKPVDPQV
O4RTLO S01336 A26137 B32965 S21711 30-Sep-1991 30-Sep-1991 03-Mar-2000
laurate omega-hydroxylase (EC 1.14.15.3) cytochrome P450 4A1 cytochrome P450 LA-omega cytochrome P452 rat Norway rat Rattus norvegicus Earnshaw, D. Dale, J.W. Goldfarb, P.S. Gibson, G.G. FEBS Lett. 2361988357-361 Differential splicing in the 3'non-coding region of rat cytochrome P-452 (P450 IV A1) mRNA. MUID88312998 S01336 mRNA 1-509 EMBLX07259 NIDg56046 PIDNCAA30245.1 PIDg56047 Hardwick, J.P. Song, B.J. Huberman, E. Gonzalez, F.J. J. Biol. Chem. 2621987801-810 Isolation, complementary DNA sequence, and regulation of rat hepatic lauric acid omega-hydroxylase (cytochrome P-450-LA-omega). Identification of a new cytochrome P-450 gene family. MUID87109183 A26137 mRNA 1-509 GBM14972 NIDg203865 PIDNAAA41061.1 PIDg203866 Kimura, S. Hanioka, N. Matsunaga, E. Gonzalez, F.J. DNA 81989503-516 The rat clofibrate-inducible CYP4A gene subfamily I. Complete intron and exon sequence of the CYP4A1 and CYP4A2 genes, unique exon organization, and identification of a conserved 19-bp upstream element. MUID89356271 B32965 DNA 1-340,'E',342-509 EMBLM57718 NIDg203786 PIDNAAA41038.1 PIDg203787 Okita, R.T. Okita, J.R. Arch. Biochem. Biophys. 2941992475-481 Characterization of a cytochrome P450 from Di(2-ethylhexyl) phthalate-treated rats which hydroxylates fatty acids. MUID92231570 S21711 preliminary protein 1-22 strain Sprague-Dawley this sequence was confirmed by protein sequencing CYP4A1 63/3; 112/1; 127/1; 169/3; 211/2; 263/1; 298/3; 362/2; 407/1; 428/3; 454/2 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum fatty acid oxidation heme iron metalloprotein microsome monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 317-478 binding-site heme iron (Cys) (axial ligand) 456 predicted 509 complete MSVSALSSTRFTGSISGFLQVASVLGLLLLLVKAVQFYLQRQWLLKAFQQFPSPPFHWFF GHKQFQGDKELQQIMTCVENFPSAFPRWFWGSKAYLIVYDPDYMKVILGRSDPKANGVYR LLAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVKNMADSIRLMLDKWEQLAGQDS SIEIFQHISLMTLDTVMKCAFSHNGSVQVDGNYKSYIQAIGNLNDLFHSRVRNIFHQNDT IYNFSSNGHLFNRACQLAHDHTDGVIKLRKDQLQNAGELEKVKKKRRLDFLDILLLARME NGDSLSDKDLRAEVDTFMFEGHDTTASGVSWIFYALATHPKHQQRCREEVQSVLGDGSSI TWDHLDQIPYTTMCIKEALRLYPPVPGIVRELSTSVTFPDGRSLPKGIQVTLSIYGLHHN PKVWPNPEVFDPSRFAPDSPRHSHSFLPFSGGARNCIGKQFAMSEMKVIVALTLLRFELL PDPTKVPIPLPRLVLKSKNGIYLYLKKLH
A32966 A32966 A27700 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 4A3 cytochrome P450DM-2, streptozotocin-inducible, hepatic oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Kimura, S. Hardwick, J.P. Kozak, C.A. Gonzalez, F.J. DNA 81989517-525 The rat clofibrate-inducible CYP4A subfamily II. cDNA sequence of IVA3, mapping of the Cyp4a locus to mouse chromosome 4, and coordinate and tissue-specific regulation of the CYP4A genes. MUID89356272 A32966 mRNA 1-507 GBM33936 NIDg204989 PIDNAAA41458.1 PIDg204990 clofibrate-treated rat liver the authors translated the codon ACC for residue 215 as Tyr Imaoka, S. Shimojo, N. Funae, Y. Biochem. Biophys. Res. Commun. 1521988680-687 Induction of renal cytochrome P-450 in hepatic microsomes of diabetic rats. MUID88209045 A27700 protein 5-15,'X',17-19 amino-terminal sequence CYP4A3 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron liver metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 315-476 binding-site heme iron (Cys) (axial ligand) 454 predicted 507 complete MGFSVFTPTRSLDGVSGFFQGAFLLSLFLVLFKAVQFYLRRQWLLKALEKFPSTPSHWLW GHDLKDREFQQVLTWVEKFPGACLQWLSGSKTRVLLYDPDYVKVVLGRSDPKASGIYQFL APWIGYGLLLLNGKKWFQHRRMLTPAFHYGILKPYVKIMADSVNIMLDKWEKLDDQDHPL EIFHYVSLMTLDTVMKCAFSHQGSVQLDVNSRSYTKAVEDLNNLTFFRVRSAFYGNSIIY NMSSDGRLSRRACQIAHEHTDGVIKMRKAQLQNEEELQKARKKRHLDFLDILLFAKMEDG KSLSDEDLRAEVDTFMFEGHDTTASGISWVFYALATHPEHQERCREEVQSILGDGTSVTW DHLDQIPYTTMCIKEALRLYPPVPSVSRELSSPVTFPDGRSIPKGITTTILIYGLHHNPS YWPNPKVFDPSRFSPDSPRHSHAYLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPD PTRIPVPMARLVLKSKNGIHLRLKKLR
A32965 A32965 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 4A2 oxidoreductase (EC 1.-.-.-) rat Norway rat Rattus norvegicus Kimura, S. Hanioka, N. Matsunaga, E. Gonzalez, F.J. DNA 81989503-516 The rat clofibrate-inducible CYP4A gene subfamily I. Complete intron and exon sequence of the CYP4A1 and CYP4A2 genes, unique exon organization, and identification of a conserved 19-bp upstream element. MUID89356271 A32965 DNA 1-504 EMBLM57719 NIDg203788 PIDNAAA41039.1 PIDg203789 CYP4A2 65/3; 110/1; 122/1; 164/3; 206/2; 258/1; 293/3; 357/2; 402/1; 423/3; 449/2 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum fatty acid oxidation heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 312-473 binding-site heme iron (Cys) (axial ligand) 451 predicted 504 complete MGFSVFSPTRSLDGVSGFFQGAFLLSLFLVLFKAVQFYLRRQWLLKALEKFPSTPSHWLW GHNLKDREFQQVLTWVEKFPGACLQWLSGSTARVLLYDPDYVKVVLGRSDPKPYQSLAPW IGYGLLLLNGKKWFQHRRMLTPAFHYDILKPYVKIMADSVSIMLDKWEKLDDQDHPLEIF HYVSLMTLDTVMKCAFSHQGSVQLDVNSRSYTKAVEDLNNLIFFRVRSAFYGNSIIYNMS SDGRLSRRACQIAHEHTDGVIKTRKAQLQNEEELQKARKKRHLDFLDILLFAKMEDGKSL SDEDLRAEVDTFMFEGHDTTASGISWVFYALATHPEHQERCREEVQSILGDGTSVTWDHL DQMPYTTMCIKEALRLYSPVPSVSRELSSPVTFPDGRSIPKGIRVTILIYGLHHNPSYWP NPKVFDPSRFSPDSPRHSHAYLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTR IPVPMPRLVLKSKNGIHLRLKKLR
A46661 A46661 10-Sep-1999 10-Sep-1999 21-Jul-2000
leukotriene B4 omega-hydroxylase (EC 1.14.15.-) cytochrome P450 human man Homo sapiens Kikuta, Y. Kusunose, E. Endo, K. Yamamoto, S. Sogawa, K. Fujii-Kuriyama, Y. Kusunose, M. J. Biol. Chem. 26819939376-9380 A novel form of cytochrome P-450 family 4 in human polymorphonuclear leukocytes. cDNA cloning and expression of leukotriene B4 omega-hydroxylase. MUID93252801 A46661 preliminary DNA mRNA 1-520 GBAB002454 NIDg3123722 PIDNBAA25990.1 PIDg3123723 GBAB002461 NIDg3126633 PIDNBAA25991.1 PIDg3126635 GBD12620 NIDg391715 PIDNBAA02144.1 PIDg391716 polymorphonuclear leukocytes sequence extracted from NCBI backbone (NCBIN:131350, NCBIP:131351) GDBLTB4H GDBCYP4F3 GDB139142 OMIM601270 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer fatty acid oxidation heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 325-490 binding-site heme iron (Cys) (axial ligand) 468 predicted 520 complete MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWF LGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPK DKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQL LASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQIL LYIDFLYYLTPDGQRFRRACRLVHDFTDDVIQERRRTLPSQGVDDFLQAKAKSKTLDFID VLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQE LLKDREPKEIEWDDLAQLPFLTMCIKESLRLHPPVPAVSRCCTQDIVLPDGRVIPKGIIC LISVFGTHHNPAVWPDPEVYDPFRFDPKNIKERSPLAFIPFSAGPRNCIGQAFAMAEMKV VLGLTLLAFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS
A39381 A39381 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 4 oxidoreductase (EC 1.-.-.-) cockroach (Blaberus discoidalis) Blaberus discoidalis Bradfield, J.Y. Lee, Y.H. Keeley, L.L. Proc. Natl. Acad. Sci. U.S.A. 8819914558-4562 Cytochrome P450 family 4 in a cockroach: molecular cloning and regulation by hypertrehalosemic hormone. MUID91239607 A39381 preliminary DNA 1-511 GBM63798 NIDg155946 PIDNAAA27819.1 PIDg155947 the authors translated the codon CAG for residue 23 as Ser, and TTT for residue 170 as Glu CYP4C1 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 311-474 binding-site heme iron (Cys) (axial ligand) 452 predicted 511 complete MEFITILLSTALFIVTFLFLFRQGAKRARFVYLVNKLPGPTAYPVVGNAIEAIVPRNKLF QVFDRRAKLYGPLYRIWAGPIAQVGLTRPEHVELILRDTKHIDKSLVYSFIRPWLGEGLL TGTGAKWHSHRKMITPTFHFKILDIFVDVFVEKSEILVKKLQSKVGGKDFDIYPFITHCA LDIICETAMGIQMNAQEESESEYVKAVYEISELTMQRSVRPWLHPKVIFDLTTMGKRYAE CLRILHGFTNKVIQERKSLRQMTGMKPTISNEEDELLGKKKRLAFLDLLLEASENGTKMS DTDIREEVDTFMFEGHDTTSAGICWALFLLGSHPEIQDKVYEELDHIFQGSDRSTTMRDL ADMKYLERVIKESLRLFPSVPFIGRVLKEDTKIGDYLVPAGCMMNLQIYHVHRNQDQYPN PEAFNPDNFLPERVAKRHPYAYVPFSAGPRNCIGQKFATLEEKTVLSSILRNFKVRSIEK REDLTLMNELILRPESGIKVELIPRLPADAC
S66374 S66374 S66477 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 4M2 oxidoreductase (EC 1.-.-.-) tobacco hornworm tobacco hornworm Manduca sexta Snyder, M.J. Stevens, J.L. Andersen, J.F. Feyereisen, R. Arch. Biochem. Biophys. 321199513-20 Expression of cytochrome P450 genes of the CYP4 family in midgut and fat body of the tobacco hornworm, Manduca sexta. MUID95366751 S66374 mRNA 1-503 GBL38671 NIDg3207185 PIDNAAC21661.1 PIDg3207186 S66477 nucleic acid sequence not shown mRNA 313-444 EMBLL38671 NIDg606409 PIDg606410 fat body and midgut CYP4M2 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 305-468 binding-site heme iron (Cys) (axial ligand) 446 predicted 503 complete MFVIIAIFALFLCLIHILFNNNKKARLLKQIPGSKYNFIIGNALDFLKSPEQLFYFMREY YETWKPLNRFWAFQIAFVNVYEPHDIEVVISSTKHNAKSPPYYFLKNWLRDGLLLSKGPK WQSRRKILTPTFHFNILRQFCGILEDNSERLVQNVGKSLGKPVNIIPTISEYTLYSICET AMGSRLGEESKESQKSYKQSICALGRQFVYRITRIYLHSDFIYNLITFGKVKKDLDVVHN FTTKVIKDRKEYVEKYGINMFGVSDIDDNNVYKKNKKIAMLDLLITAQKEGFIDDIGIQE EVDTFMFEGHDTIALALTYTLMLLANHRSIQHTVIAEIDEIFGDSERQADLDDLSKMRYL ERCIKESLRLYPPVPAIGRLLSEDVTLSGYRVPEGAYCHIQCFDLHRRGDLYKDPLVFDP DRFLPENCSDRHPYAYIPFSAGPRNCIGQKFAILEMKSAISSLLRHYELLPVTKPEDLKF TADLVLRTTNPVYVKFVKKEKNK
S25707 S25707 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 4D1 oxidoreductase (EC 1.-.-.-) fruit fly (Drosophila melanogaster) Drosophila melanogaster Gandhi, R. Varak, E. Goldberg, M.L. DNA Cell Biol. 111992397-404 Molecular analysis of a cytochrome P450 gene of family 4 on the Drosophila X chromosome. MUID92297166 S25707 preliminary mRNA 1-511 EMBLX67645 NIDg7790 PIDNCAA47887.1 PIDg7791 Cyp4d1 FlyBaseFBgn0005670 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 313-478 binding-site heme iron (Cys) (axial ligand) 456 predicted 511 complete MFLVIGAILASALFVGLLLYHLKFKRLIDLISYMPGPPVLPLVGHGHHFIGKPPHEMVKK IFEFMETISKDQVLKVWLGPELNVLMGNPKDVEVVLGTLRFNDKAGEYKALEPWLKEGLL VSRGRKWHKRRKIITPAFHFKILDQFVEVFEKGSRDLLRNMEQDRLKHGDSGFSLYDWIN LCTMDTICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLTYMLTPLARA EKKALNVLHQFTEKIIVQRREELIREGSSQESSNDDADVGAKRKMAFLDILLQSTVDERP LSNLDIREEVDTFMFKGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSY ELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREEL FSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKPSWPMCSGTTRLT LWATSFGTTRADRRTYSAYQGPLSSRCGRVY
S41192 S41192 S34291 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 4D2 oxidoreductase (EC 1.-.-.-) fruit fly (Drosophila melanogaster) Drosophila melanogaster Frolov, M.V. Alatortsev, V.E. submitted to the EMBL Data Library December1993 A cluster of cytochrome P450 genes in the X-chromosome of Drosophila melanogaster. S41192 DNA 1-496 EMBLX75955 NIDg439650 PIDNCAA53568.1 PIDg439651 strain Oregon R Frolov, M.V. Alatortsev, V.E. submitted to the EMBL Data Library June1993 Cluster of cytochrome P-450 genes on the X-chromosome in Drosophila melanogaster. S34291 DNA 'A',31-496 EMBLZ23005 NIDg312903 PIDNCAA80549.1 PIDg312904 strain Oregon R Cyp4d2 FlyBaseFBgn0011576 X 53/1; 182/1; 205/2; 392/1 human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 308-471 binding-site heme iron (Cys) (axial ligand) 449 predicted 496 complete MLGVVGVLLLVAFATLLLWDFLWRRRGNGILPGPRPLPFLGNLLMYRGLDPEQIMDFVKK NQRKYGRLYRVWILHQLAVFSTDPRDIEFVLSSQQHITKNNLYKLLNCWLGDGLLMSTGR KWHGRRKIITPTFHFKILEQFVEIFDQQSAVMVEQLQSRRDGMTPINIFPVICLTALDII AETAMGTKINAQKNPNLPYVQAVNDVTNILIKRFIHAWQRVDWIFRLTQPTEAKRQDKAI KVMHDFTENIIRERRETLVNNSKETTPEEEVNFLGQKRRMALLDVLLQSTIDGAPLSDED IREEVDTFMFEGHDTTTSAISFCLYEISRHPEVQQRLQQEIRDVLGEDRKSPVTLRDLGE LKFMENVIKESLRLHPPVPMIGRWFAEDVEIRGKHIPAGTNFTMGIFVLLRDPEYFESPD EFRPERFDADVPQIHPYAYIPFSAGPRNCIGQKFAMLEMKSTVSKLLRHFELLPLGPEPR HSMNIVCGRPTAFILA
JC5236 JC5236 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450, Cyp4e2 oxidoreductase (EC 1.-.-.-) fruit fly (Drosophila melanogaster) Drosophila melanogaster Pittendrigh, B.R. Mocelin, G. Andreev, O. ffrench-Constant, R.H. Gene 1791996295-296 The sequence of a Drosophila Cyp4e2 cytochrome P450-encoding cDNA. MUID97128322 JC5236 preliminary mRNA 1-485 GBU56957 NIDg1480636 PIDNAAC47424.1 PIDg1480637 embryo This protein lacks the hydrophobic amino-terminus, typical of microsomal cytochrome P450, and contains a small insertion at the carboxyl-terminus. human cytochrome P450 CYP4B1 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 263-425 binding-site heme iron (Cys) (axial ligand) 403 predicted 485 complete MGNAHQMGKNPSEILDTVFSWWHQYGKDNFVFWIGTYSNVLVTSSKYLEFILSSQTLITK SDIYQLTHPWLGLGLLTSTGSKWHKHRKMITPAFHFNILQDFHEVMNENSTKFIKHLKTV AAGDNIFDFQEQAHYLTLDVICDTAMGVSINAMENRSSSIVQAFKDMCYNINMRAFHPLK RNELLYRLAPDYPAYSRTLKTLQDFTNEIIAKRIEAHKSGAVSTNAGDEFTRKKMAFLDT LLSSTIDGRPLNSKELYEEVSTFMFEGHDTTTSGVSFAVYLLSRHQDEQRKLFKEQREVM GNSELGRDATFQEISQMKYLDLFIKEAQRVYPSVPFIGRFTEKDYVIDGDLVPKGTTLNL GLVMLGYNEKVFKDPHKFRPERFELEKPGPFEYVPFSAGPRNCIGQKFALLEIKTVVSKI IRNFEVLPALDELVSKDGYISTTIGLPDAERKKRDPYRHKYDPILSAVLTLKSENGLYIR LKERH
A34101 A34101 S06491 I52302 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 3A5 cytochrome P450 HLp2 oxidoreductase (EC 1.-.-.-) human man Homo sapiens Aoyama, T. Yamano, S. Waxman, D.J. Lapenson, D.P. Meyer, U.A. Fischer, V. Tyndale, R. Inaba, T. Kalow, W. Gelboin, H.V. Gonzalez, F.J. J. Biol. Chem. 264198910388-10395 Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine. MUID89278095 A34101 mRNA 1-502 GBJ04813 NIDg181345 PIDNAAA02993.1 PIDg181346 Schuetz, J.D. Molowa, D.T. Guzelian, P.S. Arch. Biochem. Biophys. 2741989355-365 Characterization of a cDNA encoding a new member of the glucocorticoid-responsive cytochromes P450 in human liver. MUID90025114 S06491 not compared with conceptual translation mRNA 1-304,'P',306-317,'F',319-323,'D',325-376,'G',378-502 Jounaidi, Y. Guzelian, P.S. Maurel, P. Vilarem, M.J. Biochem. Biophys. Res. Commun. 20519941741-1747 Sequence of the 5'-flanking region of CYP3A5: comparative analysis with CYP3A4 and CYP3A7. MUID95110318 I52302 translated from GB/EMBL/DDBJ DNA 1-24 GBS74699 NIDg786472 PIDNAAD14157.1 PIDg4261857 GDBCYP3A5 GDB118783 7q22.1-7q22.1 human cytochrome P450 CYP3A5 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 302-463 binding-site heme iron (Cys) (axial ligand) 441 predicted 502 complete MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG LLQPEKPIVLKVDSRDGTLSGE
S48161 S48161 10-Sep-1999 10-Sep-1999 21-Jul-2000
thromboxane-A synthase (EC 5.3.99.5) human man Homo sapiens Miyata, A. Yokoyama, C. Ihara, H. Bandoh, S. Takeda, O. Takahashi, E. Tanabe, T. Eur. J. Biochem. 2241994273-279 Characterization of the human gene (TBXAS1) encoding thromboxane synthase. MUID95010003 S48161 preliminary mRNA 1-533 GBD34625 NIDg559364 GDBTBXAS1 GDBCYP5 GDB128744 OMIM274180 7q34-7q35 human cytochrome P450 CYP3A5 cytochrome P450 homology chromoprotein heme intramolecular oxidoreductase iron isomerase metalloprotein domain cytochrome P450 homology 338-501 binding-site heme iron (Cys) (axial ligand) 479 predicted 533 complete MEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFFR QGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKSV ADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQR CYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPLA RILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQIVLDARHSASPMGVQDFDIV RDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLATN PDCQEKLLREVDVFKEKHMAPEFCGLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCEV LGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERFTAEARQQHRPFTYLPFGAGPRSCL GVRLGLLEVKLTLLHVLHKFRFQACPETQVPLQLESKSALGPKNGVYIKIVSR
A32157 A32157 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 6 oxidoreductase (EC 1.-.-.-) house fly house fly Musca domestica Feyereisen, R. Koener, J.F. Farnsworth, D.E. Nebert, D.W. Proc. Natl. Acad. Sci. U.S.A. 8619891465-1469 Isolation and sequence of cDNA encoding a cytochrome P-450 from an insecticide-resistant strain of the house fly, Musca domestica. MUID89160799 A32157 mRNA 1-509 GBM25367 CYP6A1 human cytochrome P450 CYP3A5 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 302-471 binding-site heme iron (Cys) (axial ligand) 449 predicted 509 complete MDFGSFLLYALGVLASLALYFVRWNFGYWKRRGIPHEEPHLVMGNVKGLRSKYHIGEIIA DYYRKFKGSDPLPGIFLGHKPAAVVLDKELRKRVLIKDFSNFANRGLYYNEKDDPLTGHL VMVEGEKWRSLRTKLSPTFTAGKMKYMYNTVLEVGQRLLEVMYEKLEVSSELDMRDILAR FNTDVIGSVAFGIECNSLRNPHDRFLAMGRKSIEVPRHNALIMAFIDSFPELSRKLGMRV LPEDVHQFFMSSIKETVDYREKNNIRRNDFLDLVLDLKNNPESISKLGGLTFNELAAQVF VFFLGGFETSSSTMGFALYELAQNQQLQDRLREEVNEVFDQFKEDNISYDALMNIPYLDQ VLNETLRKYPVGVGSALTRQTLNDYVVPHNPKYVLPKGTLVFIPVLGIHYDPELYPNPEE FDPERFSPEMVKQRDSVDWLGFGDGPRNCIGMRFGKMQSRLGLALVIRHFRFTVCSRTDI PMQINPESLAWTPKNNLYLNVQAIRKKIK
A47198 A45378 A47198 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 6A2 cytochrome P450-B1 oxidoreductase (EC 1.-.-.-) fruit fly (Drosophila melanogaster) Drosophila melanogaster Waters, L.C. Zelhof, A.C. Shaw, B.J. Ch'ang, L.Y. Proc. Natl. Acad. Sci. U.S.A. 8919924855-4859 Possible involvement of the long terminal repeat of transposable element 17.6 in regulating expression of an insecticide resistance-associated P450 gene in Drosophila. MUID92279225 A45378 DNA mRNA 1-82,'FFMRLVNDTIALRERENFKRNDFMNI',83-90,'HQ',93-246,273-507 GBM88009 NIDg157165 strain 91-C, insecticide susceptible strain sequence inconsistent with the nucleotide translation sequence extracted from NCBI backbone (NCBIN:104184, NCBIP:104179) this sequence has been corrected in A47198 Waters, L.C. Zelhof, A.C. Shaw, B.J. Ch'ang, L.Y. Proc. Natl. Acad. Sci. U.S.A. 89199212209 "Possible involvement of the long terminal repeat of transposable element 17.6 in regulating expression of an insecticide resistance-associated P450 gene in Drosophila." MUID93101696 A47198 DNA mRNA 1-507 GBS51248 NIDg261816 PIDNAAB24525.1 PIDg261817 sequence extracted from NCBI backbone (NCBIN:120806, NCBIP:120807) Cyp6a2 FlyBaseFBgn0000473 absent human cytochrome P450 CYP3A5 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome P450 homology 308-474 binding-site heme iron (Cys) (axial ligand) 452 predicted 507 complete MFVLIYLLIAISSLLAYLYHRNFNYWNRRGLPHDAPHPLYGNMVGFRKNRVMHDFFYDYY NKYRKSGFPFVGFYFLHKPAAFIVDTQLAKNILIKDFSNFADRGQFHNGRDDPLTQHLFN LDGKKWKDMRQRLTPTFTSGKMKFMFPTVIKVSEEFVKVITEQVPAAQNGAVLEIKELMA RFTTDVIGTCRFGIECNTLRTPVSDFRTMGQKVFTDMRHGKLLTMFVFSFPKLASRLRMR MMPEDVHQFFMRLVNDTIALRERENFKRNDFMNLLIELKQKGSSFTLDNGEVIEGMDIGE LAAQVFVFYVAGFETSSSTMSYCLYELAQNQDIQDRLRNEIQTVLEEQEGQLTYESIKAM TYLNQVISETLRLYTLVPHLERKALNDYVVPGHEKLVIEKGTQVIIPACAYHRDEDLYPN PETFDPERFSPEKVAARESVEWLPFGDGPRNCIGMRFGQMQARIGLAQIISRFRVSVCDT TEIPLKYSPMSIVLGTVGGIYLRVERI
S48058 S48058 A46367 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 CYP6B1 oxidoreductase (EC 1.-.-.-) black swallowtail black swallowtail Papilio polyxenes Prapaipong, H. Berenbaum, M.R. Schuler, M.A. Nucleic Acids Res. 2219943210-3217 Transcriptional regulation of the Papilio polyxenes CYP6B1 gene. MUID94344788 S48058 preliminary DNA 1-498 EMBLZ29624 NIDg520879 PIDNCAA82732.1 PIDg520880 Cohen, M.B. Schuler, M.A. Berenbaum, M.R. Proc. Natl. Acad. Sci. U.S.A. 89199210920-10924 A host-inducible cytochrome P-450 from a host-specific caterpillar: molecular cloning and evolution. MUID93066355 A46367 preliminary mRNA protein 1-23,'N',25-154,'NS',157-498 GBM80828 NIDg160763 PIDNAAA29789.1 PIDg160764 sequence extracted from NCBI backbone (NCBIN:118719, NCBIP:118720) 445/1 human cytochrome P450 CYP3A5 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 300-465 binding-site heme iron (Cys) (axial ligand) 443 predicted 498 complete MLYLLALVTVLAGLLHYYFTRTFDYWKKRNVAGPKPVPFFGNLKDSVLRRKPQVMVYKSI YDEFPNEKVVGIYRMTTPSVLLRDLDIIKHVLIKDFESFADRGVEFSLDGLGANIFHADG DRWRSLRNRFTPLFTSGKLKSMLPLMSQVGDRFIKCIDEVSQTQPEQSIHNLVQKFTMTN IAACVFGLNLDEGMLKTLEDLDKHIFTVNYSAELDMMYPGILKKLNGSLFPKVVSKFFDN LTKNVLEMRKGTPSYQKDMIDLIQELREKKTLELSRKHENEDVKALELTDGVISAQMFIF YMAGYETSATTMTYLFYELAKNPDIQDKLIAEIDEVLSRHDGNITYECLSEMTYLSKVFD ETLRKYPVADFTQRNAKTDYVFPGTDITIKKGQTIIVSTWGIQNDPKYYPNPEKFDPERF NPENVKDRHPCAYLPFSAGPRNCLGMRFAKWQSEVCIMKVLSKYRVEPSMKSSGPFKFDP MRLFALPKGGIYVNLVRR
S57337 S57337 10-Sep-1999 10-Sep-1999 21-Jul-2000
trichodiene oxygenase (EC 1.14.-.-) cytochrome P450 CYP58 TRI4 protein fungus (Fusarium sporotrichioides) Fusarium sporotrichioides Hohn, T.M. Desjardins, A.E. McCormick, S.P. Mol. Gen. Genet. 248199595-102 The Tri4 gene of Fusarium sporotrichioides encodes a cytochrome P450 monooxygenase involved in trichothecene biosynthesis. MUID95379755 S57337 preliminary DNA 1-520 EMBLU22462 NIDg837031 PIDNAAB72032.1 PIDg837032 the authors did not translate the codon for residue 101 tri4 82/1; 403/3; 459/2 Fusarium trichodiene oxygenase 4 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 311-477 binding-site heme iron (Cys) (axial ligand) 455 predicted 520 complete MVDQDWIKALVNIPISHAVGVVAASTVIYFLSSCFYNLYLHPLRKIPGPKLAAIGPYLEF YHEVIRDGQYLWEIAKMHDKYGPIVRVNDKEVHIRDPSYYSTIYTAGARKTNKDPATVGA FDVPTATAATVDHDHHRARRGYLNPYFSKRSITNLEPFIHERVTKLLSRFQEHLDNDQVL SLDGAFCALTADVITSRFYGKHYNYLDLPDFHFVVRDGFLGLTKVYHLARFIPVLVTVLK RLPYSCLRLIAPSVSDLLQMRNEIHERGGDEFLSSKTSEAKSSILFGALADTHIPPVERT VERMLDEGTVILFAGTETTSRTLAITFFYLLTHPECLRKLREELNSLPKVEGDRFPLATL ENLPYLNGVVHEGFRLACGPISRSGRVATQENLKYKEHVIPAGTPVSQSTYFMHTDPKIF PEPEKFKPERWIEAAEKKIPLKKYITNFSQGSRQCIGYTMAFAEMYLAMSRIARAYDVEL YDTTKADIDMTHARIVAYPKAIPGKTEHVGEIRVKVLKAL
B36395 B36395 S14228 S69684 S13502 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 56 protein YDR402c spore wall maturation protein DIT2 oxidoreductase (EC 1.-.-.-) yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Briza, P. Breitenbach, M. Ellinger, A. Segall, J. Genes Dev. 419901775-1789 Isolation of two developmentally regulated genes involved in spore wall maturation in Saccharomyces cerevisiae. MUID91065523 B36395 DNA 1-489 EMBLX55713 Segall, J. submitted to the EMBL Data Library October1990 S14228 DNA 1-444,'I',446-489 EMBLX55713 NIDg3655 PIDNCAA39246.1 PIDg3656 Dietrich, F.S. submitted to the EMBL Data Library July1995 The sequence of S. cerevisiae cosmids 9481, 9509, 9926, 9461, and lambda 3641. S69684 DNA 1-489 EMBLU32274 NIDg927313 PIDNAAB64842.1 PIDg927333 GSPDBGN00004 MIPSYDR402c DIT2 CYP56 MIPSYDR402c 4R probably involved in dityrosine biosynthesis yeast cytochrome P450 CYP56 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 8-24 predicted domain transmembrane 33-49 predicted domain cytochrome P450 homology 290-457 binding-site heme iron (Cys) (axial ligand) 435 predicted 489 complete MELLKLLCLILFLTLSYVAFAIIVPPLNFPKNIPTIPFYVVFLPVIFPIDQTELYDLYIR ESMEKYGAVKFFFGSRWNILVSRSEYLAQIFKDEDTFAKSGNQKKIPYSALAAYTGDNVI SAYGAVWRNYRNAVTNGLQHFDDAPIFKNAKILCTLIKNRLLEGQTSIPMGPLSQRMALD NISQVALGFDFGALTHEKNAFHEHLIRIKKQIFHPFFLTFPFLDVLPIPSRKKAFKDVVS FRELLVKRVQDELVNNYKFEQTTFAASDLIRAHNNEIIDYKQLTDNIVIILVAGHENPQL LFNSSLYLLAKYSNEWQEKLRKEVNGITDPKGLADLPLLNAFLFEVVRMYPPLSTIINRC TTKTCKLGAEIVIPKGVYVGYNNFGTSHDPKTWGTTADDFKPERWGSDIETIRKNWRMAK NRCAVTGFHGGRRACLGEKLALTEMRISLAEMLKQFRWSLDPEWEEKLTPAGPLCPLNLK LKFNENIME
S45583 S45583 10-Sep-1999 10-Sep-1999 03-Mar-2000
pisatin demethylase (EC 1.14.-.-) cytochrome P450 CYP57 PDAT9 protein fungus (Nectria haematococca) Nectria haematococca Maloney, A.P. VanEtten, H.D. Mol. Gen. Genet. 2431994506-514 A gene from the fungal plant pathogen Nectria haematococca that encodes the phytoalexin-detoxifying enzyme pisatin demethylase defines a new cytochrome P450 family. MUID94268495 S45583 DNA 1-515 EMBLL20976 NIDg309579 PIDNAAC01762.1 PIDg487426 PDAT9 84/1; 200/3; 402/3; 445/3 pisatin demethylase cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 312-475 binding-site heme iron (Cys) (axial ligand) 453 predicted 515 complete MLVDTGLGLISELQAKLGWAVLLQIVPITIVAYNLLWFIYASFFSSLRKIPGPFLARISR VWEMKKTATGNIHEIMMDLHRRHGAIVRIGPRRYDFDTMEALKIIYRIGNALPKADYYKP FGLPSFPNLFDEQNPARHSAIKKQVASLYTMTALLSYEEGVDGQTAILKEQLQRFCDQKQ VIDLPRFLQYYAFDVIGVITVGKSMGMMESNSDTNGACSALDGMWHYASMMAYIPNMHAW WLRLSSLLPIEVPIKGLTEYVERRIIQYRLKAAEFGDDAALKGENNFLAKLLLMEKKGTV TPVETQQAVGLNIGAGSDTTANALSTILYYLYTNPRTLHTLREELERYVKDGPISFQQSQ SMPYLQAVIKEALRLHPGVGTQLTRVVPKGGLVIEGQFFPEGTEVGVNGWALYHNKAIFG NDASIFRPERWLEANENINIGGSFAFGAGSRSCIGKNISILEMSKAIPQIVRNFDIEINH GDMTWKNECWWFVKPEYKAMIKPRRCCLSRDESLV
S34286 S34286 03-Dec-1999 03-Dec-1999 03-Mar-2000
pisatin demethylase PDA6-1 oxidoreductase (EC 1.-.-.-) fungus (Nectria haematococca) Nectria haematococca Reimmann, C. van Etten, H.D. submitted to the EMBL Data Library June1993 Cloning and characterization of PDA6-1 a fungal gene encoding a cytochrome P-450 which can detoxify the phytoalexin pisatin from garden pea. S34286 DNA 1-506 EMBLX73145 NIDg312163 PIDNCAA51665.1 PIDg312164 84/1; 200/3; 402/3; 445/3 pisatin demethylase cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 312-475 binding-site heme iron (Cys) (axial ligand) 453 predicted 506 complete MLVDTGLGLISELRARLGWAALLQIVPVTVVAYNLLWFIYTSFFSSLRKIPGPFLARISR VWEIKKAATGNIHEIVMDLHRCHGPIVRIGPNRYDFDTMEALKIIYRIGNALPKADYYIP FGLPSSPNLFDVQNPARHSAMKKQVASLYTMTALLSYEAGVDGQTIILKEQLQRFCDQKQ VIDLPQFLQYYAFDVIGVITVGKSMGMMETNSDTNGACGALDAMWHYSSMMAFIPHMHAW WLRLSSLLPIDVPIKGLTEYVEQRIIQYRLKAAEFGDDDALKGENNFLAKLILMERQGTV TSTETQQAVGLNIGAGSDTTANALSSILYFLYTNPRTLRRLREELDTHVKEDPIRFQQSQ SMPYLQAVIKEALRLHPGVGTQLTRVVPKGGLVIEGQFFPEGAEVGVNGWALYHNKAIFG NDASVFRPERWLETKGNLNIGGSFAFGAGSRSCIGKNISILEMSKAIPQIVRNFDIEINH GDMTWKNECWWFVKPEYKAMIKPRAA
S12015 S12015 S10453 03-Dec-1999 03-Dec-1999 03-Mar-2000
benzoate 4-monooxygenase (EC 1.14.13.12) cytochrome P450 53 benzoate-para-hydroxylase Aspergillus niger Aspergillus niger van Gorcom, R.F.M. Boschloo, J.G. Kuijvenhoven, A. Lange, J. van Vark, A.J. Bos, C.J. van Balken, J.A.M. Pouwels, P.H. van den Hondel, C.A.M.J.J. Mol. Gen. Genet. 2231990192-197 Isolation and molecular characterisation of the benzoate-para-hydroxylase gene (bphA) of Aspergillus niger: a member of a new gene family of the cytochrome P450 superfamily. MUID91066829 S12015 DNA 1-517 EMBLX52521 NIDg2336 PIDNCAA36753.1 PIDg295920 bphA 1 100/2 pisatin demethylase cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 1-21 predicted domain cytochrome P450 homology 315-483 binding-site heme iron (Cys) (axial ligand) 461 predicted 517 complete MLALLLSPYGAYLGLALLVLYYLLPYLKRAHLRDIPAPGLAAFTNFWLLLQTRRGHRFVV VDNAHKKYGKLVRIAPRHTSIADDGAIQAVYGHGNGFLKSDFYDAFVSIHRGLFNTRDRA EHTRKRKTVSHTFSMKSIGQFEQYIHGNIELFVKQWNRMADTQRNPKTGFASLDALNWFN YLAFDIIGDLAFGAPFGMLDKGKDFAEMRKTPDSPPSYVQAVEVLNRRGEVSATLGCYPA LKPFAKYLPDSFFRDGIQAVEDLAGIAVARVNERLRPEVMANNTRVDLLARLMEGKDSNG EKLGRAELTAEALTQLIAGSDTTSNTSCAILYWCMRTPGVIEKLHKALDEAIPQDVDVPT HAMVKDIPYLQWVIWETMRIHSTSAMGLPREIPAGNPPVTISGHTFYPGDVVSVPSYTIH RSKEIWGPDAEQFVPERWDPARLTPRQKAAFIPFSTGPRACVGRNVAEMELLVICGTVFR LFEFEMQQEGPMETREGFLRKPLGLQVGMKRRQPGSA
O4CKA3 B56578 JU0095 JQ1040 A33254 S65522 S50815 S08667 31-Mar-1992 31-Mar-1992 03-Nov-2000
cytochrome P450 52A3-a cytochrome P450, alkane-inducible cytochrome P450-cm1 oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Schunck, W.H. Vogel, F. Gross, B. Kargel, E. Mauersberger, S. Kopke, K. Gengnagel, C. Muller, H.G. Eur. J. Cell Biol. 551991336-345 Comparison of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum. MUID92037671 B56578 nucleic acid sequence not shown mRNA 1-523 EMBLX51931 NIDg2607 PIDNCAA36197.1 PIDg2608 strain EH15D submitted to the EMBL Data Library, February 1990 Takagi, M. Ohkuma, M. Kobayashi, N. Watanabe, M. Yano, K. Agric. Biol. Chem. 5319892217-2226 Purification of cytochrome P-450alk from n-alkane-grown cells of Candida maltosa, and cloning and nucleotide sequencing of the encoding gene. JU0095 mRNA 1-20,'L',22-51,'E',53-146,'L',148-523 DDBJD00481 NIDg218379 PIDNBAA00371.1 PIDg218380 strain IAM12247 parts of this sequence, including the amino end of the mature protein, were determined by protein sequencing Ohkuma, M. Hikiji, T. Tanimoto, T. Schunck, W.H. Mueller, H.G. Yano, K. Takagi, M. Agric. Biol. Chem. 5519911757-1764 Evidence that more than one gene encodes n-alkane-inducible cytochrome P-450s in Candida maltosa, found by two-step gene disruption. MUID92109967 JQ1040 DNA 1-20,'L',22-51,'E',53-146,'L',148-523 DDBJD12475 NIDg218377 strain CHA1, gene a Schunck, W.H. Kaergel, E. Gross, B. Wiedmann, B. Mauersberger, S. Koepke, K. Kiessling, U. Strauss, M. Gaestel, M. Mueller, H.G. Biochem. Biophys. Res. Commun. 1611989843-850 Molecular cloning and characterization of the primary structure of the alkane hydroxylating cytochrome P-450 from the yeast Candida maltosa. MUID89286595 A33254 mRNA 1-216,'S',218-220,223-230,'VR',233-523 GBM27081 NIDg553117 PIDNAAA34320.1 PIDg553118 strain EH-15 Scheller, U. Zimmer, T. Kaergel, E. Schunck, W.H. Arch. Biochem. Biophys. 3281996245-254 Characterization of the n-alkane and fatty acid hydroxylating cytochrome P450 forms 52A3 and 52A4. MUID96213873 S65522 protein 2-21 Sugiyama, H. Ohkuma, M. Masuda, Y. Park, S.M. Ohta, A. Takagi, M. Yeast 11199543-52 In vivo evidence for non-universal usage of the codon CUG in Candida maltosa. MUID95282512 S50815 preliminary protein 2-8 Cytochromes P450 are heme-containing monooxygenases that catalyze diverse oxidative reactions in the metabolism of a number of endogenous and xenobiotic compounds. CYP52A3-a Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein product cytochrome P450 52A3 2-523 predicted domain transmembrane 18-35 predicted domain cytochrome P450 homology 317-493 binding-site heme iron (Cys) (axial ligand) 471 predicted 523 complete MAIEQIIEEVLPYLTKWYTIIFGAAVTYFLSIALRNKFYEYKLKCENPVYFQDAGLFGIP ALIDIIKVRKAGQLADYTDTTFDKYPNLSSYMTVAGVLKIVFTVDPENIKAVLATQFNDF ALGARHAHFDPLLGDGIFTLDGEGWKHSRAMLRPQFAREQIAHVKALEPHVQILAKQIKL NKGKTFDLQELFFRFTVDTATEFLFGESVHSLYDEKLGIPAPNDIPGRENFAEAFNTSQH YLATRTYSQIFYWLTNPKEFRDCNAKVHKLAQYFVNTALNATEKEVEEKSKGGYVFLYEL VKQTRDPKVLQDQLLNIMVAGRDTTAGLLSFAMFELARNPKIWNKLREEVEVNFGLGDEA RVDEISFETLKKCEYLKAVLNETLRMYPSVPINFRTATRDTTLPRGGGKDGNSPIFVPKG SSVVYSVYKTHRLKQFYGEDAYEFRPERWFEPSTRKLGWAYLPFNGGPRICLGQQFALTE ASYVIARLAQMFEHLESKDETYPPNKCIHLTMNHNEGVFISAK
JQ1039 JQ1039 03-Dec-1999 03-Dec-1999 03-Nov-2000
cytochrome P450 52A3-b oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Ohkuma, M. Hikiji, T. Tanimoto, T. Schunck, W.H. Mueller, H.G. Yano, K. Takagi, M. Agric. Biol. Chem. 5519911757-1764 Evidence that more than one gene encodes n-alkane-inducible cytochrome P-450s in Candida maltosa, found by two-step gene disruption. MUID92109967 JQ1039 DNA 1-523 GBD12475 GBD01168 NIDg218377 PIDNBAA02041.1 PIDg218378 GBS77461 NIDg242017 PIDNAAC60531.1 PIDg242018 strain CHA1 CYP52A3-b Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer endoplasmic reticulum heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 317-493 binding-site heme iron (Cys) (axial ligand) 471 predicted 523 complete MAIEQIIEEVLPYLTKWYTILFGAAFTYFLSIALRNKYYEYKLKCENPPYFKTAGFVGIP GLIDVIKAKNAGKLADYADQTFDEYPHHSFYMTVAGMLKIVLTVDPENIKAVLATQFNDF ALGARHAHFDPLLGDGIFTLDGEGWKHSRAMLRPQFAREQIAHVKALEPHVQVLAKQIKL NKGETFDLQELFFRFTVDTATEFLFGESVHSLYDEKLGVPPPNNIPGRENFAKAFNTSQH YLATRTYSQMFYFLTNPKEFRDCNAKVHKLAQYFVNKALDASEDEVAEKSKGGYVFLYEL VKQTRDPKVLQDQLLNIMVAGRDTTAGLLSFAMFELARNPKIWNKLREEIEVNFGLGEEA RVDEISFETLKKCEYLKAVLNETLRMYPSVPVNFRTATRDTTLPRGGGKDGTSPIFVPKG SSVVYTVYKTHRLEEYYGKDAYEFRPERWFEPSTRKLGWAYVPFNGGPRICLGQQFALTE ASYVITRLAQMFEHLESKDETYPPNKCIHLTMNHNEGVFISAK
O4CKA4 S08668 A56578 S65523 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome P450 52A4 cytochrome P450-cm2 oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Schunck, W.H. Gross, B. Mueller, H.G. submitted to the EMBL Data Library February1990 S08668 mRNA 1-538 EMBLX51932 NIDg2609 PIDNCAA36198.1 PIDg2610 strain EH15D Schunck, W.H. Vogel, F. Gross, B. Kargel, E. Mauersberger, S. Kopke, K. Gengnagel, C. Muller, H.G. Eur. J. Cell Biol. 551991336-345 Comparison of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum. MUID92037671 A56578 mRNA 1-255,'D',257-538 sequence inconsistent with nucleotide translation sequence extracted from NCBI backbone (NCBIN:64322, NCBIP:64324) Scheller, U. Zimmer, T. Kaergel, E. Schunck, W.H. Arch. Biochem. Biophys. 3281996245-254 Characterization of the n-alkane and fatty acid hydroxylating cytochrome P450 forms 52A3 and 52A4. MUID96213873 S65523 protein 2-15 CYP52A4 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase product cytochrome P450 52A4 2-538 experimental domain cytochrome P450 homology 331-507 binding-site heme iron (Cys) (axial ligand) 485 predicted 538 complete MSVSFVHNVLEVVTPYVEYYQENLTKWYILIPTILLTLPFLSILHTKYLEYKFNAKPLTN FAQDYSFGVITPLMLMYFKWHGTVMEFACNVWNNKFLVLNGNVRTVGLRIMGLNIIETTD PENVKAILATQFNDFSLGTRHDFLYSLLGDGIFTLDGAGWKHSRAMLRPQFAREQVAHVK LLEPHVQVLFKHVRKSQGKTFDIQELFFRLTVDSSTEFLFGGSVESLRDASIGMVPSTKN IAGREEFADAFNYSQTYNAYRFLLQQFYWILNGSKFNKSIKTVHKFADFYVQKALSLTDD DLEKQEGYVFLYELAKQTRDPKVLRDQLLNILVAGRDTTAGLLSFLFFELSRNPTVFEKL KEEIHNRFGAKEDARVEEITFESLKLCEYLKACVNEALRVYPSVPHNFRVATRNTTLPRG GGKDGMSPIAIKKGQNVMYTISATHRDPSIYGEDANVFRPERWFEPETRKLGWAYVPFNG GPRICLGQQFALTEASYVTVRLLQEFHTLTQDANTRYPPRLQNSLTVSLCDGANIQMY
B40576 B40576 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 ALK3-A oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Ohkuma, M. Tanimoto, T. Yano, K. Takagi, M. DNA Cell Biol. 101991271-282 CYP52 (cytochrome P450alk) multigene family in Candida maltosa: molecular cloning and nucleotide sequence of the two tandemly arranged genes. MUID91229697 B40576 DNA 1-538 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 331-507 binding-site heme iron (Cys) (axial ligand) 485 predicted 538 complete MPVSFVHNVLEVVTPYVEYYQENLTKWYILIPTILLTLNFLSILHTKYLEYKFNAKPLTN FAQDYSFGVITPLMLMYFKWHGTVMEFACNVWNNKFLVLNGNVRTVGLRIMGLNIIETTD PENVKAILATQFNDFSLGTRHDFLYSLLGDGIFTLDGAGWKHSRAMLRPQFAREQVAHVK LLEPHVQVLFKHVRKSQGKTFDIQELFFRLTVDSSTEFLFGGSVESLRDASIGMTPSTKN IAGREEFADAFNYSQTYNAYRFLLQQFYWILNGSKFNKSIKTVHKFADFYVQKALSLTEA DLEKQEGYVFLYELAKQTRDPKVLRDQLLNILVAGRDTTAGLLSFLFFELSRNPTVFEKL KEEIHNRFGAKEDARVEEITFESLKLCEYLKACVNEALRVYPSVPHNFRVATRNTTLPRG GGKDGMSPIAIKKGQNVMYTILATHRDPNIYGEDANVFRPERWFEPETRKLGWAYVPFNG GPRICLGQQFALTEASYVTVRLLQEFHTLTQDADTRYPPRLQNSLTLSLCDGANIQMY
S22972 S22972 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 52A6 cytochrome P450alk3 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Seghezzi, W. Meili, C. Ruffiner, R. Kuenzi, R. Sanglard, D. Fiechter, A. submitted to the EMBL Data Library June1992 Isolation and characterization of additional members of the cytochrome P450 gene family CYP52 of Candida tropicalis. S22972 DNA 1-524 EMBLZ13010 NIDg2659 PIDNCAA78354.1 PIDg2660 CYP52A6 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 318-494 binding-site heme iron (Cys) (axial ligand) 472 predicted 524 complete MATQEIIDSALPYLTKWYTVITLAALVFLISSNIKNYVKAKKLKCRDPPYFKGAGWTGIS PLIEIIKVKGNGRLARFWPIKTFDDYPNHTFYMSIIGALKIVLTVIQENIKAVLATQFTD FSLGTRHAHFYPLLGDGIFTLDGEGWKHSRAMLRPQFARDQIGHVKALEPHIQILAKQIK LNKGKTFDIQELFFRFTVDTATEFLFGESVHSLYDEKLGIPTPNEIPGRDNFATAFNTSQ HYLATRTYSQTFYFLTNPKEFRDCNAKVHYLAKYFVNKALNFTPEEIEEKSKSGYVFLYE LVKQTRDPKVLQDQLLNIMVAGRDTTAGLLSFAMFELARHPEIWSKLREEIEVNFGVGEE SRVEEITFESLKRCEYLKAILNETLRMYPSVPVNSRTATRDTTLPRGGGPNGTDPIFIPK GSTVAYIVYKTHRLEEYYGKDADDFRPERWFEPSTKKLGWAYVPFNGGPRICLGQQFALT EASYVITRLVQMFETVSSPPDVEYPPPKCIHLTMSHDDGVFVKM
JS0203 JS0203 A29297 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 52A1, alkane-inducible cytochrome P450alk 1 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Sanglard, D. Loper, J.C. Gene 761989121-136 Characterization of the alkane-inducible cytochrome P450 (P450alk) gene from the yeast Candida tropicalis: identification of a new P450 gene family. MUID89306647 JS0203 DNA 1-543 ATCC 750 Sanglard, D. Chen, C. Loper, J.C. Biochem. Biophys. Res. Commun. 1441987251-257 Isolation of the alkane inducible cytochrome. P450 (P450alk) gene from the yeast candida tropicalis. MUID87213173 A29297 DNA 438-543 GBM15945 NIDg170846 PIDNAAA34334.1 PIDg170847 ATCC 750 Candida tropicalis contains an alkane-inducible monooxygenase consisting of this protein and NADPH cytochrome P450 oxidoreductase. This system catalyzes the terminal hydroxylation as the first step in the assimilation of alkanes and fatty acids. CYP52A1 P450alk Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 29-48 predicted domain transmembrane 59-80 predicted domain cytochrome P450 homology 333-509 binding-site heme iron (Cys) (axial ligand) 487 predicted 543 complete MSSSPSIAQEFLATITPYVEYCQENYTKWYYFIPLVILSLNLISMLHTKYLERKFKAKPL AVYVQDYTFCLITPLVLIYYKSKGTVMQFACDLWDKKLIVSDPKAKTIGLKILGIPLIET KDPENVKAILATQFNDFSLGTRHDFLYSLLGDGIFTLDGAGWKHSRTMLRPQFAREQVSH VKLLEPHMQVLFKHIRKHHGQTFDIQELFFRLTVDSATEFLLGESAESLRDESVGLTPTT KDFDGRNEFADAFNYSQTNQAYRFLLQQMYWILNGSEFRKSIAIVHKFADHYVQKALELT DEDLEKKEGYVFLFELAKQTRDPKVLRDQLLNILVAGRDTTAGLLSFLFFELSRNPEIFA KLREEIENKFGLGQDARVEEISFETLKSCEYLKAVINETLRIYPSVPHNFRVATRNTTLP RGGGEGGLSPIAIKKGQVVMYTILATHRDKDIYGEDAYVFRPERWFEPETRKLGWAYVPF NGGPRICLGQQFALTEASYVTVRLLQEFGNLKQDPNTEYPPKLQNTLTLSLFEGAEVQMY LIL
JT0980 JT0980 S06148 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 52A2, alkane-inducible cytochrome P450-alk2 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Seghezzi, W. Sanglard, D. Fiechter, A. Gene 106199151-60 Characterization of a second alkane-inducible cytochrome P450-encoding gene, CYP52A2, from Candida tropicalis. MUID92039063 JT0980 DNA 1-522 GBM63258 NIDg170890 PIDNAAA34353.1 PIDg170891 the gene encoding this protein is located 1Kb upstream from the gene encoding another alkane-inducible protein, alk1 the authors translated the codon AGA for residue 152 as Thr Sanglard, D. Fiechter, A. FEBS Lett. 2561989128-134 Heterogeneity within the alkane-inducible cytochrome P450 gene family of the yeast Candida tropicalis. MUID90033287 S06148 DNA 'IS',312-522 EMBLX17560 NIDg2671 PIDNCAA35593.1 PIDg685237 CYP52A2 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain transmembrane 14-33 predicted domain cytochrome P450 homology 315-491 binding-site heme iron (Cys) (axial ligand) 469 predicted 522 complete MSIQDIVETYSTKWYVVVLVALIVYKVFDFFYARYLMYKLGAKPFLQSQTDGYLGFRVPF ELMGKKSEGTLIDFTYQRTLELDNPDIPTFTFPIFSVLIISTLEPDNIKAILATQFNDFS LGTRHSHFAPLLGDGIFTLDGAGWKHSRSMLRPQFAREQVSHVKLLEPHMQVFFKHIRKH HGQTFDIQELFFRLTVDSATEFLFGESVESLRDESIGMLNDALDFDGKAGFADAFNYSQN YLASRALMQQMYWILNGKKFKECNAKVHKFADYYVEKALELTPDQLEKQDGYVFLYELVK QTRDRQVLRDQLLNILVAGRDTTAGLLSFVFFELARTPRVANKLREEIEDKFGLGQDARV EEISFESLKSCEYLKAVLNECLRLYPSVPQNFRVATRNTTLPRGGGKDGLSPVLVRKGQT VMYSVYAAHRNKQIYGEDALEFRPERWFEPETKKLGWAFLPFNGGPRICLGQQFALTEAS YVTVRLLQEFSHLTMDPNTEYSPKKMSHLTMSLFDGANIQMY
A40576 A40576 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 ALK2-A oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Ohkuma, M. Tanimoto, T. Yano, K. Takagi, M. DNA Cell Biol. 101991271-282 CYP52 (cytochrome P450alk) multigene family in Candida maltosa: molecular cloning and nucleotide sequence of the two tandemly arranged genes. MUID91229697 A40576 preliminary DNA 1-526 CYP52A5 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 319-495 binding-site heme iron (Cys) (axial ligand) 473 predicted 526 complete MTSDSTIHELIQSYITKWYVIVPLAIIIYKVFDYFYVLSLRKRLGAAVPTNEETDGYFGF HLPFVLMSKKKDGTIIDFSIERYPELKHPETPTFEFPIFTVKLISTIDPENIKAILATQF SDFSLGTRHAHFAPLIGDGIFTLDGAGWKHSRAMLRPQFAREQVGHVKLLEPHVQVLFKH IRKNKGREFDLQELFFRFTVDSATEFLFGESVESLRDASIGMTSKSKDVDGIEDFTGAFN YSQNYLASRSIMQQFYWILNGKKFRECNAIVHKFADHYVQKALNLTEADLEKQAGYVFLY ELVKQTRDPQVLRDQLLNILVAGRDTTAGLLSFVFFELARNPDVVAKLKDEIDTKFGLGE DARIEEITFESLKQCEYLKAVLNECLRLYPSVPQNFRVATKNTTLPRGGGKDGLSPILVR KGQTVMYSVYATHRMESVYGKDATTFRPERWFEPETRKLGWAFVPFNGGPRICLGQQFAL TEASYVTVRLLQEFSTLTLDPNLEYPPKKMSHLTMSLFDGTNVQMY
JS0723 JS0723 03-Dec-1999 03-Dec-1999 21-Jul-2000
cytochrome P450 ALK5-A, alkane-inducible oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Ohkuma, M. submitted to JIPID July1992 JS0723 translation not shown DNA 1-521 DDBJD12717 NIDg218352 PIDNBAA02211.1 PIDg218353 ALK5-A Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 314-490 binding-site heme iron (Cys) (axial ligand) 468 predicted 521 complete MIDEILPKLVQYWYIVLPTLLIIKHVVSYINTQRLMRKFRAKPVTNVLNDGFFGIPNGIK AIKEKNKGRAQEYNDEKFAAGPKPKVGTYLFKLFTKDVLVTKDPENIKAILATQFEDFSL GKRLDFFKPLLGYGIFTLDGEGWKHSRAMLRPQFAREQVGHVKLIEPHFQSLKKHIIKNK GQFFDIQELFFRFTVDSATEFLFGESVESLKDESIGYDQQDFDFDGRKNFAEAFNKAQEY LGTRAILQLFYWLVNGADFKKSVAEVHKFTDYYVQKALDATPEELEKHSGYIFLYELVQQ TRDPKVLRDQSLNILLAGRDTTAGLLSFALFELARNPEVWSRLREEIGDKFGLDEDATIE GISFESLKQCEYLKAVVNECLRMYPSVPRNFRIATKHTTLPRGGGPDGKDPIFIKKGAVV SYGINSTHLDPMYYGPDARLFNPDRWSKPETKKLGWAFLPFNGGPRICLGQQFALTEASY VLVRMIQNFKELELTPNTVYPPRRLTNLTMSLYDGAYIKVN
S22974 S22974 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 52A8 cytochrome P450alk5 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Seghezzi, W. Meili, C. Ruffiner, R. Kuenzi, R. Sanglard, D. Fiechter, A. submitted to the EMBL Data Library June1992 Isolation and characterization of additional members of the cytochrome P450 gene family CYP52 of Candida tropicalis. S22974 DNA 1-517 EMBLZ13012 NIDg2663 PIDNCAA78356.1 PIDg2664 CYP52A8 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 310-486 binding-site heme iron (Cys) (axial ligand) 464 predicted 517 complete MYEQVVEYWYVVLPLVFILHKVFDMWHTRRLMKQLGAAPVTNQLHDNFFGIINGWKHLSS RKKVELKNIMIINLPIRKFQVWVHMLVPSLEQSSSSQKIRRNIKALLATQFSDFSLGKRH TLFKPLLGDGIFTLDGQGWKHSRAMLRPQFAREQVAHVTSLEPHFQLLKKHMVKNKGGFF DIQELFFRFTVDSATEFLFGESVHSLKDETIGSYQDDIDFVGRKDFAESFNKAQEYLAIR TLVQDFYYLVNNQEFRDCNKLVHKFTNYYVQRALDATPEELEKQSGYVFLYELVKQTRGP NVLRDQSLNILLAGRDTSAGLLSFAVFELARNPHIWAKLREDVESQFGLGEQSRIEEITF ESLKRCGYLKAFLNETLRVYPSVPRNFRIATKNTTLPRGGGSDGNSPVLVKKGEAVSYGI NSTHLDPVYYGDDAAEFRPERWNEPSTRKLGWAYLPFNGGPRICLGQQFALTEAGYVLVR LAQSFDTLELKPPVVYPPKRLTNLTMSLQDGTIVKID
S22973 S22973 03-Dec-1999 03-Dec-1999 03-Mar-2000
cytochrome P450 52A7 cytochrome P450alk4 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Seghezzi, W. Meili, C. Ruffiner, R. Kuenzi, R. Sanglard, D. Fiechter, A. submitted to the EMBL Data Library June1992 Isolation and characterization of additional members of the cytochrome P450 gene family CYP52 of Candida tropicalis. S22973 DNA 1-507 EMBLZ13011 NIDg2661 PIDNCAA78355.1 PIDg2662 CYP52A7 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome P450 homology 303-478 binding-site heme iron (Cys) (axial ligand) 456 predicted 507 complete MIEQVLHYWYYVLPAFIIFHWIVSAIHTNSLRRKLGAKPFTHTQLDGFYGFKFGRDFLKA KRIGRQVDLINSRFPDDIDTFSSYTFGNHVIFTRDPENIKALLATQFNDFSLGGRIKFFK PLLGYGIFTLDGEGWKHSRAMLRPQFAREQLPMSPSLEPHFNVKAYPQEQRWVFDIQELF FRFTVDSATEFLFGESVNSLKSASIGCDEETELEERKKFAEAFNKAQEYISTRVALQQLY WFVNNSEFKECNEIVHKFTNYYVQKALDATPEELEKQSGYVFLYELVKQTRDPNVLRDHH SISLLAGRDTTAGLLSFAVFELARNPHIWAKLREDVESQFGLGEESRIEEITFESLKRCE YLKAVMNETLRLHPSVPRNARFALKDTTLPRGGGPDGKDPILVRKMSCSIFISGTQIDPK HYGKDAKLFRPERWFESSTRNLGWAYLPFNGGPRICLGQQFALTEAGYILVRLAQSFDTL ELKPDTEYLTKISHLTMCLFGAFVKMD
JS0726 JS0726 03-Dec-1999 03-Dec-1999 16-Jun-2000
cytochrome P450 ALK8, alkane-inducible oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Ohkuma, M. submitted to JIPID July1992 JS0726 translation not shown DNA 1-519 DDBJD12719 NIDg218356 PIDNBAA02214.1 PIDg218358 ALK8 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 312-488 binding-site heme iron (Cys) (axial ligand) 466 predicted 519 complete MVFTAFILEYWYFTLLSLAAGHFIGKHVYTNYLMRKHHAEPILDVVDDGAFGFKFGFQAL KAKKIGKQIDLLFKKFNEAKHPSIGTFVTRSFGMQFIATKDPENIKAMLATQFNDFTLGQ RLSYFAPLLGKGIFTLDGEGWKHSRAMLRPQFSRDQVGHVKMLEPHFQLLKKHIIKNKGS FFDIQELFFRFTVDSATEFLFGESVSSLKDESIGYDQEEIDFAGRKDFAEAFNKSQVYLS TRSLLQLLYWLVNSSDFKRCNKIVHKFSDYYIKKALTATPEELEKHSSYIFLYELAKQTR DPIVLRDQSLNILLAGRDTTAGLLSFAVFELGRNPEVWSKLREEIGDKFGLDPDSRIEDI SFELLKLCEYLKAVINETLRLYPSVPRNGRFAAANTTLPHGGGPDGMSPILVRKGQTVMY SVYALQRDEKYYGKDANEFRPERWFEPEVRKLGWAFLPFNGGPRICLGQQFALTEASYVL VRLIQSFETLELSPDAPYPPAKLTHLTMCLFDGAPVRIE
JS0725 JS0725 03-Dec-1999 03-Dec-1999 16-Jun-2000
cytochrome P450 ALK7, alkane-inducible oxidoreductase (EC 1.-.-.-) yeast (Candida maltosa) Candida maltosa Ohkuma, M. submitted to JIPID July1992 JS0725 translation not shown DNA 1-519 DDBJD12719 NIDg218356 PIDNBAA02213.1 PIDg218357 ALK7 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 312-488 binding-site heme iron (Cys) (axial ligand) 466 predicted 519 complete MIFTAFILDYWYFTLLFLIAAYFIGKHVYTNYLMRKHHAEPILDVVDDGAFGFKFGFQSL KAKKIGNQIDLLFLKFNEAKHPSIGTFVTRSFGMQFIATKDPENIKAMLATQFNEYTLGQ RLNFLAPLLGKGIFTLDGNGWKHSRAMLRPQFSRDQIGHVKMLEPHFQLLKKHIIKNKGT FFDIQELFFRFTVDSATEFLFGESVSSLKDESIGYDQEEIDFAGRKDFAEAFNKSQVYLS TRTLLQLLYWLVNSADFKRCNKIVHKFSDYYIKKALTATPEELEKHSSYIFLYELAKQTR DPIVLRDQSLNILLAGRDTTAGLLSFAVFELGRNPEVWSKLRQEIGHKFGLDSYSRVEDI SFELLKLCEYLKAVLNETLRLYPSVPRNARFAAKNTTLPHGGGPDGMSPILVRKGQTVMY SVYALQRDEKYYGKDANEFRPERWFEPEVRKLGWAFLPFNGGPRICLGQQFALTEASYVL ARLIQSFETLELSPEAAYPPAKLSHLTMCLFDGTPVRFE
S69988 S69988 S38894 10-Sep-1999 10-Sep-1999 03-Mar-2000
unspecific monooxygenase (EC 1.14.14.1) cytochrome P450 52E1 Candida apicola (ATCC 96134) Candida apicola ATCC 96134 Lottermoser, K. Schunck, W.H. Asperger, O. Yeast 121996565-575 Cytochromes P450 of the sophorose lipid-producing yeast Candida apicola: heterogeneity and polymerase chain reaction-mediated cloning of two genes. MUID96367597 S69988 DNA 1-519 EMBLX76225 NIDg840727 PIDNCAA53811.1 PIDg431234 ATCC 96134 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 309-483 binding-site heme iron (Cys) (axial ligand) 461 predicted 519 complete MIIGLSDAFALGGIALSFLVAYQFIYFYFIYSPRAKKLGCAPPVIVFSFPLGLPALYKFA TAMLHDNLLEYISIRIADMKVRTGFQTLAGQRWLVTLEPENIKTVLATSFKDYSLGFRYD IMYGLLGNGIFTLSGDGWKHSRALLRPQFSREQVSHLESMRTHINLMINNHFKGGQVVDA QALYHNLTIDTATEFLFGESTNTLDPDLAQQGLPGPKGLVTGEQFAEAFTSALEILSVRV IVGAAWFLIWTPKFWRSCKVCHNFIDYFVYKALATPMEKDQEADRYVFIRELTKETSDPR VIRDQALNILLAGRDTTAGLLSFITYYLGAYPEVYAELREAVLSEFGSTDVETPTFEQLK QCKVLQNVIREVLRLHPNVPLNFRQAIVDTKLPTGGGPNGDQPVFVPKGQNVFYSTYSMQ RRTDIWGPDATTFRPDRWNEPREALASGWDYIPFNGGPRICLGQQFALTEASYTIVRICQ EFSRIEVLHPDVITSKNSMKQRMRLTQTASGGVITRFIR
S22976 S22976 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 52C1 cytochrome P450alk7 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Seghezzi, W. Meili, C. Ruffiner, R. Kuenzi, R. Sanglard, D. Fiechter, A. submitted to the EMBL Data Library June1992 Isolation and characterization of additional members of the cytochrome P450 gene family CYP52 of Candida tropicalis. S22976 DNA 1-505 EMBLZ13014 NIDg2667 PIDNCAA78358.1 PIDg2668 CYP52C1 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase transmembrane protein domain cytochrome P450 homology 307-475 binding-site heme iron (Cys) (axial ligand) 453 predicted 505 complete MYQLFCFLAGIIVVYKAAQYYKRRTLVTKFHCKPARISPNKSWLEYLGIASVVHADEMIR KGGLYSEIDGRFKSLDVSTFKSITLGKTTYVTKDIENIRHILSATEMNSWNLGARPIALR PFIGDGIFASEGQSWKHSRIMLRPVFAKEHVKQITSMEPYVQLLIKIIKNHEGEPLEFQT LAHLFTIDYSTDFLLGESCDSLKDFLGEESNSTLDTSLRLAFASQFNKTQQQMTIRFMLG KLAFLMYPKSFQYSIQMQKDFVDVYIDRVVGMSEEELNNHPKSYVLLYQLARQTKNRDIL QDELMSILLAGRDTTASLLTFLFFELSHHPEVFNKLKEEIERHFPDVESVTFGTIQRCDY LQWCINETMRLHPSVPFNFRTAANDTVIPRGGGKSCTDPILVHKGEQVLFSFYSVNREEK YFGTNTDKFAPERWSESLRRTEFIPFSAGPRACLGQQLPRVEASYVTIRLLQTFHGLHNA SKQYPPNRVVAATMRLTDGCNVCFI
S22975 S22975 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 52B1 cytochrome P450alk6 oxidoreductase (EC 1.-.-.-) yeast (Candida tropicalis) Candida tropicalis Seghezzi, W. Meili, C. Ruffiner, R. Kuenzi, R. Sanglard, D. Fiechter, A. submitted to the EMBL Data Library June1992 Isolation and characterization of additional members of the cytochrome P450 gene family CYP52 of Candida tropicalis. S22975 preliminary DNA 1-506 EMBLZ13013 NIDg2665 PIDNCAA78357.1 PIDg2666 CYP52B1 Candida cytochrome P450 52A3 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase transmembrane protein domain cytochrome P450 homology 299-473 binding-site heme iron (Cys) (axial ligand) 451 predicted 506 complete MSLTETTATFIYNYWYIIFHLYFYTTSKIIKYHHTTYLMIKFKASPPLNYINKGFFGIQA TFTELKHLICHTSIDYAIDQFNNVPFPHVHTFVTKVLGNELIMTKDPENIKVLLRFPVFD KFDYGTRSSAVQPSLGMGIFTLEGENWKATRSVLRNMFDRKSIDKVHDFEPHFKTLQKRI DGKVGYFDIQQEFLKLGLELSIEFIFGQVVSEDVPHYDDFTQAWDRCQDYMMLRLLLGDF YWMANDWRYKQSNQIVQAFCDYLVQKSLENTCNDKFVFVHQLAKHTTNKTFIRDQALSLI MASRDTTAELMAFTILELSRKSHHLGKLREEIDANFGLESPDLLTFDSLRKFKYVQAILN ETLRMYPGVPRNMKTAKCTTTLPKGGGPDGQDPILVKKGQSVGFISIATHLDPVLNFGSD AHVFRPDRWFDSSMKNLGCKYLPFNAGPRTCLGQQYTLIEASYLLVRLAQTYETVESHPD SVYPPRKKALINMCAADGVDVKFHRL
C37842 C37842 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 oxidoreductase (EC 1.-.-.-) Anabaena sp. (strain PCC 7120) Anabaena sp. Lammers, P.J. McLaughlin, S. Papin, S. Trujillo-Provencio, C. Ryncarz II, A.J. J. Bacteriol. 17219906981-6990 Developmental rearrangement of cyanobacterial nif genes: nucleotide sequence, open reading frames, and cytochrome P-450 homology of the Anabaena sp. strain PCC 7120 nifD element. MUID91072249 C37842 DNA 1-354 GBM38044 CYP110 Anabaena cytochrome P450 CYP110 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 153-310 binding-site heme iron (Cys) (axial ligand) 288 predicted 354 complete MEKGIQAYAQQICLITNQIASEWQIGQPFVARSAMQKLSLEVIIQIVFGLADGERYQQIK PLFTDWLNMTDSPLRSSMLFLKSLQKDWGTWTPWGQMKHKQRSIYDLLQAEIEEKRTKEN EQRGDVLSLMMAARDENGQAMTDEELKDELLTILFAGHETTATTIAWAFYQILKNVNVQE KLQQELDRLGANPNPMEIAQLPYLTAVSQETLRMYPVLPTLFPRITKSSINIAGYQLEPD TTLMASIYLIHYREDLYPNPQQFRPERFIERQYSPSEYIPFGGGSRRCLGIALALLEIKL VIATVLSNYQLALAEDKPVNVQRRGFTLAPDGGVRVIMTGKKSLKFEQSSKIFN
S75761 S75761 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 protein slr0574 oxidoreductase (EC 1.-.-.-) Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S75761 nucleic acid sequence not shown translation not shown DNA 1-444 EMBLD64003 GBAB001339 NIDg1001200 PIDNBAA10496.1 PIDg1001252 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 cyp Synechocystis cytochrome P450 slr0574 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 251-413 binding-site heme iron (Cys) (axial ligand) 391 predicted 444 complete MITSPTNLNSLPIPPGDFGLPWLGETLNFLNDGDFGKKRQQQFGPIFKTRLFGKNVIFIS GALANRFLFTKEQETFQATWPLSTRILLGPNALATQMGEIHRSRRKILYQAFLPRTLDSY LPKMDGIVQGYLEQWGKANEVIWYPQLRRMTFDVAATLFMGEKVSQNPQLFPWFETYIQG LFSLPIPLPNTLFGKSQRARALLLAELEKIIKARQQQPPSEEDALGILLAARDDNNQPLS LPELKDQILLLLFAGHETLTSALSSFCLLLGQHSDIRERVRQEQNKLQLSQELTAETLKK MPYLDQVLQEVLRLIPPVGGGFRELIQDCQFQGFHFPKGWLVSYQISQTHADPDLYPDPE KFDPERFTPDGSATHNPPFAHVPFGGGLRECLGKEFARLEMKLFATRLIQQFDWTLLPGQ NLELVVTPSPRPKDNLRVKLHSLM
S55379 S55379 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 CYP90 oxidoreductase (EC 1.-.-.-) Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana Szekeres, M. Nemeth, K. Koncz, Z. Nagy, F. Koncz, C. submitted to the EMBL Data Library May1995 S55379 mRNA 1-472 EMBLX87367 NIDg853718 PIDNCAA60793.1 PIDg853719 CYP90 Synechocystis cytochrome P450 slr0574 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 275-440 binding-site heme iron (Cys) (axial ligand) 418 predicted 472 complete MAFTAFLLLLSSIAAGFLLLLRRTRYRRMGLPPGSLGLPLIGETFQLIGAYKTENPEPFI DERVARYGSVFMTHLFGEPTIFSADPETNRFVLQNEGKLFECSYPASICNLLGKHSLLLM KGSLHKRMHSLTMSFANSSIIKDHLMLDIDRLVRFNLDSWSSRVLLMEEAKKITFELTVK QLMSFDPGEWSESLRKEYLLVIEGFFSLPLPLFSTTYRKAIQARRKVAEALTVVVMKRRE EEEEGAERKKDMLAALLAADDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLA LAQLKEEHEKIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGVFRRAMTDVEIK GYKIPKGWKVFSSFRAVHLDPNHFKDARTFNPWRWQSNSVTTGPSNVFTPFGGGPRLCPG YELARVALSVFLHRLVTGFSWVPAEQDKLVFFPTTRTQKRYPIFVKRRDFAT
D71417 D71417 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 d13700w oxidoreductase (EC 1.-.-.-) Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana columbia Bevan, M. Bancroft, I. Bent, E. Love, K. Goodman, H. Dean, C. Bergkamp, R. Dirkse, W. Van Staveren, M. Stiekema, W. Drost, L. Ridley, P. Hudson, S.A. Patel, K. Murphy, G. Piffanelli, P. Wedler, H. Wedler, E. Wambutt, R. Weitzenegger, T. Pohl, T.M. Terryn, N. Gielen, J. Villarroel, R. De Clerck, R. Van Montagu, M. Lecharny, A. Auborg, S. Gy, I. Kreis, M. Lao, N. Kavanagh, T. Hempel, S. Kotter, P. Entian, K.D. Rieger, M. Schaeffer, M. Funk, B. Mueller-Auer, S. Silvey, M. James, R. Montfort, A. Pons, A. Puigdomenech, P. Douka, A. Voukelatou, E. Milioni, D. Hatzopoulos, P. Piravandi, E. Obermaier, B. Hilbert, H. Duesterhoft, A. Moores, T. Jones, J.D.G. Eneva, T. Palme, K. Benes, V. Rechman, S. Ansorge, W. Cooke, R. Berger, C. Delseny, M. Voet, M. Volckaert, G. Mewes, H.W. Klosterman, S. Schueller, C. Chalwatzis, N. Nature 3911998485-488 Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. MUID98121113 D71417 preliminary nucleic acid sequence not shown translation not shown DNA 1-324 GBZ97338 NIDg2244870 PIDNCAB10310.1 PIDg2244889 d13700w 4COP9-4G3845 Synechocystis cytochrome P450 slr0574 cytochrome P450 homology oxidoreductase 324 complete MEIAKASSQLRATESVTRIFGENNPFLQSKEIHKYVRNLTSRFVGPEGLKTRLIHDIDNL LRNDVENGARNGSFDVREATIKMVGELIAKKIMGETESEAVKELGLCWSAFRTSWFQFSY NIPGTTVYRLVKARRKAAKLLKALILKKKASKEGLGDFLDIIFDEMEKDGTALDIDKAVN LIFVFFILSQETTPGVQGAVVKLVADHPSVMEELQREHEAIVQNRADKDTGVTWEEYKSM TFTHMVIKESLRFTSTQPTVHRIPDQDVQIGAQARSFRKMLDILVNTVVELEPHALKMFN NDVDQKMLDLQYNVMHKNFQRDCS
C71417 C71417 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 d13695c oxidoreductase (EC 1.-.-.-) Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana columbia Bevan, M. Bancroft, I. Bent, E. Love, K. Goodman, H. Dean, C. Bergkamp, R. Dirkse, W. Van Staveren, M. Stiekema, W. Drost, L. Ridley, P. Hudson, S.A. Patel, K. Murphy, G. Piffanelli, P. Wedler, H. Wedler, E. Wambutt, R. Weitzenegger, T. Pohl, T.M. Terryn, N. Gielen, J. Villarroel, R. De Clerck, R. Van Montagu, M. Lecharny, A. Auborg, S. Gy, I. Kreis, M. Lao, N. Kavanagh, T. Hempel, S. Kotter, P. Entian, K.D. Rieger, M. Schaeffer, M. Funk, B. Mueller-Auer, S. Silvey, M. James, R. Montfort, A. Pons, A. Puigdomenech, P. Douka, A. Voukelatou, E. Milioni, D. Hatzopoulos, P. Piravandi, E. Obermaier, B. Hilbert, H. Duesterhoft, A. Moores, T. Jones, J.D.G. Eneva, T. Palme, K. Benes, V. Rechman, S. Ansorge, W. Cooke, R. Berger, C. Delseny, M. Voet, M. Volckaert, G. Mewes, H.W. Klosterman, S. Schueller, C. Chalwatzis, N. Nature 3911998485-488 Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. MUID98121113 C71417 nucleic acid sequence not shown translation not shown DNA 1-487 GBZ97338 NIDg2244870 PIDNCAB10309.1 PIDg2244888 d13695c 4COP9-4G3845 Synechocystis cytochrome P450 slr0574 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase binding-site heme iron (Cys) (axial ligand) 433 predicted 487 complete MVSLFLVKIFHWVYQWRNPKTNGKLPPGSMGFPFIGETFEFFKPHDALQFSTFIKDRVLR FFADFSSIHLSFFRTSLFGDKAIISMDMELNLEMAKANSVPGVTKSVIRLFGENNLFLQS KESHKHVRNLTFQLLGPQGLKSRMIEDVDLLARTYMEEGARNGYLDVKETSSKILIGCLA KKVMGEMEPEAAKELALCWRYFQSGWFRFFLNLPGTGVYKMMKVLFVQYTEADISWQARK RMMKLLRKTVLTKRASGEELGEFFNIIFGEMEGEGETMSVENAVEYIYTFFLVANETTPR ILAATVKFISDHPKVKQELQREHEEIVRGKAEKEGGLTWEDYKSMHFTQMVINESLRIIS TAPTVLRVLEHDFQVGDYTIPAGWTFMGYPHIHFNSEKYEDPYAFNPWRWEGKDLGAIVS KTFIPFGAGRRLCVGAEFAKMQMAVFIHHLFRYRWSMKSGTTIIRSFMLMFPGGCDVQIS EDTEVDK
T02263 T02263 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 DWARF3 oxidoreductase (EC 1.-.-.-) maize maize Zea mays Winkler, R.G. Helentjaris, T. Plant Cell 719951307-1317 The maize dwarf3 gene encodes a cytochrome P450-mediated early step in gibberellin biosynthesis. MUID96004534 T02263 preliminary translated from GB/EMBL/DDBJ mRNA 1-519 EMBLU32579 NIDg987266 PIDNAAC49067.1 PIDg987267 strain B73 dwarf3 involved in an early step in gibberellin biosynthesis gibberellin biosynthesis Synechocystis cytochrome P450 slr0574 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 325-488 519 complete MLGVGMAAAVLLGAVALLLADAAARRAHWWYREAAEAVLVGAVALVVVDAAARRAHGWYR EAALGAARRARLPPGEMGWPLVGGMWAFLRAFKSGKPDAFIASFVRRFGRTGVYRSFMFS SPTVLVTTAEGCKQVLMDDDAFVTGWPKATVALVGPRSFVAMPYDEHRRIRKLTAAPING FDALTGYLPFIDRTVTSSLRAWADHGGSVEFLTELRRMTFKIIVQIFLGGADQATTRALE RSYTELNYGMRAMAINLPGFAYRGALRARRRLVAVLQGVLDERRAARAKGVSGGGVDMMD RLIEAQDERGRHLDDDEIIDVLVMYLNAGHESSGHITMWATVFLQENPDMFARAKAEQEA IMRSIPSSQRGLTLRDFRKMEYLSQVIDETLRLVNISFVSFRQATRDVFVNGYLIPKGWK VQLWYRSVHMDPQVYPDPTKFDPSRWEGHSPRAGTFLAFGLGARLCPGNDLAKLEISVFL HHFLLGYKLARTNPRCRVRYLPHPRPVDNCLAKITRVGS
S71163 S71163 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 oxidoreductase (EC 1.-.-.-) garden pea garden pea Pisum sativum Baltrusch, M. submitted to the EMBL Data Library May1995 Isolation of cytochrome P450 cDNA from Pisum sativum seedlings. S71163 preliminary mRNA 1-552 EMBLZ49263 NIDg1360117 PIDNCAA89260.1 PIDg1360118 pea cytochrome P450 CYP97 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 359-549 binding-site heme iron (Cys) (axial ligand) 528 predicted 552 complete MVAAPISTVKLTDANLHTRFHSSSSSTPSTLSLPLSLHFHFSSHSKRFSSIRCQSVNGEK RKQSSRNVFDNASNLLTSLLSGANLGSMPIAEGAVTDLFDRPLFFSLYDWFLEHGSVYKL AFGPKAFVVVSDPIVARHILRENAFSYDKGVLADILEPIMGKGLIPADLETWKQRRRVIA PGFHTSYLEAMVQLFTSCSERTVLKVNELLEGEGRDGQKSVELDLEAEFSNLALEIIGLG VFNYDFGSVTNESPVIKAVYGTLFEAEHRSTFYIPYWKFPLARWIVPRQRKFQDDLKVIN TCLDGLIRNAKESRQETDVEKLQQRDYSNLKDASLLRFLVDMRGVDVDDRQLRDDLMTML IAGHETTAAVLTWAVFLLAQNPDKMKKAQAEVDLVLGMGKPTFELLKKLEYIRLIVVETL RLYPQPPLLIRRSLKPDVLPGGHKGDKDGYTIPAGTDVFISVYNLHRSPYFWDRPNDFEP ERFLVQNNNEEVEGWAGFDPSRSPGALYPNEIISDFAFLPFGGGPRKCVGDQFALMESTV ALVCCYRISMWN
H71414 H71414 10-Sep-1999 10-Sep-1999 21-Jul-2000
probable cytochrome P450 oxidoreductase (EC 1.-.-.-) Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana columbia Bevan, M. Bancroft, I. Bent, E. Love, K. Goodman, H. Dean, C. Bergkamp, R. Dirkse, W. Van Staveren, M. Stiekema, W. Drost, L. Ridley, P. Hudson, S.A. Patel, K. Murphy, G. Piffanelli, P. Wedler, H. Wedler, E. Wambutt, R. Weitzenegger, T. Pohl, T.M. Terryn, N. Gielen, J. Villarroel, R. De Clerck, R. Van Montagu, M. Lecharny, A. Auborg, S. Gy, I. Kreis, M. Lao, N. Kavanagh, T. Hempel, S. Kotter, P. Entian, K.D. Rieger, M. Schaeffer, M. Funk, B. Mueller-Auer, S. Silvey, M. James, R. Montfort, A. Pons, A. Puigdomenech, P. Douka, A. Voukelatou, E. Milioni, D. Hatzopoulos, P. Piravandi, E. Obermaier, B. Hilbert, H. Duesterhoft, A. Moores, T. Jones, J.D.G. Eneva, T. Palme, K. Benes, V. Rechman, S. Ansorge, W. Cooke, R. Berger, C. Delseny, M. Voet, M. Volckaert, G. Mewes, H.W. Klosterman, S. Schueller, C. Chalwatzis, N. Nature 3911998485-488 Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. MUID98121113 H71414 preliminary nucleic acid sequence not shown translation not shown DNA 1-576 GBZ97337 NIDg2244829 PIDNCAB10290.1 PIDg2244868 4COP9-4G3845 pea cytochrome P450 CYP97 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 352-543 binding-site heme iron (Cys) (axial ligand) 521 predicted 576 complete MAFPAAATYPTHFQGGALHLGRTDHCLFGFYPQTISSVNSRRASVSIKCQSTEPKTNGNI LDNASNLLTNFLSGGSLGSMPTAEGSVSDLFGKPLFLSLYDWFLEHGGIYKLAFGPKAFV VISDPIIARHVLRENAFSYDKGVLAEILEPIMGKGLIPADLDTWKLRRRAITPAFHKLYL EAMVKVFSDCSEKMILKSEKLIREKETSSGEDTIELDLEAEFSSLALDIIGLSVFNYDFG SVTKESPVIKAVYGTLFEAEHRSTFYFPYWNFPPARWIVPRQRKFQSDLKIINDCLDGLI QNAKETRQETDVEKLQERDYTNLKDASLLRFLVDMRGVDIDDRQLRDDLMTMLIAGHETT AAVLTWAVFLLSQNPEKIRKAQAEIDAVLGQGPPTYESMKKLEYIRLIVVEVLRLFPQPP LLIRRTLKPETLPGGHKGEKEGHKVPKGTDIFISVYNLHRSPYFWDNPHDFEPERFLRTK ESNGIEGWAGFDPSRSPGALYPNEIIADFAFLPFGGGPRKCIGDQFALMESTVALAMLFQ KFDVELRGTPESVELVSGATIHAKNGMWCKLKRRSK
O4BS6M S07764 S17973 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome P450 106 cytochrome P450BM-1 oxidoreductase (EC 1.-.-.-) Bacillus megaterium Bacillus megaterium He, J.S. Ruettinger, R.T. Liu, H.M. Fulco, A.J. Biochim. Biophys. Acta 10091989301-303 Molecular cloning, coding nucleotides and the deduced amino acid sequence of P-450(BM-1) from Bacillus megaterium. MUID90089408 S07764 DNA 1-410 EMBLX16610 NIDg39626 PIDNCAA34612.1 PIDg39627 S17973 protein 1-25 CYP106 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase product cytochrome P450 106 1-410 experimental domain cytochrome P450 homology 241-378 binding-site heme iron (Cys) (axial ligand) 356 predicted 410 complete MNKEVIPVTEIPKFQSRAEEFFPIQWYKEMLNNSPVYFHEETNTWNVFQYEHVKQVLSNY DFFSSDGQRTTIFVGDNSKKKSTSPITNLTNLDPPDHRKARSLLAAAFTPRSLKNWEPRI KQIAADLVEAIQKNSTINIVDDLSSPFPSLVIADLFGVPVKDRYQFKKWVDILFQPYDQE RLEEIEQEKQRAGAEYFQYLYPIVIEKRSNLSDDIISDLIQAEVDGETFTDEEIVHATML LLGAGVETTSHAIANMFYSFLYDDKSLYSELRNNRELAPKAVEEMLRYRFHISRRDRTVK QDNELLGVKLKKGDVVIAWMSACNMDETMFENPFSVDIHRPTNKKHLTFGNGPHFCLGAP LARLEMKIILEAFLEAFSHIEPFEDFELEPHLTASATGQSLTYLPMTVYR
B69851 B69851 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 yjiB oxidoreductase (EC 1.-.-.-) Bacillus subtilis Bacillus subtilis Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 B69851 nucleic acid sequence not shown translation not shown DNA 1-396 GBZ99110 GBAL009126 NIDg2633472 PIDNCAB13078.1 PIDg2633575 strain 168 yjiB Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 236-371 396 complete MNVLNRRQALQRALLNGKNKQDAYHPFPWYESMRKDAPVSFDEENQVWSVFLYDDVKKVV GDKELFSSCMPQQTSSIGNSIINMDPPKHTKIRSVVNKAFTPRVMKQWEPRIQEITDELI QKFQGRSEFDLVHDFSYPLPVIVISELLGVPSAHMEQFKAWSDLLVSTPKDKSEEAEKAF LEERDKCEEELAAFFAGIIEEKRNKPEQDIISILVEAEETGEKLSGEELIPFCTLLLVAG NETTTNLISNAMYSILETPGVYEELRSHPELMPQAVEEALRFRAPAPVLRRIAKRDTEIG GHLIKEGDMVLAFVASANRDEAKFDRPHMFDIRRHPNPHIAFGHGIHFCLGAPLARLEAN IALTSLISAFPHMECVSITPIENSVIYGLKSFRVKM
S49051 S49051 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 tylI (EC 1.1.-.-) [validated] Streptomyces fradiae (strain T59235) Streptomyces fradiae strain T59235 Merson-Davies, L.A. Cundliffe, E. Mol. Microbiol. 131994349-355 Analysis of five tylosin biosynthetic genes from the tyIIBA region of the Streptomyces fradiae genome. MUID95075319 S49051 preliminary nucleic acid sequence not shown translation not shown DNA 1-417 EMBLU08223 NIDg6849140 PIDNAAA21341.1 PIDg473597 strain T59235 the nucleotide sequence was submitted to the EMBL Data Library, March 1994 tylI involved in C20ring oxidation of O-mycaminosyl tylactone [validated; MUID:95075319] Bacillus cytochrome P450 CYP106 cytochrome P450 homology heme oxidoreductase domain cytochrome P450 homology 253-388 417 complete MTTQTLEAEKPPEPERTANSVHPLAQPAGAGARGLLEWFARARAEAPVFWDESRQAWQVF RYDDYLTVSTNPQLFSSDFSPVFPVPEELAILMGPGTFGGIDPPRHGPLRKLVSQAFTPR RIATLEPRIAEITRGLLDGLREKGQIDVVSDLAYPLPVIVIAELLGIPAEDRDLFREWVD VILNNEGMEYPNLPDDFSETMGPAIKEWGDYLYRRIALKRETPTDDLMSGLIEAEVEGRR LTDEEIVNIVALLLTAGHISSATLLGNLFLVLDEHREAQAELRADRDLIPGAIEETLRYR SPFNNIFRLLKEDTDILGHPMKAGQMVVAWIASANRDSAHFSDPDTFDVRRQPNKHMSFG HGIHHCLGSFLARLEAKVFLELFFDEFSDYRVEHDEVEFYEEDELTARRLPVTVTRH
B40634 B40634 10-Sep-1999 10-Sep-1999 03-Mar-2000
erythromycin monooxygenase (EC 1.14.-.-) erythromycin C-12 hydroxylase EryK Saccharopolyspora erythraea Saccharopolyspora erythraea Stassi, D. Donadio, S. Staver, M.J. Katz, L. J. Bacteriol. 1751993182-189 Identification of a Saccharopolyspora erythraea gene required for the final hydroxylation step in erythromycin biosynthesis. MUID93106953 B40634 preliminary DNA 1-412 GBU82823 GBL05776 NIDg2327012 sequence extracted from NCBI backbone (NCBIN:121243, NCBIP:121245) CYP113A1 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 238-376 binding-site heme iron (Cys) (axial ligand) 354 predicted 412 complete VCADVETTCCARRTLTTIDEVPGMADETALLDWLGTMREKQPVWQDRYGVWHVFRHADVQ TVLRDTATFSSDPTRVIEGASPTPGMIHEIDPPEHRALRKVVSSAFTPRTISDLEPRIRD VTRSLLADAGESFDLVDVLAFPLPVTIVAELLGLPPMDHEQFGDWSGALVDIQMDDPTDP ALAERIADVLNPLTAYLKARCAERRADPGDDLISRLVLAEVDGRALDDEEAANFSTALLL AGHITTTVLLGNIVRTLDEHPAHWDAAAEDPARIPAIVEEVLRYRPPFPQMQRTTTKATE VAGVPIPADVMVNTWVLSANRDSDAHDDPDRFDPSAQVRPAPRTSSFGHGVHFCLAAPLA RLENRVALEEIIARFGRLTVDRDDERLRHFEQIVLGTRHLPVLAGSSPRQSA
S71328 S71328 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 CYP119 oxidoreductase (EC 1.-.-.-) Sulfolobus solfataricus Sulfolobus solfataricus Wright, R.L. Harris, K. Solow, B. White, R.H. Kennelly, P.J. FEBS Lett. 3841996235-239 Cloning of a potential cytochrome P450 from the Archaeon Sulfolobus solfataricus. MUID96197795 S71328 DNA 1-368 EMBLU51337 NIDg1256447 PIDNAAB03278.1 PIDg1256448 ATCC 35091 CYP119 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 206-339 binding-site heme iron (Cys) (axial ligand) 317 predicted 368 complete MYDWFSEMRKKDPVYYDGNIWQVFSYRYTKEVLNNFSKFSSDLTGYHERLEDLRNGKIRF DIPTRYTMLTSDPPLHDELRSMSADIFSPQKLQTLETFIRETTRSLLDSIDPREDDIVKK LAVPLPIIVISKILGLPIEDKEKFKEWSDLVAFRLGKPGEIFELGKKYLELIGYVKDHLN SGTEVVSRVVNSNLSDIEKLGYIILLLIAGNETTTNLISNSVIDFTRFNLWQRIREENLY LKAIEEALRYSPPVMRTVRKTKERVKLGDQTIEEGEYVRVWIASANRDEEVFHDGEKFIP DRNPNPHLSFGSGIHLCLGAPLARLEARIAIEEFSKRFRHIEILDTEKVPNEVLNGYKRL VVRLKSNE
B42606 B42606 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 CVIIB1 oxidoreductase (EC 1.-.-.-) Saccharopolyspora erythraea Saccharopolyspora erythraea Andersen, J.F. Hutchinson, C.R. J. Bacteriol. 1741992725-735 Characterization of Saccharopolyspora erythraea cytochrome P-450 genes and enzymes, including 6-deoxyerythronolide B hydroxylase. MUID92121109 B42606 preliminary not compared with conceptual translation DNA protein 1-405 GBM83110 NIDg152682 PIDNAAA26483.1 PIDg152684 NRRL2338 sequence extracted from NCBI backbone (NCBIP:77484) CYP107B1 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 238-374 binding-site heme iron (Cys) (axial ligand) 352 predicted 405 complete MTTGEVPDLLAFDDAFAQDRHNRYARMREEPVQRIRTVNGLDAWLITRYEDVKQALLDPR IAKDFGRTQQIIEKRLADAERRPGFSPDLGPHMLNTDPPDHTRLRKLVVKAFTARRVEGL RPRIEQITDDLLDRLAGRSEVDLIDEFAFPLPITVISELMGVEDSRRDDFRSWTNVLVDG SQPEAQAQASVAMVEYLTELIAKKRTEPGDDLLTALLEAVEDGDRLSEGELIAMVFLLLV AGHETTVNLIGNCVLSLLGNPDQLAALRNDPSLLPGAIEETLRYESPVANGTFRHTAEAV RFGDVVIPEGELVWVALGAANRDGERFEDPDRFDITRETTGHVAFGHGIHFCVGAALARL EAQIAVGRLLERFPDLRMAASPDDLRWRFSVLMRGLEKLPVRPGA
JC4003 JC4003 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 oxidoreductase (EC 1.-.-.-) Streptomyces sp. Streptomyces sp. Arisawa, A. Tsunekawa, H. Okamura, K. Okamoto, R. Biosci. Biotechnol. Biochem. 591995582-588 Nucleotide sequence analysis of the carbomycin biosynthetic genes including the 3-O-acyltransferase gene from Streptomyces thermotolerans. MUID95290751 JC4003 DNA 1-411 DDBJD30759 NIDg551628 PIDNBAA06420.1 PIDg551630 the source was designated as Streptomyces thermotolerans Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 242-382 411 complete MTALNLMDPEVLRDPFGAYAEIRAQAPLVRASYPWGAVQWLATRYSDVKAVLTDPRLVNN PANVPEMHLPHPYEQALGDGGIPDEYVRYLAGSILSQDGPGHLRLRRLSSRAFTVRRVNA LRPRVTELAHRLLASLPDRAQDGVIDVLEDFSYPLSIDVICEIVGIPEEAREQWHTWGSA FYTMDPAVIGPAVRGMADHLHLLIEQRRATPTGDLLTGLVQAEDEQGEPLTDEEIATLVL TFVTAGNETTAHLIGNGVAALLTHSDQLALLRSDRRLLSQAVDELMRWCTPVQVTQPRYA TEDLDVGGVTVRKGEQVVAVIGAAGHDPDRFPDPERFDITRNHRAPHEAHVGFGFGPHYC LGAALAHQETAIALDTLFDRFPSLALAVPPSALERQPFPGAWRLKSLPVRL
S18531 S18531 S16745 10-Sep-1999 10-Sep-1999 10-Sep-1999
cytochrome P450 eryF oxidoreductase (EC 1.-.-.-) Saccharopolyspora erythraea Saccharopolyspora erythraea Haydock, S.F. Dowson, J.A. Dhillon, N. Roberts, G.A. Cortes, J. Leadlay, P.F. Mol. Gen. Genet. 2301991120-128 Cloning and sequence analysis of genes involved in erythromycin biosynthesis in Saccharopolyspora erythraea: sequence similarities between EryG and a family of S-adenosylmethionine-dependent methyltransferases. MUID92079886 S18531 DNA 1-406 EMBLX60379 NIDg48941 PIDNCAA42927.1 PIDg48943 the authors translated the codon AGG for residue 190 as Lys eryF Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 238-375 406 complete MTTVPDLESDSFHVDWYRTYAELRETAPVTPVRFLGQDAWLVTGYDEAKAALSDLRLSSD PKKKYPGVEVEFPAYLGFPEDVRNYFATNMGTSDPPTHTRLRKLVSQEFTVRRVEAMRPR VEQITAELLDEVGDSGVVDIVDRFAHPLPIKVICELLGVDEKYRGEFGRWSSEILVMDPE RAEQRGQAAREVVNFILDLVERRRTEPGDDLLSALIRVQDDDDGRLSADELTSIALVLLL AGFEASVSLIGIGTYLLLTHPDQDQLALVRRDPSALPNAVEEILRYIAPPETTTRFAAEE VEIRGVAIPQYSTVLVANGAANRDPKQFPDPHRFDVTRDTRGHLSFGQGIHFCMGRPLAK LEGEVALRALFGRFPALSLGIDADDVVWRRSLLLRGIDHLPVRLDG
S51594 S51594 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 mycG oxidoreductase (EC 1.-.-.-) Micromonospora griseorubida Micromonospora griseorubida Inouye, M. Takada, Y. Muto, N. Beppu, T. Horinouchi, S. Mol. Gen. Genet. 2451994456-464 Characterization and expression of a P-450-like mycinamicin biosynthesis gene using a novel Micromonospora-Escherichia coli shuttle cosmid vector. MUID95107242 S51594 DNA 1-397 EMBLD16098 NIDg286050 PIDNBAA03672.1 PIDg303644 mycG GTG Bacillus cytochrome P450 CYP106 cytochrome P450 homology heme oxidoreductase domain cytochrome P450 homology 231-368 397 complete MTSAEPRAYPFNDVHGLTLAGRYGELQETEPVSRVRPPYGEEAWLVTRYEDVRAVLGDGR FVRGPSMTRDEPRTRPEMVKGGLLSMDPPEHSRLRRLVVKAFTARRAESLRPRAREIAHE LVDQMAATGQPADLVAMFARQLPVRVICELLGVPSADHDRFTRWSGAFLSTAEVTAEEMQ EAAEQAYAYMGDLIDRRRKEPTDDLVSALVQARDQQDSLSEQELLDLAIGLLVAGYESTT TQIADFVYLLMTRPELRRQLLDRPELIPSAVEELTRWVPLGVGTAFPRYAVEDVTLRGVT IRAGEPVLASTGAANRDQAQFPDADRIDVDRTPNQHLGFGHGVHHCLGAPLARVELQVAL EVLLQRLPGIRLGIPETQLRWSEGMLLRGPLELPVVW
JC5859 JC5859 10-Sep-1999 10-Sep-1999 16-Jun-2000
polyketide synthase cytochrome P450 chain 10 oxidoreductase (EC 1.-.-.-) Actinomadura hibisca Actinomadura hibisca Dairi, T. Hamano, Y. Igarashi, Y. Furumai, T. Oki, T. Biosci. Biotechnol. Biochem. 6119971445-1453 Cloning and nucleotide sequence of the putative polyketide synthase genes for pradimicin biosynthesis from Actinomadura hibisca. MUID97480928 JC5859 DNA 1-411 DDBJD87924 NIDg2580441 PIDNBAA23153.1 PIDg2580451 This enzyme is involved in pradimicin A biosynthesis. pms10 Bacillus cytochrome P450 CYP106 cytochrome P450 homology antibiotic biosynthesis oxidoreductase domain cytochrome P450 homology 245-382 411 complete MPSSKDAPTVDPRPDVTPAFPFRPDDPFQPPCEHARLRASDPVAKVVLPTGDHAWVVTRY ADVRFVTSDRRFSKEAVTRPGAPRLIPMQRGSKSLVIMDPPEHTRMRKIVSRAFTARRVE GMRAHVRDLTSGFVDEMVEHGPPADLIAHLALPLPVTVICEMLGVPPEDRPRFQDWTDRM LTIGAPALAQADEIKAAVGRLRGYLAELIDAKTAAPADDLLSLLSRAHADDGLSEEELLT FGMTLLAAGYHTTTAAITHSVYHLLREPSRYARLREDPSGIPAAVEELLRYGQIGGGAGA IRIAVEDVEVGGTLVRAGEAVIPLFNAANRDPEVFADPEELDLGRTDNPHIALGHGIHYC LGAPLARLELQVVLETLVERTPALRLAIDDADITWRPGLAFARPDALPIAW
S15809 S15809 S19629 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 CYP105C1 oxidoreductase (EC 1.-.-.-) Streptomyces sp. Streptomyces sp. Horii, M. Ishizaki, T. Paik, S.Y. Manome, T. Murooka, Y. J. Bacteriol. 17219903644-3653 An operon containing the genes for cholesterol oxidase and a cytochrome P-450-like protein from a Streptomyces sp. MUID90299781 S15809 DNA 1-381 EMBLM31939 Ishizaki, T. submitted to the EMBL Data Library February1990 S19629 DNA 1-144,'P',146-148,'H',150-381 EMBLM31939 NIDg153210 PIDNAAA26718.1 PIDg153211 CYP105C1 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 216-352 binding-site heme iron (Cys) (axial ligand) 358 predicted 381 complete MTQAAPVTFSTVRENYFGPPAEMQALRHKAPVTRTAFADGRPGWLVTGYSAARAVLSDSR FTARGEREHPAVPRAATLEDERCRRLIAGQFTARRMRQLTGRTERIVREHLDAMEHMGSP ADLVEHFALPVPSLVIAELLGVPPADREQFQHDTLRWGGFGRSTEEVTEAFVSLGGQLQR LVRLKRTEPGDDLLSGLIAADPALTDEELASIAFLLLVAGHGTTAHQIALGAFLLLEHPD QLAALRADPALTESAVEELLRHLSVVHHGPTRAALQDADIEGTPVKAGEVVVVSLGAANR DPARFERPDAVDVTREDTGHLAFGHGMHQCLGRQLARIELRVALTALLERFPHLRLACPA AEIPLRHDMQVYGADRLPVAW
A55578 A55578 S42052 10-Sep-1999 10-Sep-1999 10-Sep-1999
cytochrome P450 oxidoreductase (EC 1.-.-.-) Rhodococcus fascians plasmid Rhodococcus fascians Crespi, M. Vereecke, D. Temmerman, W. Van Montagu, M. Desomer, J. J. Bacteriol. 17619942492-2501 The fas operon of Rhodococcus fascians encodes new genes required for efficient fasciation of host plants. MUID94222824 A55578 preliminary DNA 1-399 GBZ29635 NIDg455000 PIDNCAA82741.1 PIDg455001 plasmid pFiD188 plasmid Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 235-371 399 complete MAGTADLPLEMRRNGLNPTEELAQVRDRDGVIPVGELYGAPAFLVCRYEDVRRIFADSNR FSNAHTPMFAIPSGGDVIEDELAAMRAGNLIGLDPPDHTRLRHILAAEFSVHRLSRLQPR IAEIVDSALDGLEQAGQPADLMDRYALPVSLLVLCELLGVPYADRDELRDRTARLLDLSA SAEQRAVAQREDRRYMATLVTRAQEQPGDDLLGILARKIGDNLSTDELISIISLIMLGGH ETTASMIGLSVLALLHHPEQAAMMIEDPNCVNSGIEELLRWLSVAHSQPPRMAVTEVQIA GVTIPAGSFVIPSLLAANRDSNLTDRPDDLDITRGVAGHLAFGHGVHFCLGHSLARMTLR TAVPAVLRRFPDLALSPSHDVRLRSASIVLGLEELQLTW
E69611 E69611 T44774 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 cypA oxidoreductase (EC 1.-.-.-) Bacillus subtilis Bacillus subtilis Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 E69611 nucleic acid sequence not shown translation not shown DNA 1-410 GBZ99117 GBAL009126 NIDg2634966 PIDNCAB14615.1 PIDg2635119 strain 168 Belitsky, B.R. Gustafsson, M.C.U. Sonenshein, A.L. von Wachenfeldt, C. J. Bacteriol. 17919975448-5457 An lrp-like gene of Bacillus subtilis involved in branched-chain amino acid transport. MUID97431495 T44774 translated from GB/EMBL/DDBJ DNA 1-410 EMBLY11043 NIDg1926275 PIDNCAA71937.1 PIDg1926278 strain 1A1 cypA Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 245-381 410 complete MSSKEKKSVTILTESQLSSRAFKDEAYEFYKELRKSQALYPLSLGALGKGWLISRYDDAI HLLKNEKLKKNYENVFTAKEKRPALLKNEETLTKHMLNSDPPDHNRLRTLVQKAFTHRMI LQLEDKIQHIADSLLDKVQPNKFMNLVDDYAFPLPIIVISEMLGIPLEDRQKFRVWSQAI IDFSDAPERLQENDHLLGEFVEYLESLVRKKRREPAGDLISALIQAESEGTQLSTEELYS MIMLLIVAGHETTVNLITNMTYALMCHHDQLEKLRQQPDLMNSAIEEALRFHSPVELTTI RWTAEPFILHGQEIKRKDVIIISLASANRDEKIFPNADIFDIERKNNRHIAFGHGNHFCL GAQLARLEAKIAISTLLRRCPNIQLKGEKKQMKWKGNFLMRALEELPISF
G69679 G69679 10-Sep-1999 10-Sep-1999 16-Jun-2000
polyketide hydroxylase (EC 1.-.-.-) pksS Bacillus subtilis Bacillus subtilis Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 G69679 nucleic acid sequence not shown translation not shown DNA 1-376 GBZ99113 GBAL009126 NIDg2634090 PIDNCAB13607.1 PIDg2634107 strain 168 pksS Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 240-376 376 complete MQMEKLMFHPHGKEFHHNPFSVLGRFREEEPIHRFELKRFGATYPAWLITRYDDCMAFLK DNRITRDVKNVMNQEQIKMLNVSEDIDFVSDHMLAKDTPDHTRLRSLVHQAFTPRTIENL RGSIEQIAEQLLDEMEKENKADIMKSFASPLPFIVISELMGIPKEDRSQFQIWTNAMVDT SEGNRELTNQALREFKDYIAKLIHDRRIKPKDDLISKLVHAEENGSKLSEKELYSMLFLL VVAGLETTVNLLGSGTLALLQHKKECEKLKQQPEMIATAVEELLRYTSPVVMMANRWAIE DFTYKGHSIKRGDMIFIGIGSANRDPNFFENPEILNINRSPNRHISFGFGIHFCLGAPLA RLEGHIAFKAAFEEIS
G69594 G69594 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 bioI oxidoreductase (EC 1.-.-.-) Bacillus subtilis Bacillus subtilis Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 G69594 nucleic acid sequence not shown translation not shown DNA 1-395 GBZ99119 GBAL009126 NIDg2635411 PIDNCAB14997.1 PIDg2635503 strain 168 bioI Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 232-367 395 complete MTIASSTASSEFLKNPYSFYDTLRAVHPIYKGSFLKYPGWYVTGYEETAAILKDARFKVR TPLPESSTKYQDLSHVQNQMMLFQNQPDHRRLRTLASGAFTPRTTESYQPYIIETVHHLL DQVQGKKKMEVISDFAFPLASFVIANIIGVPEEDREQLKEWAASLIQTIDFTRSRKALTE GNIMAVQAMAYFKELIQKRKRHPQQDMISMLLKGREKDKLTEEEAASTCILLAIAGHETT VNLISNSVLCLLQHPEQLLKLRENPDLIGTAVEECLRYESPTQMTARVASEDIDICGVTI RQGEQVYLLLGAANRDPSIFTNPDVFDITRSPNPHLSFGHGHHVCLGSSLARLEAQIAIN TLLQRMPSLNLADFEWRYRPLFGFRALEELPVTFE
I40208 I40208 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 BJ-1 CYP112 oxidoreductase (EC 1.-.-.-) Bradyrhizobium japonicum Bradyrhizobium japonicum Tully, R.E. Keister, D.L. Appl. Environ. Microbiol. 5919934136-4142 Cloning and mutagenesis of a cytochrome P-450 locus from Bradyrhizobium japonicum that is expressed anaerobically and symbiotically. I40208 preliminary translated from GB/EMBL/DDBJ DNA 1-401 EMBLU12678 NIDg529961 PIDNAAC28889.1 PIDg529962 CYP112 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 234-372 binding-site heme iron (Cys) (axial ligand) 350 predicted 401 complete MSEQQPLPTLPMWRVDHIEPSPEMLALRANGPIHRVRFPSGHEGWWVTGYDEAKAVLSDA AFRPAGMPPAAFTPDSVILGSPGWLVSHEGREHARLRAIVAPAFSDRRVKLLVQQVEAIA AHLFETLAAQPQPADLRRHLSFPLPAMVISALMGVLYEDHAFFAGLSDEVMTHQHESGPR SASRLAWEELRAYIRGKMRDKRQDPDDNLLTDLLAAVDQGKASEEEAVGLAAGMLVAGHE STVAQIEFGLHAMFRHPQQRERLVGDPSLVDKAVQEILRMYPPGAGWDGIMRYPRTDVTI AGEHIPAESKVLVGLPATSFDPHHFDDPEIFDIERQEKPHLAFSYGPHACIGVALARLEL KVVFGSIFQRLPALRLAVAPEQLKLRKEIITGGFEQFPVLW
I40209 I40209 10-Sep-1999 10-Sep-1999 03-Mar-2000
cytochrome P450 BJ-3 CYP114 oxidoreductase (EC 1.-.-.-) Bradyrhizobium japonicum Bradyrhizobium japonicum Tully, R.E. Keister, D.L. Appl. Environ. Microbiol. 5919934136-4142 Cloning and mutagenesis of a cytochrome P-450 locus from Bradyrhizobium japonicum that is expressed anaerobically and symbiotically. I40209 preliminary translated from GB/EMBL/DDBJ DNA 1-382 EMBLU12678 NIDg529961 PIDNAAC28890.1 PIDg529963 CYP114 TTG Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 204-351 binding-site heme iron (Cys) (axial ligand) 329 predicted 382 complete MLSRHADIFWAFKATGDAFRGPAPGELARYFSRAATSPSLNLLASTLAMKDPPTHTRLRR LISRDFTMGQIDNLRPSIARIVAARLDGITPALERGEAVDLHREFALALPMLVFAELFGM PQDDMFELAAGIGTILEGLGPHASDPQLAAADAASARVQAYFGDLIQRKRTDPRRDIVSM LVGAHDDDADTLSDAELISMLWGMLLGGFVTTAASIDHAVLAMLAYPEQRHWLQADAARV RAFVEEVLRCDAPAMFSSIPRIAQRDIELGGVVIPKNADVRVLIASGNRDPDAFADPDRF DPARFYGTSPGMSTDGKIMLSFGHGIHFCLGAQLARVQLAESLPRIQARFPTLAFAGQPT REPSAFLRTFRTLPVRLHAQGS
JC5150 JC5150 PC4246 A40401 JX0335 10-Sep-1999 10-Sep-1999 16-Jun-2000
nitric-oxide reductase (EC 1.7.99.7) cytochrome P450 55A1 cytochrome P450 norA nitric-oxide reductase A fungus (Fusarium oxysporum) Fusarium oxysporum Nakahara, K. Shoun, H. J. Biochem. 12019961082-1087 N-terminal processing and amino acid sequence of two isoforms of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum. MUID97164007 JC5150 preliminary mRNA 1-404 PC4246 preliminary protein 1-31;32-39;51-57;68-78;90-121;129-138;144-169;215-227;246-268;278-293;300-381;386-393 Kizawa, H. Tomura, D. Oda, M. Fukamizu, A. Hoshino, T. Gotoh, O. Yasui, T. Shoun, H. J. Biol. Chem. 266199110632-10637 Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum. MUID91244845 A40401 mRNA 2-404 GBM63340 NIDg168152 PIDNAAA33337.1 PIDg168153 Tomura, D. Obika, K. Fukamizu, A. Shoun, H. J. Biochem. 116199488-94 Nitric oxide reductase cytochrome P-450 gene, CYP 55, of the fungus Fusarium oxysporum containing a potential binding-site for FNR, the transcription factor involved in the regulation of anaerobic growth of Escherichia coli. MUID95096031 JX0335 DNA 2-404 DDBJD14517 NIDg285800 PIDNBAA03390.1 PIDg285801 strain MT-811 The expression of this protein is regulated in response to oxygen tension by an fumarate and nitrate reduction-like system. This enzyme is involved in fungal denitrification, acting as a nitric oxide reductase. CYP55A1 63/3; 99/2; 152/3; 190/2; 251/3; 304/3; 368/1 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein cytosol heme iron metalloprotein oxidoreductase product nitric-oxide reductase cytochrome P450 55A1 3-404 experimental domain cytochrome P450 homology 237-375 binding-site heme iron (Cys) (axial ligand) 353 predicted 404 complete TMASGAPSFPFSRASGPEPPAEFAKLRATNPVSQVKLFDGSLAWLVTKHKDVCFVATSEK LSKVRTRQGFPELSASGKQAAKAKPTFVDMDPPEHMHQRSMVEPTFTPEAVKNLQPYIQR TVDDLLEQMKQKGCANGPVDLVKEFALPVPSYIIYTLLGVPFNDLEYLTQQNAIRTNGSS TAREASAANQELLDYLAILVEQRLVEPKDDIISKLCTEQVKPGNIDKSDAVQIAFLLLVA GNATMVNMIALGVATLAQHPDQLAQLKANPSLAPQFVEELCRYHTASALAIKRTAKEDVM IGDKLVRANEGIIASNQSANRDEEVFENPDEFNMNRKWPPQDPLGFGFGDHRCIAEHLAK AELTTVFSTLYQKFPDLKVAVPLGKINYTPLNRDVGIVDLPVIF
S47520 S47520 10-Sep-1999 10-Sep-1999 16-Jun-2000
vitamin D-3 25-hydroxylase (EC 1.-.-.-) cytochrome P450 VD25 Amycolata autotrophica Amycolata autotrophica Kawauchi, H. Sasaki, J. Adachi, T. Hanada, K. Beppu, T. Horinouchi, S. Biochim. Biophys. Acta 12191994179-183 Cloning and nucleotide sequence of a bacterial cytochrome P-450(VD25) gene encoding vitamin D-3 25-hydroxylase. MUID94368852 S47520 DNA 1-398 GBD26543 NIDg559303 PIDNBAA05541.1 PIDg1225904 the sequence from Fig. 4 is inconsistent with that from Fig. 3 in having 296-Asp P450-VD25 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 238-369 binding-site heme iron (Cys) (axial ligand) 347 predicted 398 complete MTTDATDPRTTDAAPFPSNRSAPYRFSDGYAQLRDPPGPLRLGTRYDGRQAWVVVIHEAA RKLLASRFESADAHRTGFPFLTAGGRDMIGTNPTLFRMDDPEHARLRRMTISHYTVKRIK TISEFVEEVVLVFLRRMTISGPTADLVSQFLIGAGHMVICRLLGVPYEDHAFFQERSRVL LTLRSTPEEVRAAQDELLQYLARLARTKRERPDDAIISRLVARGEILREEDISDAMLLLI AGHATDANLTSMSLYALADRSEQYAALRADRSLVPGAVEDPLRYVAIADIATEDVPIRGR TIAAGNTQIAMGSSANLDHEYYEDPDALTARVEDLVHLAFGFGRHQCLGQNLARADQLRE DLMTARNDPTLRLAVPVQSSARLEGTTIQGVNELPVTW
A48495 A48495 10-Sep-1999 10-Sep-1999 10-Sep-1999
linalool 8-monooxygenase (EC 1.14.99.28) Pseudomonas incognita Pseudomonas incognita Ropp, J.D. Gunsalus, I.C. Sligar, S.G. J. Bacteriol. 17519936028-6037 Cloning and expression of a member of a new cytochrome P-450 family: cytochrome P-450lin (CYP111) from Pseudomonas incognita. MUID93388536 A48495 preliminary DNA 1-406 GBL23310 NIDg405542 PIDNAAA25810.1 PIDg405543 Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 242-377 406 complete MERPDLKNPDLYTQQVPHDIFARLRREEPVYWNPESDGSGFWAVLRHKDIIEVSRQPLLF SSAYENGGHRIFNENEVGLTNAGEAAVGVPFISLDPPVHTQYRKVIMPALSPARLGDIEQ RIRVRAEALIERIPLGEEVDLVPLLSAPLPLLTLAELLGLDPDCWYELYNWTNAFVGEDD PEFRKSPEDMAKVLGEFMGFCQELFESRRANPGPDIATLLANAEINGQPVALRDFIGNLT LTLVGGNETTRNSISHTIVTLSQQPDQWDILRQRPELLKTATAEMVRHASPVLHMRRTAM EDTEIGGQAIAKGDKVVLWYASGNRDESVFSDADRFDVTRTGVQHVGFGSGQHVCVGSRL AEMQLRVVFEILSTRVKRFELCSKSRRFRSNFLNGLKNLNVVLVPK
A42971 A42971 S27653 10-Sep-1999 10-Sep-1999 10-Sep-1999
cytochrome P450terp cytochrome P450-terpredoxin oxidoreductase (EC 1.-.-.-) Pseudomonas sp. Pseudomonas sp. Peterson, J.A. Lu, J.Y. Geisselsoder, J. Graham-Lorence, S. Carmona, C. Witney, F. Lorence, M.C. J. Biol. Chem. 267199214193-14203 Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. MUID92332528 A42971 preliminary DNA protein 1-428 EMBLM91440 NIDg151584 PIDNAAA25996.1 PIDg151587 sequence extracted from NCBI backbone (NCBIP:108469) Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 264-399 428 complete MDARATIPEHIARTVILPQGYADDEVIYPAFKWLRDEQPLAMAHIEGYDPMWIATKHADV MQIGKQPGLFSNAEGSEILYDQNNEAFMRSISGGCPHVIDSLTSMDPPTHTAYRGLTLNW FQPASIRKLEENIRRIAQASVQRLLDFDGECDFMTDCALYYPLHVVMTALGVPEDDEPLM LKLTQDFFGVHEPDEQAVAAPRQSADEAARRFHETIATFYDYFNGFTVDRRSCPKDDVMS LLANSKLDGNYIDDKYINAYYVAIATAGHDTTSSSSGGAIIGLSRNPEQLALAKSDPALI PRLVDEAVRWTAPVKSFMRTALADTEVRGQNIKRGDRIMLSYPSANRDEEVFSNPDEFDI TRFPNRHLGFGWGAHMCLGQHLAKLEMKIFFEELLPKLKSVELSGPPRLVATNFVGGPKN VPIRFTKA
F69611 F69611 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 cypX oxidoreductase (EC 1.-.-.-) Bacillus subtilis Bacillus subtilis Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 F69611 nucleic acid sequence not shown translation not shown DNA 1-405 GBZ99121 GBZ99122 GBAL009126 NIDg2636029 PIDNCAB15523.1 PIDg2636032 NIDg2635827 PIDg2636019 strain 168 cypX Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 230-375 405 complete MSQSIKLFSVLSDQFQNNPYAYFSQLREEDPVHYEESIDSYFISRYHDVRYILQHPDIFT TKSLVERAEPVMRGPVLAQMHGKEHSAKRRIVVRSFIGDALDHLSPLIKQNAENLLAPYL ERGKSDLVNDFGKTFAVCVTMDMLGLDKRDHEKISEWHSGVADFITSISQSPEARAHSLW CSEQLSQYLMPVIKERRVNPGSDLISILCTSEYEGMALSDKDILALILNVLLAATEPADK TLALMIYHLLNNPEQMNDVLADRSLVPRAIAETLRYKPPVQLIPRQLSQDTVVGGMEIKK DTIVFCMIGAANRDPEAFEQPDVFNIHREDLGIKSAFSGAARHLAFGSGIHNCVGAAFAK NEIEIVANIVLDKMRNIRLEEDFCYAESGLYTRGPVSLLVAFDGA
C70616 C70616 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv0136 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 C70616 nucleic acid sequence not shown translation not shown DNA 1-441 GBZ92770 GBAL123456 NIDg3261720 PIDNCAB07042.1 PIDg1877261 strain H37Rv Rv0136 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 263-410 binding-site heme iron (Cys) (axial ligand) 388 predicted 441 complete MSEVVTAAPAPPVVRLPPAVRGPKLFQGLAFVVSRRRLLGRFVRRYGKAFTANILMYGRV VVVADPQLARQVFTSSPEELGNIQPNLSRMFGSGSVFALDGDDHRRRRRLLAPPFHGKSM KNYETIIEEETLRETANWPQGQAFATLPSMMHITLNAILRAIFGAGGSELDELRRLIPPW VTLGSRLAALPKPKRDYGRLSPWGRLAEWRRQYDTVIDKLIEAERADPNFADRTDVLALM LRSTYDDGSIMSRKDIGDELLTLLAAGHETTAATLGWAFERLSRHPDVLAALVEEVDNGG HELRQAAILEVQRARTVIDFAARRVNPPVYQLGEWVIPRGYSIIINIAQIHGDPDVFPQP DRFDPQRYIGSKPSPFAWIPFGGGTRRCVGAAFANMEMDVVLRTVLRHFTLETTTAAGER SHGRGVAFTPKDGGRVVMRRR
A70707 A70707 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv0766c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 A70707 nucleic acid sequence not shown translation not shown DNA 1-402 GBZ80226 GBAL123456 NIDg3261638 PIDNCAB02396.1 PIDg1550644 strain H37Rv Rv0766c Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 236-372 402 complete MTVRVGDPELVLDPYDYDFHEDPYPYYRRLRDEAPLYRNEERNFWAVSRHHDVLQGFRDS TALSNAYGVSLDPSSRTSEAYRVMSMLAMDDPAHLRMRTLVSKGFTPRRIRELEPQVLEL ARIHLDSALQTESFDFVAEFAGKLPMDVISELIGVPDTDRARIRALADAVLHREDGVADV PPPAMAASIELMRYYADLIAEFRRRPANNLTSALLAAELDGDRLSDQEIMAFLFLMVIAG NETTTKLLANAVYWAAHHPGQLARVFADHSRIPMWVEETLRYDTSSQILARTVAHDLTLY DTTIPEGEVLLLLPGSANRDDRVFDDPDDYRIGREIGCKLVSFGSGAHFCLGAHLARMEA RVALGALLRRIRNYEVDDDNVVRVHSSNVRGFAHLPISVQAR
E70708 E70708 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv0778 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 E70708 preliminary nucleic acid sequence not shown translation not shown DNA 1-414 GBZ80226 GBAL123456 NIDg3261638 PIDNCAB02390.1 PIDg1550656 strain H37Rv Rv0778 Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 250-385 414 complete MTTAAGLSGIDLTDLDNFADGFPHHLFAIHRREAPVYWHRPTEHTPDGEGFWSVATYAET LEVLRDPVTYSSVTGGQRRFGGTVLQDLPVAGQVLNMMDDPRHTRIRRLVSSGLTPRMIR RVEDDLRRRARGLLDGVEPGAPFDFVVEIAAELPMQMICILLGVPETDRHWLFEAVEPGF DFRGSRRATMPRLNVEDAGSRLYTYALELIAGKRAEPADDMLSVVANATIDDPDAPALSD AELYLFFHLLFSAGAETTRNSIAGGLLALAENPDQLQTLRSDFELLPTAIEEIVRWTSPS PSKRRTASRAVSLGGQPIEAGQKVVVWEGSANRDPSVFDRADEFDITRKPNPHLGFGQGV HYCLGANLARLELRVLFEELLSRFGSVRVVEPAEWTRSNRHTGIRHLVVELRGG
H70752 H70752 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv1256c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 H70752 preliminary nucleic acid sequence not shown translation not shown DNA 1-405 GBZ77137 GBAL123456 NIDg3261593 PIDNCAB00896.1 PIDg1480330 strain H37Rv Rv1256c Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 240-376 405 complete MTSVMSHEFQLATAETWPNPWPMYRALRDHDPVHHVVPPQRPEYDYYVLSRHADVWSAAR DHQTFSSAQGLTVNYGELEMIGLHDTPPMVMQDPPVHTEFRKLVSRGFTPRQVETVEPTV RKFVVERLEKLRANGGGDIVTELFKPLPSMVVAHYLGVPEEDWTQFDGWTQAIVAANAVD GATTGALDAVGSMMAYFTGLIERRRTEPADDAISHLVAAGVGADGDTAGTLSILAFTFTM VTGGNDTVTGMLGGSMPLLHRRPDQRRLLLDDPEGIPDAVEELLRLTSPVQGLARTTTRD VTIGDTTIPAGRRVLLLYGSANRDERQYGPDAAELDVTRCPRNILTFSHGAHHCLGAAAA RMQCRVALTELLARCPDFEVAESRIVWSGGSYVRRPLSVPFRVTS
F70729 F70729 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv2266 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 F70729 preliminary nucleic acid sequence not shown translation not shown DNA 1-428 GBZ77163 GBAL123456 NIDg3261610 PIDNCAB00969.1 PIDg1449354 strain H37Rv Rv2266 Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 264-401 428 complete MGLNTAIATRVNGTPPPEVPIADIELGSLDFWALDDDVRDGAFATLRREAPISFWPTIEL PGFVAGNGHWALTKYDDVFYASRHPDIFSSYPNITINDQTPELAEYFGSMIVLDDPRHQR LRSIVSRAFTPKVVARIEAAVRDRAHRLVSSMIANNPDRQADLVSELAGPLPLQIICDMM GIPKADHQRIFHWTNVILGFGDPDLATDFDEFMQVSADIGAYATALAEDRRVNHHDDLTS SLVEAEVDGERLSSREIASFFILLVVAGNETTRNAITHGVLALSRYPEQRDRWWSDFDGL APTAVEEIVRWASPVVYMRRTLTQDIELRGTKMAAGDKVSLWYCSANRDESKFADPWTFD LARNPNPHLGFGGGGAHFCLGANLARREIRVAFDELRRQMPDVVATEEPARLLSQFIHGI KTLPVTWS
H70729 H70729 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv2268c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 H70729 preliminary nucleic acid sequence not shown translation not shown DNA 1-489 GBZ77163 GBAL123456 NIDg3261610 PIDNCAB00967.1 PIDg1449352 strain H37Rv Rv2268c Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 322-457 489 complete MTATQSPPEPAPDRVRLAGCPLAGTPDVGLTAQDATTALGVPTRRRASSGGIPVATSMWR DAQTVRTYGPAVAKALALRVAGKARSRLTGRHCRKFMQLTDFDPFDPAIAADPYPHYREL LAGERVQYNPKRDVYILSRYADVREAARNHDTLSSARGVTFSRGWLPFLPTSDPPAHTRM RKQLAPGMARGALETWRPMVDQLARELVGGLLTQTPADVVSTVAAPMPMRAITSVLGVDG PDEAAFCRLSNQAVRITDVALSASGLISLVQGFAGFRRLRALFTHRRDNGLLRECTVLGK LATHAEQGRLSDDELFFFAVLLLVAGYESTAHMISTLFLTLADYPDQLTLLAQQPDLIPS AIEEHLRFISPIQNICRTTRVDYSVGQAVIPAGSLVLLAWGAANRDPRQYEDPDVFRADR NPVGHLAFGSGIHLCPGTQLARMEGQAILREIVANIDRIEVVEPPTWTTNANLRGLTRLR VAVTPRVAP
H70730 H70730 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv2276 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 H70730 preliminary nucleic acid sequence not shown translation not shown DNA 1-396 GBZ77163 GBAL123456 NIDg3261610 PIDNCAB00959.1 PIDg1449344 strain H37Rv Rv2276 Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 230-367 396 complete MTATVLLEVPFSARGDRIPDAVAELRTREPIRKVRTITGAEAWLVSSYALCTQVLEDRRF SMKETAAAGAPRLNALTVPPEVVNNMGNIADAGLRKAVMKAITPKAPGLEQFLRDTANSL LDNLITEGAPADLRNDFADPLATALHCKVLGIPQEDGPKLFRSLSIAFMSSADPIPAAKI NWDRDIEYMAGILENPNITTGLMGELSRLRKDPAYSHVSDELFATIGVTFFGAGVISTGS FLTTALISLIQRPQLRNLLHEKPELIPAGVEELLRINLSFADGLPRLATADIQVGDVLVR KGELVLVLLEGANFDPEHFPNPGSIELDRPNPTSHLAFGRGQHFCPGSALGRRHAQIGIE ALLKKMPGVDLAVPIDQLVWRTRFQRRIPERLPVLW
B70677 B70677 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv3545c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 B70677 preliminary nucleic acid sequence not shown translation not shown DNA 1-433 GBZ82098 GBAL123456 NIDg3261664 PIDNCAB05061.1 PIDg1666115 strain H37Rv Rv3545c Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 265-399 433 complete MSWNHQSVEIAVRRTTVPSPNLPPGFDFTDPAIYAERLPVAEFAELRSAAPIWWNGQDPG KGGGFHDGGFWAITKLNDVKEISRHSDVFSSYENGVIPRFKNDIAREDIEVQRFVMLNMD APHHTRLRKIISRGFTPRAVGRLHDELQERAQKIAAEAAAAGSGDFVEQVSCELPLQAIA GLLGVPQEDRGKLFHWSNEMTGNEDPEYAHIDPKASSAELIGYAMKMAEEKAKNPADDIV TQLIQADIDGEKLSDDEFGFFVVMLAVAGNETTRNSITQGMMAFAEHPDQWELYKKVRPE TAADEIVRWATPVTAFQRTALRDYELSGVQIKKGQRVVMFYRSANFDEEVFQDPFTFNIL RNPNPHVGFGGTGAHYCIGANLARMTINLIFNAVADHMPDLKPISAPERLRSGWLNGIKH WQVDYTGRCPVAH
F70791 F70791 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv3685c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 F70791 preliminary nucleic acid sequence not shown translation not shown DNA 1-476 GBAL022121 GBAL123456 NIDg3261559 PIDNCAA18007.1 PIDg2960109 strain H37Rv Rv3685c Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 298-444 binding-site heme iron (Cys) (axial ligand) 422 predicted 476 complete MVLRSLASPAALTDPKRCASVVGVAAFAVRREHAPDALGGPPGLPAPRGFRAAFAAAYAV AYLAGGERRMLRLIRRYGPIMTMPILSLGDVAIVSDSALAKEVFTAPTDVLLGGEGVGPA AAIYGSGSMFVQEEPEHLRRRKLLTPPLHGAALDRYVPIIENSTRAAMHTWPVDRPFAML TVARSLMLDVIVKVIFGVDDPEEVRRLGRPFERLLNLGVSEQLTVRYALRRLGALRVWPA RARANTEIDDVVMALIAQRRADPRLGERHDVLSLLVSARGESGEQLSDSEIRDDLITLVL AGHETTATTLAWAFDLLLHHPDALRRVRAEAVGGGEAFTTAVINETLRVRPPAPLTARVA AQPLTIGGYRVEAGTRIVVHIIAINRSAEVYEHPHEFRPERFLGTRPQTYAWVPFGGGVK RCLGANFSMRELITVLHVLLREGEFTAVDDEPERIVRRSIMLVPRRGTRVRFRPAR
D70985 D70985 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv1666c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 D70985 preliminary nucleic acid sequence not shown translation not shown DNA 1-430 GBZ95617 GBAL123456 NIDg3242249 PIDNCAB09102.1 PIDg3242251 strain H37Rv Rv1666c Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 231-394 binding-site heme iron (Cys) (axial ligand) 372 predicted 430 complete MRYPLGEALLALYRWRGPLINAGVGGHGYTYLLGAEANRFVFANADAFSWSQTFESLVPV DGPTALIVSDGADHRRRRSVVAPGLRHHHVQRYVATMVSNIDTVIDGWQPGQRLDIYQEL RSAVRRSTAESLFGQRLAVHSDFLGEQLQPLLDLTRRPPQVMRLQQRVNSPGWRRAMAAR KRIDDLIDAQIADARTAPRPDDHMLTTLISGCSEEGTTLSDNEIRDSIVSLITAGYETTS GALAWAIYALLTVPGTWESAASEVARVLGGRVPAADDLSALTYLNGVVHETLRLYSPGVI SARRVLRDLWFDGHRIRAGRLLIFSAYVTHRLPEIWPEPTEFRPLRWDPNAADYRKPAPH EFIPFSGGLHRCIGAVMATTEMTVILARLVARAMLQLPAQRTHRIRAANFAALRPWPGLT VEIRKSAPAQ
G70932 G70932 10-Sep-1999 10-Sep-1999 21-Jul-2000
probable monoxygenase cytochrome P450 Rv0568 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 G70932 preliminary nucleic acid sequence not shown translation not shown DNA 1-472 GBAL021942 GBAL123456 NIDg3242298 PIDNCAA17439.1 PIDg2909627 strain H37Rv Rv0568 Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 258-410 binding-site heme iron (Cys) (axial ligand) 388 predicted 472 complete MSGTSSMGLPPGPRLSGSVQAVLMLRHGLRFLTACQRRYGSVFTLHVAGFGHMVYLSDPA AIKTVFAGNPSVFHAGEANSMLAGLLGDSSLLLIDDDVHRDRRRLMSPPFHRDAVARQAG PIAEIAAANIAGWPMAKAFAVAPKMSEITLEVILRTVIGASDPVRLAALRKVMPRLLNVG PWATLALANPSLLNNRLWSRLRRRIEEADALLYAEIADRRADPDLAARTDTLAMLVRAAD EDGRTMTERELRDQLITLLVAGHDTTATGLSWALERLTRHPVTLAKAVQAADASAAGDPA GDEYLDAVAKETLRIRPVVYDVGRVLTEAVEVAGYRLPAGVMVVPAIGLVHASAQLYPDP ERFDPDRMVGATLSPTTWLPFGGGNRRCLGATFAMVEMRVVLREILRRVELSTTTTSGER PKLKHVIMVPHRGARIRVRATRDVSATSQATAQGAGCPAARGGGPSRAVGSQ
H70526 H70526 10-Sep-1999 10-Sep-1999 21-Jul-2000
probable cytochrome P450 Rv0327c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 H70526 preliminary nucleic acid sequence not shown translation not shown DNA 1-449 GBZ96800 GBAL123456 NIDg3261800 PIDNCAB09576.1 PIDg2193948 strain H37Rv Rv0327c Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 259-405 binding-site heme iron (Cys) (axial ligand) 383 predicted 449 complete MASTLTTGLPPGPRLPRYLQSVLYLRFREWFLPAMHRKYGDVFSLRVPPYADNLVVYTRP EHIKEIFAADPRSLHAGEGNHILGFVMGEHSVLMTDEAEHARMRSLLMPAFTRAALRGYR DMIASVAREHITRWRPHATINSLDHMNALTLDIILRVVFGVTDPKVKAELTSRLQQIINI HPAILAGVPYPSLKRMNPWKRFFHNQTKIDEILYREIASRRIDSDLTARTDVLSRLLQTK DTPTKPLTDAELRDQLITLLLAGHETTAAALSWTLWELAHAPEIQSQVVWAAVGGDDGFL EAVLKEGMRRHTVIASTARKVTAPAEIGGWRLPAGTVVNTSILLAHASEVSHPKPTEFRP SRFLDGSVAPNTWLPFGGGVRRCLGFGFALTEGAVILQEIFRRFTITAAGPSKGETPLVR NITTVPKHGAHLRLIPQRRLGGLGDSDPP
B70511 B70511 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv1777 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 B70511 preliminary nucleic acid sequence not shown translation not shown DNA 1-434 GBZ97345 GBAL123456 NIDg3261824 PIDNCAB10567.1 PIDg2245328 strain H37Rv Rv1777 Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 271-407 434 complete MRRSPKGSPGAVLDLQRRVDQAVSADHAELMTIAKDANTFFGAESVQDPYPLYERMRAAG SVHRIANSDFYAVCGWDAVNEAIGRPEDFSSNLTATMTYTAEGTAKPFEMDPLGGPTHVL ATADDPAHAVHRKLVLRHLAAKRIRVMEQFTVQAADRLWVDGMQDGCIEWMGAMANRLPM MVVAELIGLPDPDIAQLVKWGYAATQLLEGLVENDQLVAAGVALMELSGYIFEQFDRAAA DPRDNLLGELATACASGELDTLTAQVMMVTLFAAGGESTAALLGSAVWILATRPDIQQQV RANPELLGAFIEETLRYEPPFRGHYRHVRNATTLDGTELPADSHLLLLWGAANRDPAQFE APGEFRLDRAGGKGHISFGKGAHFCVGAALARLEARIVLRLLLDRTSVIEAADVGGWLPS ILVRRIERLELAVQ
E70515 E70515 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv1880c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 E70515 preliminary nucleic acid sequence not shown translation not shown DNA 1-438 GBZ97193 GBAL123456 NIDg3261816 PIDNCAB10066.1 PIDg2225980 strain H37Rv Rv1880c Bacillus cytochrome P450 CYP106 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 267-403 binding-site heme iron (Cys) (axial ligand) 381 predicted 438 complete MKDKLHWLAMHGVIRGIAAIGIRRGDLQARLIADPAVATDPVPFYDEVRSHGALVRNRAN YLTVDHRLAHDLLRSDDFRVVSFGENLPPPLRWLERRTRGDQLHPLREPSLLAVEPPDHT RYRKTVSAVFTSRAVSALRDLVEQTAINLLDRFAEQPGIVDVVGRYCSQLPIVVISEILG VPEHDRPRVLEFGELAAPSLDIGIPWRQYLRVQQGIRGFDCWLEGHLQQLRHAPGDDLMS QLIQIAESGDNETQLDETELRAIAGLVLVAGFETTVNLLGNGIRMLLDTPEHLATLRQHP ELWPNTVEEILRLDSPVQLTARVACRDVEVAGVRIKRGEVVVIYLAAANRDPAVFPDPHR FDIERPNAGRHLAFSTGRHFCLGAALARAEGEVGLRTFFDRFPDVRAAGAGSRRDTRVLR GWSTLPVTLGPARSMVSP
H70807 H70807 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv3518c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 H70807 preliminary nucleic acid sequence not shown translation not shown DNA 1-398 GBAL022022 GBAL123456 NIDg3261554 PIDNCAA17755.1 PIDg2924455 strain H37Rv Rv3518c Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 227-362 398 complete MTEAPDVDLADGNFYASREARAAYRWMRANQPVFRDRNGLAAASTYQAVIDAERQPELFS NAGGIRPDQPALPMMIDMDDPAHLLRRKLVNAGFTRKRVKDKEASIAALCDTLIDAVCER GECDFVRDLAAPLPMAVIGDMLGVRPEQRDMFLRWSDDLVTFLSSHVSQEDFQITMDAFA AYNDFTRATIAARRADPTDDLVSVLVSSEVDGERLSDDELVMETLLILIGGDETTRHTLS GGTEQLLRNRDQWDLLQRDPSLLPGAIEEMLRWTAPVKNMCRVLTADTEFHGTALCAGEK MMLLFESANFDEAVFCEPEKFDVQRNPNSHLAFGFGTHFCLGNQLARLELSLMTERVLRR LPDLRLVADDSVLPLRPANFVSGLESMPVVFTPSPPLG
H70921 H70921 10-Sep-1999 10-Sep-1999 16-Jun-2000
cytochrome P450 Rv3121 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 H70921 preliminary nucleic acid sequence not shown translation not shown DNA 1-400 GBZ95150 GBAL123456 NIDg3250708 PIDNCAB08378.1 PIDg2076696 strain H37Rv Rv3121 Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 232-368 400 complete MTSTSIPTFPFDRPVPTEPSPMLSELRNSCPVAPIELPSGHTAWLVTRFDDVKGVLSDKR FSCRAAAHPSSPPFVPFVQLCPSLLSIDGPQHTAARRLLAQGLNPGFIARMRPVVQQIVD NALDDLAAAEPPVDFQEIVSVPIGEQLMAKLLGVEPKTVHELAAHVDAAMSVCEIGDEEV SRRWSALCTMVIDILHRKLAEPGDDLLSTIAQANRQQSTMTDEQVVGMLLTVVIGGVDTP IAVITNGLASLLHHRDQYERLVEDPGRVARAVEEIVRFNPATEIEHLRVVTEDVVIAGTA LSAGSPAFTSITSANRDSDQFLDPDEFDVERNPNEHIAFGYGPHACPASAYSRMCLTTFF TSLTQRFPQLQLARPFEDLERRGKGLHSVGIKELLVTWPT
C70929 C70929 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv1785c oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 C70929 preliminary nucleic acid sequence not shown translation not shown DNA 1-393 GBAL022021 GBAL123456 NIDg3250699 PIDNCAA17707.1 PIDg2924467 strain H37Rv Rv1785c Bacillus cytochrome P450 CYP106 cytochrome P450 homology oxidoreductase domain cytochrome P450 homology 229-364 393 complete MTTPGEDHAGSFYLPRLEYSTLPMAVDRGVGWKTLRDAGPVVFMNGWYYLTRREDVLAAL RNPKVFSSRKALQPPGNPLPVVPLAFDPPEHTRYRRILQPYFSPAALSKALPSLRRHTVA MIDAIAGRGECEAMADLANLFPFQLFLVLYGLPLEDRDRLIGWKDAVIAMSDRPHPTEAD VAAARELLEYLTAMVAERRRNPGPDVLSQVQIGEDPLSEIEVLGLSHLLILAGLDTVTAA VGFSLLELARRPQLRAMLRDNPKQIRVFIEEIVRLEPSAPVAPRVTTEPVTVGGMTLPAG SPVRLCMAAVNRDGSDAMSTDELVMDGKVHRHWGFGGGPHRCLGSHLARLELTLLVGEWL NQIPDFELAPDYAPEIRFPSKSFALKNLPLRWS
A32306 A32306 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 CYP103 cytochrome P450 pinF1 oxidoreductase (EC 1.-.-.-) Agrobacterium tumefaciens plasmid pTiA6 Agrobacterium tumefaciens Kanemoto, R.H. Powell, A.T. Akiyoshi, D.E. Regier, D.A. Kerstetter, R.A. Nester, E.W. Hawes, M.C. Gordon, M.P. J. Bacteriol. 17119892506-2512 Nucleotide sequence and analysis of the plant-inducible locus pinF from Agrobacterium tumefaciens. MUID89213933 A32306 DNA 1-422 GBM19352 NIDg142260 PIDNAAA82502.1 PIDg142261 pinF1 plasmid Agrobacterium plasmid cytochrome P450 pinF1 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 255-391 binding-site heme iron (Cys) (axial ligand) 369 predicted 422 complete MIANSSTDVSVADQKFLNVAKSNQIDPDAVPISRLDSEGHSIFAEWRPKRPFLRREDGIF LVLRADHIFLLGTDPRTRQIETELMLNRGVKAGAVFDFIDHSMLFSNGETHGKRRSGLSK AFSFRMVEALRPEIAKITECLWDDLQKVDDFNFTEMYASQLPALTIASVLGLPSEDTPFF TRLVYKVSRCLSPSWRDEEFEEIEASAIELQDYVRSVIADSGRRMRDDFLSRYLKAVREA GTLSPIEEIMQLMLIILAGSDTTRTAMVMVTALALQNPALWSSLRGNQSYVAAAVEEGLR FEPPVGSFPRLALKDIDLDGYVLPKGSLLALSVMSGLRDEKHYEHPQLFDVGRQQMRWHL GFGAGVHRCLGETLARIELQEGLRTLLRRAPNLAVVGDWPRMMGHGGIRRATDMMVKLSF DL
B32306 B32306 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 CYP104 cytochrome P450 pinF2 oxidoreductase (EC 1.-.-.-) Agrobacterium tumefaciens plasmid pTiA6 Agrobacterium tumefaciens Kanemoto, R.H. Powell, A.T. Akiyoshi, D.E. Regier, D.A. Kerstetter, R.A. Nester, E.W. Hawes, M.C. Gordon, M.P. J. Bacteriol. 17119892506-2512 Nucleotide sequence and analysis of the plant-inducible locus pinF from Agrobacterium tumefaciens. MUID89213933 B32306 DNA 1-407 GBM19352 NIDg142260 PIDNAAA82503.1 PIDg142262 pinF2 plasmid Agrobacterium plasmid cytochrome P450 pinF2 cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 244-379 binding-site heme iron (Cys) (axial ligand) 356 predicted 407 complete MEERRVSISSITWRFPMLFAPVDDVTTIDDLTLDPYPIYRRMRVQNPVVHVASVRRTFLT KAFDTKMVKDDPSRFSSDDPSTPMKPAFQAHTLMRKDGTEHARERMAMARAFAPKAIADH WAPIYRDIVNEYLDRLPRGDTVDLFAEICGPVAARILAHILGICEASDVEIIRWSQRLID GAGNFGWRSELFERSDEANAEMNCLFNDLVKKHRSAPNPSAFATMLNAPDPIPLSQIYAN IKIAIGGGVNEPRDALGTILYGLLTNPEQLEEVKRQQCWGQAFEEGLRWVAPIQASSRLV REDTEIRGFIVPKGDIVMTIQASANRDEDVFEDGESFNVFRPKSAHQSFGSGPHHCPGAQ ISRQTVGAIMLPILFDRFPDMILPHPELVQWRGFGFRGPINLPVTLR
I40212 I40212 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 BJ-4 CYP117 oxidoreductase (EC 1.-.-.-) Bradyrhizobium japonicum Bradyrhizobium japonicum Tully, R.E. Keister, D.L. Appl. Environ. Microbiol. 5919934136-4142 Cloning and mutagenesis of a cytochrome P-450 locus from Bradyrhizobium japonicum that is expressed anaerobically and symbiotically. I40212 preliminary translated from GB/EMBL/DDBJ DNA 1-356 EMBLU12678 NIDg529961 PIDNAAC28893.1 PIDg529966 CYP117 TTG Bradyrhizobium cytochrome P450 CYP117 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 164-323 binding-site heme iron (Cys) (axial ligand) 301 predicted 356 complete MFGGTLVAQDGIAHRQARDAIQAALLPKGLTLAGIGELFAPVIRARVQRWRERGDVTILR ETGDLMLKLIFSLMGIPAQDLPGWHRKYRQLLQLIVAPPVDLPGLPLRRGRAARDWIDAR LREFVRAAREHASRTGLINDMVSAFDRSDDALSDDVLVANIRLLLLGGHDTTASTMAWMV IELARQPGLWDALVEEAQRVGAVPTRHADLAQCPVAEALFRETLRVHPATPLLVRRALRE LRIGQQRIPTGTDLCIPLLHFSTSALLHEAPDQFRLARWLQRTEPIRPVDMLQFGTGPHF CMGYHLVWLELVQFCIALALTMHEAGVRPRLLSGVEKGRRYYPTAHPSMTIRIGFS
D70649 D70649 10-Sep-1999 10-Sep-1999 21-Jul-2000
cytochrome P450 Rv3059 oxidoreductase (EC 1.-.-.-) Mycobacterium tuberculosis (strain H37RV) Mycobacterium tuberculosis Cole, S.T. Brosch, R. Parkhill, J. Garnier, T. Churcher, C. Harris, D. Gordon, S.V. Eiglmeier, K. Gas, S. Barry III, C.E. Tekaia, F. Badcock, K. Basham, D. Brown, D. Chillingworth, T. Connor, R. Davies, R. Devlin, K. Feltwell, T. Gentles, S. Hamlin, N. Holroyd, S. Hornsby, T. Jagels, K. Krogh, A. McLean, J. Moule, S. Murphy, L. Oliver, S. Osborne, J. Quail, M.A. Rajandream, M.A. Rogers, J. Rutter, S. Seeger, K. Skelton, S. Squares, S. Sqares, R. Sulston, J.E. Taylor, K. Whitehead, S. Barrell, B.G. Nature 3931998537-544 Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. MUID98295987 D70649 nucleic acid sequence not shown translation not shown DNA 1-492 GBZ83866 GBAL123456 NIDg3261691 PIDNCAB06263.1 PIDg1781154 strain H37Rv Rv3059 Mycobacterium cytochrome P450 Rv3059 cytochrome P450 homology chromoprotein heme iron metalloprotein oxidoreductase domain cytochrome P450 homology 300-461 binding-site heme iron (Cys) (axial ligand) 439 predicted 492 complete MATIHPPAYLLDQAKRRFTPSFNNFPGMSLVEHMLLNTKFPEKKLAEPPPGSGLKPVVGD AGLPILGHMIEMLRGGPDYLMFLYKTKGPVVFGDSAVLPGVAALGPDAAQVIYSNRNKDY SQQGWVPVIGPFFHRGLMLLDFEEHMFHRRIMQEAFVRSRLAGYLEQMDRVVSRVVADDW VVNDARFLVYPAMKALTLDIASMVFMGHEPGTDHELVTKVNKAFTITTRAGNAVIRTSVP PFTWWRGLRARELLENYFTARVKERREASGNDLLTVLCQTEDDDGNRFSDADIVNHMIFL MMAAHDTSTSTATTMAYQLAAHPEWQQRCRDESDRHGDGPLDIESLEQLESLDLVMNESI RLVTPVQWAMRQTVRDTELLGYYLPKGTNVIAYPGMNHRLPEIWTDPLTFDPERFTEPRN EHKRHRYAFTPFGGGVHKCIGMVFDQLEIKTILHRLLRRYRLELSRPDYQPRWDYSAMPI PMDGMPIVLRPR
O4PSCP A25660 S34614 C60886 A00194 30-Apr-1982 31-Dec-1993 03-Mar-2000
camphor 5-monooxygenase (EC 1.14.15.1) cytochrome P450 101 cytochrome P450-CAM Pseudomonas putida plasmid CAM Pseudomonas putida Unger, B.P. Gunsalus, I.C. Sligar, S.G. J. Biol. Chem. 26119861158-1163 Nucleotide sequence of the Pseudomonas putida cytochrome P-450-cam gene and its expression in Escherichia coli. MUID86111751 A25660 DNA 1-415 GBM12546 NIDg151114 PIDNAAA25760.1 PIDg151115 Aramaki, H. Koga, H. Sagara, Y. Hosoi, M. Horiuchi, T. Biochim. Biophys. Acta 1174199391-94 Complete nucleotide sequence of the 5-exo-hydroxycamphor dehydrogenase gene on the CAM plasmid of Pseudomonas putida (ATCC 17453). MUID93326643 S34614 not compared with conceptual translation DNA 1-42 PpG1; ATCC 17453; CAM plasmid Romeo, C. Moriwaki, N. Yasunobu, K.T. Gunsalus, I.C. Koga, H. J. Protein Chem. 61987253-261 Identification of the coding region for the putidaredoxin reductase gene from the plasmid of Pseudomonas putida. C60886 DNA 408-415 Haniu, M. Armes, L.G. Yasunobu, K.T. Shastry, B.A. Gunsalus, I.C. J. Biol. Chem. 257198212664-12671 Amino acid sequence of the Pseudomonas putida cytochrome P-450. II. Cyanogen bromide peptides, acid cleavage peptides, and the complete sequence. MUID83030788 A00194 protein 2-55,58-276,'Q',278-361,'S',363-407,'N',409-415 camC CYP101 plasmid catalyzes hydroxylation of camphor to yield 5-exo-hydroxycamphor; electron transfer; monooxygenase; oxidoreductase Pseudomonas plasmid camphor 5-monooxygenase cytochrome P450 homology chromoprotein electron transfer heme iron metalloprotein monooxygenase oxidoreductase domain cytochrome P450 homology 246-380 binding-site heme iron (Cys) (axial ligand) 358 experimental 415 complete MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVV GMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKY LTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAK RMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGR ILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV
FECL2P JH0804 S34628 A24460 S31452 28-Dec-1987 28-Dec-1987 11-Jun-1999
ferredoxin [2Fe-2S] Clostridium pasteurianum Clostridium pasteurianum Fujinaga, J. Meyer, J. Biochem. Biophys. Res. Commun. 19219931115-1122 Cloning and expression in Escherichia coli of the gene encoding the [2Fe-2S] ferredoxin from Clostridium pasteurianum. MUID93282812 JH0804 DNA 1-102 EMBLZ19005 NIDg40561 PIDNCAA79492.1 PIDg40563 Meyer, J. Biochim. Biophys. Acta 11741993108-110 Cloning and sequencing of the gene encoding the [2Fe-2S] ferredoxin from Clostridium pasteurianum. MUID93326627 S34628 DNA 1-102 EMBLZ19005 NIDg40561 PIDNCAA79492.1 PIDg40563 Meyer, J. Bruschi, M.H. Bonicel, J.J. Bovier-Lapierre, G.E. Biochemistry 2519866054-6061 Amino acid sequence of [2Fe-2S] ferredoxin from Clostridium pasteurianum. MUID87076518 A24460 protein 1-102 Meyer, J. Fujinaga, J. Gaillard, J. Lutz, M. Biochemistry 33199413642-13650 Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster. MUID95034798 annotation iron-sulfur cluster ligands Cys-14 is not a ligand for the iron-sulfur cluster the fourth ligand was not determined Golinelli, M.P. Akin, L.A. Crouse, B.R. Johnson, M.K. Meyer, J. Biochemistry 3519968995-9002 Cysteine ligand swapping on a deletable loop of the [2Fe-2S] ferredoxin from Clostridium pasteurianum. MUID96280659 annotation iron-sulfur cluster ligands Cys-24 is normally a ligand for the 2Fe-2S cluster. The binding loop is sufficiently flexible for Cys-14 also to serve as a ligand when Cys-24 is converted to Ala by mutagenesis. Clostridium ferredoxin [2Fe-2S] 2Fe-2S electron transfer iron-sulfur protein metalloprotein binding-site 2Fe-2S cluster (Cys) (covalent) 11,24,56,60 experimental 102 complete MVNPKHHIFVCTSCRLNGKQQGFCYSKNSVEIVETFMEELDSRDLSSEVMVNNTGCFGIC SQGPIVVVYPEGVWYGNVTADDVEEIVESHIENGEVVKRLQI
JC7085 JC7085 D70310 20-Apr-2000 20-Apr-2000 20-Apr-2000
ferredoxin [2Fe-2S] fdx4 [validated] Aquifex aeolicus Aquifex aeolicus Chatelet, C. Gaillard, J. Petillot, Y. Louwagie, M. Meyer, J. Biochem. Biophys. Res. Commun. 2611999885-889 A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex aeolicus. MUID99373173 JC7085 DNA 1-111 this corrects the sequence in reference A70300 a C is inserted in nucleotide sequence GB:AE000674 after position 151 Deckert, G. Warren, P.V. Gaasterland, T. Young, W.G. Lenox, A.L. Graham, D.E. Overbeek, R. Snead, M.A. Keller, M. Aujay, M. Huber, R. Feldman, R.A. Short, J.M. Olson, G.J. Swanson, R.V. Nature 3921998353-358 The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. MUID98196666 D70310 nucleic acid sequence not shown translation not shown DNA 47-111 GBAE000674 NIDg2982850 PIDNAAC06474.1 PIDg2982853 GBAE000657 strain VF5 this predicted open reading frame is incomplete at the amino end compared with other members of the superfamily this sequence is corrected in reference JC7085 fdx4 Clostridium ferredoxin [2Fe-2S] 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] fdx4 2-111 predicted binding-site 2Fe-2S cluster (Cys) (covalent) 10,23,56,60 predicted 111 complete MAEFKHVFVCVQDRPPGHPQGSCAQRGSREVFQAFMEKIQTDPQLFMTTVITPTGCMNAC MMGPVVVVYPDGVWYGQVKPEDVDEIVEKHLKGGEPVERLVISKGKPPGMF
FEHS S35235 A00220 24-Apr-1984 10-Oct-1997 28-Jan-2000
ferredoxin [2Fe-2S] [validated] Halobacterium salinarum Halobacterium salinarum Pfeifer, F. Griffig, J. Oesterhelt, D. Mol. Gen. Genet. 239199366-71 The fdx gene encoding the [2Fe-2S] ferredoxin of Halobacterium salinarium (H. halobium). MUID93288008 S35235 DNA 1-129 EMBLX68103 NIDg311840 PIDNCAA48224.1 PIDg311841 strain R1 the source is designated as Halobacterium salinarium (H. halobium) Hase, T. Wakabayashi, S. Matsubara, H. Kerscher, L. Oesterhelt, D. Rao, K.K. Hall, D.O. J. Biochem. 8319781657-1670 Complete amino acid sequence of Halobacterium halobium ferredoxin containing an N(epsilon)-acetyllysine residue. MUID78218096 A00220 protein 2-129 NRL R1 strain M1 the source is designated as Halobacterium halobium fdx redox cofactor for various oxidoreductases [validated; MUID:78218096] ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S acetyllysine electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 2-129 experimental domain ferredoxin [2Fe-2S] homology 49-104 binding-site 2Fe-2S cluster (Cys) (covalent) 64,69,72,103 predicted binding-site acetyl (Lys) (covalent) 119 experimental 129 complete MPTVEYLNYETLDDQGWDMDDDDLFEKAADAGLDGEDYGTMEVAEGEYILEAAEAQGYDW PFSCRAGACANCASIVKEGEIDMDMQQILSDEEVEEKDVRLTCIGSPAADEVKIVYNAKH LDYLQNRVI
FEHSX A00221 14-Nov-1983 14-Nov-1983 23-Mar-2001
ferredoxin [2Fe-2S] [validated] Haloarcula marismortui Haloarcula marismortui Hase, T. Wakabayashi, S. Matsubara, H. Mevarech, M. Werber, M.M. Biochim. Biophys. Acta 6231980139-145 Amino acid sequence of 2Fe-2S ferredoxin from an extreme halophile, Halobacterium of the Dead Sea. MUID80198519 A00221 protein 1-128 the source is designated as Halobacterium sp. from the Dead Sea Frolow, F. Harel, M. Sussman, J.L. Shoham, M. submitted to the Brookhaven Protein Data Bank April1996 PDB1DOI annotation X-ray crystallography, 1.9 angstroms, residues 1-128 Frolow, F. Harel, M. Sussman, J.L. Mevarech, M. Shoham, M. Nat. Struct. Biol. 31996452-458 Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. MUID96196882 annotation X-ray crystallography, 1.9 angstroms Sussman, J.L. Brown, J.H. Shoham, M. Iron-Sulfur Protein Research, Matsubara, H., et al., eds., pp.69-82, Japan Sci. Soc. Press, Tokyo 1986 X-ray structural studies on a salt-loving ferredoxin from Halobacterium of the Dead Sea. annotation X-ray crystallography, 2.2 angstroms redox cofactor for various oxidoreductases [validated; MUID:80198519] ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S acetyllysine electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-128 experimental domain ferredoxin [2Fe-2S] homology 48-103 binding-site 2Fe-2S cluster (Cys) (covalent) 63,68,71,102 experimental binding-site acetyl (Lys) (covalent) 118 experimental 128 complete PTVEYLNYEVVDDNGWDMYDDDVFGEASDMDLDDEDYGSLEVNEGEYILEAAEAQGYDWP FSCRAGACANCAAIVLEGDIDMDMQQILSDEEVEDKNVRLTCIGSPDADEVKIVYNAKHL DYLQNRVI
B39181 B39181 S16368 03-Dec-1999 03-Dec-1999 03-Dec-1999
ferredoxin [2Fe-2S]-like protein nahG-nahH intergenic region Pseudomonas putida (strain PpG7) Pseudomonas putida You, I.S. Ghosal, D. Gunsalus, I.C. Biochemistry 3019911635-1641 Nucleotide sequence analysis of the Pseudomonas putida PpG7 salicylate hydroxylase gene (nahG) and its 3'-flanking region. MUID91129237 B39181 DNA 1-108 GBM60055 GBJ05317 NIDg151380 PIDNAAA25898.1 PIDg151382 Harayama, S. Polissi, A. Rekik, M. FEBS Lett. 285199185-88 Divergent evolution of chloroplast-type ferredoxins. MUID91293320 S16368 DNA 1-108 GBX61466 GBS40145 NIDg311896 PIDNCAA43701.1 PIDg311897 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein domain ferredoxin [2Fe-2S] homology 24-81 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,80 predicted 108 complete MSEVFEITVQPGGERFVCQPQQSALHAMETQGKRCLPVGCRGGGCGLCKVRVLAGDYESG RVSCKHLPVEAREQGYALACRLFARSDLCIERYSKPCSESTVDQQQRE
S54762 S54762 B58972 S44309 S47420 03-Dec-1999 03-Dec-1999 03-Dec-1999
ferredoxin [2Fe-2S]-like protein phlG Pseudomonas putida Pseudomonas putida Herrmann, H. Mueller, C. Schmidt, I. Mahnke, J. Petruschka, L. Hahnke, K. Mol. Gen. Genet. 2471995240-246 Localization and organization of phenol degradation genes of Pseudomonas putida strain H. MUID95272534 S54762 nucleic acid sequence not shown translation not shown DNA 1-101 EMBLX80765 NIDg527546 PIDNCAA56746.1 PIDg527553 the nucleotide sequence was submitted to the EMBL Data Library, July 1994 Ng, L.C. Shingler, V. Sze, C.C. Poh, C.L. Gene 151199429-36 Cloning and sequences of the first eight genes of the chromosomally encoded (methyl) phenol degradation pathway from Pseudomonas putida P35X. MUID95129877 B58972 DNA 1-72,'GE',75-101 EMBLX79063 NIDg483477 PIDNCAA55666.1 PIDg483484 strain P35X (NCBI 9869) the nucleotide sequence was submitted to the EMBL Data Library, April 1994 phlG ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein domain ferredoxin [2Fe-2S] homology 25-82 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,81 predicted 101 complete MSSPPFQVHETNSGQSFTCRPDQSVLRAMEEQGKRCVPVGCRGGGCGLCKVRVLSGDYQC GRMSCSQVPPEAAQQGLALACQLYPRADLYIESLRQVRSNP
S24417 S24417 03-Dec-1999 03-Dec-1999 03-Dec-1999
ferredoxin [2Fe-2S]-like protein dmpQ Pseudomonas putida Pseudomonas putida Shingler, V. Powlowski, J. Marklund, U. J. Bacteriol. 1741992711-724 Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. MUID92121108 S24417 DNA 1-112 EMBLX60657 NIDg45687 PIDNCAA43064.1 PIDg45688 dmpQ ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein domain ferredoxin [2Fe-2S] homology 25-82 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,81 predicted 112 complete MNRAGYEIRETVSGQTFRCLPDQSVLSAMEQQGKRCVPVGCRGGGCGLCKVRVLSGTYQC HKMSCNHVPPEAAKQGLALACQLFPQTDLNIECLRRQGPGDHNNKNQQEVSS
S16193 S16193 S23486 03-Dec-1999 03-Dec-1999 03-Dec-1999
ferredoxin [2Fe-2S]-like protein xylT Pseudomonas putida plasmid pWW0 Pseudomonas putida Harayama, S. Polissi, A. Rekik, M. FEBS Lett. 285199185-88 Divergent evolution of chloroplast-type ferredoxins. MUID91293320 S16193 DNA 1-112 EMBLX61467 NIDg311898 PIDNCAA43702.1 PIDg311899 Neidle, E.L. Hartnett, C. Ornston, L.N. Bairoch, A. Rekik, M. Harayama, S. Eur. J. Biochem. 2041992113-120 Cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. MUID92155191 S23486 nucleic acid sequence not shown translation not shown DNA 1-112 EMBLM64747 NIDg151718 PIDNAAA26051.1 PIDg151723 the nucleotide sequence was submitted to the EMBL Data Library, March 1992 xylT plasmid pWW0 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein domain ferredoxin [2Fe-2S] homology 25-82 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,81 predicted 112 complete MNSAGYEVFEVLSGQSFRCAEGQSVLRAMEAQGKRCIPVGCRGGGCGLCRVRVLSGAYRS GRMSRGHVPAKAAAEALALACQVFPQTDLTIEYFRHVGGNKPDNMNYEEVTS
FEPM1 S11495 S06468 S07445 30-Sep-1991 30-Sep-1991 11-Jun-1999
ferredoxin [2Fe-2S] I precursor garden pea garden pea Pisum sativum Elliott, R.C. Pedersen, T.J. Fristensky, B. White, M.J. Dickey, L.F. Thompson, W.F. Plant Cell 11989681-690 Characterization of a single copy gene encoding ferredoxin I from pea. MUID92393406 S11495 DNA 1-149 GBM31713 EMBLX14207 NIDg169086 PIDNAAA33665.1 PIDg169087 Dobres, M.S. Elliott, R.C. Watson, J.C. Thompson, W.F. Plant Mol. Biol. 8198753-59 A phytochrome regulated pea transcript encodes ferredoxin I. S06468 mRNA 31-130 EMBLM17107 Dutton, J.E. Rogers, L.J. Haslett, B.G. Takruri, I.A.H. Gleaves, J.T. Boulter, D. J. Exp. Bot. 311980379-391 Comparative studies on the properties of two ferredoxins from Pisum sativum L. S07445 protein 53-58,'I',60-84,'L',86-92 FedI ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S chloroplast electron transfer iron-sulfur protein metalloprotein domain transit peptide (chloroplast) 1-52 predicted product ferredoxin [2Fe-2S] 53-149 experimental domain ferredoxin [2Fe-2S] homology 76-130 binding-site 2Fe-2S cluster (Cys) (covalent) 91,96,99,129 predicted 149 complete MATTPALYGTAVSTSFLRTQPMPMSVTTTKAFSNGFLGLKTSLKRGDLAVAMASYKVKLV TPDGTQEFECPSDVYILDHAEEVGIDLPYSCRAGSCSSCAGKVVGGEVDQSDGSFLDDEQ IEAGFVLTCVAYPTSDVVIETHKEEDLTA
FESP1 S00437 A00228 S13386 13-Jun-1983 31-Mar-1992 11-Jun-1999
ferredoxin [2Fe-2S] I precursor spinach spinach Spinacia oleracea Wedel, N. Bartling, D. Herrmann, R.G. Bot. Acta 1011988295-300 Analysis of cDNA clones encoding the entire ferredoxin I precursor polypeptide from spinach. S00437 mRNA 1-147 GBM35660 NIDg170108 PIDNAAA34028.1 PIDg170109 Matsubara, H. Sasaki, R.M. J. Biol. Chem. 24319681732-1757 Spinach ferredoxin. II. Tryptic, chymotryptic, and thermolytic peptides, and complete amino acid sequence. MUID68243193 A00228 protein 51-147 there may be variants with 81-Lys and 83-Met and a possible deletion of 141-Lys Morigasaki, S. Takata, K. Sanada, Y. Wada, K. Yee, B.C. Shin, S. Buchanan, B.B. Arch. Biochem. Biophys. 283199075-80 Novel forms of ferredoxin and ferredoxin-NADP reductase from spinach roots. MUID91053194 S13386 protein 51-69 leaf ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S chloroplast electron transfer iron-sulfur protein metalloprotein domain transit peptide (chloroplast) 1-50 predicted product ferredoxin [2Fe-2S] I 51-147 experimental domain ferredoxin [2Fe-2S] homology 74-128 binding-site 2Fe-2S cluster (Cys) (covalent) 89,94,97,127 predicted 147 complete MAATTTTMMGMATTFVPKPQAPPMMAALPSNTGRSLFGLKTGSRGGRMTMAAYKVTLVTP TGNVEFQCPDDVYILDAAEEEGIDLPYSCRAGSCSSCAGKLKTGSLNQDDQSFLDDDQID EGWVLTCAAYPVSDVTIETHKEEELTA
FESP2 A00231 13-Jun-1983 13-Jun-1983 13-Nov-1998
ferredoxin [2Fe-2S] II spinach spinach Spinacia oleracea Takahashi, Y. Hase, T. Wada, K. Matsubara, H. Plant Cell Physiol. 241983189-198 Ferredoxins in developing spinach cotyledons: the presence of two molecular species. A00231 protein 1-97 cv. Munstarlander ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-97 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 97 complete ATYKVTLVTPSGSQVIECGDDEYILDAAEEKGMDLPYSCRAGACSSCAGKVTSGSVDQSD QSFLEDGQMEEGWVLTCIAYPTGDVTIETHKEEELTA
FELG A92055 A93771 A00232 07-May-1981 07-May-1981 31-Mar-2000
ferredoxin [2Fe-2S] white popinac white popinac Leucaena leucocephala Benson, A.M. Yasunobu, K.T. J. Biol. Chem. 2441969955-963 Non-heme iron proteins. X. The amino acid sequences of ferredoxins from Leucaena glauca. MUID69184140 A92055 protein 1-96 sequence heterogeneity in several positions: Glu and Asp at position 33, Gly and Ala at position 96, and either 6-Leu and 12-Pro or 6-Val and 12-Ala Benson, A.M. Yasunobu, K.T. Proc. Natl. Acad. Sci. U.S.A. 6319691269-1273 Nonheme iron proteins, XI. Some genetic aspects. MUID70050801 A93771 protein 1-96 ferredoxin from individual trees was analyzed half of the molecules contained 6-Leu and 12-Pro, and the other half contained 6-Val and 12-Ala 66% 96-Gly and 34% 96-Ala were also found ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-96 experimental domain ferredoxin [2Fe-2S] homology 23-77 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,76 predicted 96 complete tentative AFKVKLLTPDGPKEFECPDDVY.ILDQAEEL.GIELPY.SCRAGSCSSCAGKLVEGDLDQ SDQSFLDDEQIEEGW.VL.TCAAY.PRSDVVIETHKEEELTG
FEED A00233 30-Apr-1980 30-Apr-1980 31-Mar-2000
ferredoxin [2Fe-2S] European elder European elder Sambucus nigra Takruri, I.A.H. Boulter, D. Phytochemistry 1819791481-1484 The amino acid sequence of ferredoxin from Sambucus nigra. A00233 protein 1-97 the amidation states of residues 57, 58, 60, 61, 68, and 88 were identified by homology with other ferredoxin sequences ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-97 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 97 complete tentative ASYKVKLITPDGPQEFECPDDVYILEHAEELGIDIPYSCRAGSCSSCAGKLVAGSVDQSD QSFLDDEQIEEGWVLTCVAYPKSDVT(I.E.T.H)KEEELTA
FETA A00229 24-Apr-1984 30-Sep-1988 31-Mar-2000
ferredoxin [2Fe-2S] taro taro Colocasia esculenta Rao, K.K. Matsubara, H. Biochem. Biophys. Res. Commun. 381970500-506 The amino acid sequence of taro ferredoxin. MUID70181822 A00229 protein 1-97 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-97 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 97 complete tentative ATYKVKLVTPSGQQEFQCPDDVYILDQAEEVGIDLPYSCRAGSCSSCAGKVK.VGD.VDQ SDGSF.LDDEQ.IGEGWVLTCVAYPVSDGTIETHKEEELTA
FERP A00234 28-Feb-1980 28-Feb-1980 13-Nov-1998
ferredoxin [2Fe-2S] rape rape Brassica napus Takruri, I. Boulter, D. Biochem. J. 1851980239-243 The amino acid sequence of ferredoxin from Brassica napus (rape). MUID80197725 A00234 protein 1-96 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-96 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 96 complete ATYKVKFITPEGEQEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGFVDQSD ESFLDDDQIAEGFVLTCAAYPTSDVTIETHKEEELV
FEAA A00227 07-May-1981 07-May-1981 13-Nov-1998
ferredoxin [2Fe-2S] alfalfa alfalfa Medicago sativa Keresztes-Nagy, S. Perini, F. Margoliash, E. J. Biol. Chem. 2441969981-995 Primary structure of alfalfa ferredoxin. MUID69184143 A00227 protein 1-97 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-97 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 97 complete ASYKVKLVTPEGTQEFECPDDVYILDHAEEEGIVLPYSCRAGSCSSCAGKVAAGEVNQSD GSFLDDDQIEEGWVLTCVAYAKSDVTIETHKEEELTA
FEBQ A00230 03-Aug-1984 03-Aug-1984 13-Nov-1998
ferredoxin [2Fe-2S] great burdock great burdock Arctium lappa Takruri, I.A.H. Gilroy, J. Boulter, D. Phytochemistry 211982325-327 Amino acid sequence of ferredoxin from Arctium lappa. A00230 protein 1-97 63-Phe was also found ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-97 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 97 complete ATYKVTLITPEGKQEFEVPDDVYILDHAAEEVGDLPYSCRAGSCSSCAGKVTAGSVDQSD GSYLDDDQMEAGWVLTCVAYPTSDVTIETHKEEELTA
FEQH A23011 30-Sep-1991 30-Sep-1991 11-Jun-1999
ferredoxin [2Fe-2S] precursor white campion white campion, evening lychnis Silene pratensis, Lychnis alba Smeekens, S. van Binsbergen, J. Weisbeek, P. Nucleic Acids Res. 1319853179-3194 The plant ferredoxin precursor: nucleotide sequence of a full length cDNA clone. MUID85215678 A23011 mRNA 1-146 GBX02432 NIDg21361 PIDNCAA26281.1 PIDg21362 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S chloroplast electron transfer iron-sulfur protein metalloprotein domain transit peptide (chloroplast) 1-48 predicted product ferredoxin [2Fe-2S] 49-146 predicted domain ferredoxin [2Fe-2S] homology 73-127 binding-site 2Fe-2S cluster (Cys) (covalent) 88,93,96,126 predicted 146 complete MASTLSTLSVSASLLPKQQPMVASSLPTNMGQALFGLKAGSRGRVTAMATYKVTLITKES GTVTFDCPDDVYVLDQAEEEGIDLPYSCRAGSCSSCAGKVVAGSVDQSDQSFLDDDQIEA GWVLTCAAYPSADVTIETHKEEELTA
FEWT S52993 A00235 S37226 30-Jun-1979 19-May-1995 07-Dec-1999
ferredoxin [2Fe-2S] precursor wheat common wheat Triticum aestivum Bringloe, D.H. Dyer, T.A. Gray, J.C. Plant Mol. Biol. 271995293-306 Developmental, circadian and light regulation of wheat ferredoxin gene expression. MUID95195157 S52993 DNA 1-143 EMBLX75089 NIDg403032 PIDNCAA52980.1 PIDg403033 leaf submitted to the EMBL Data Library, August 1993 Takruri, I. Boulter, D. Biochem. J. 1791979373-378 The amino acid sequence of ferredoxin from Triticum aestivum (wheat). MUID80020138 A00235 protein 47-143 petF multifunctional electron carrier ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein domain transit peptide (chloroplast) 1-46 predicted product ferredoxin [2Fe-2S] 47-143 experimental domain ferredoxin [2Fe-2S] homology 70-124 binding-site 2Fe-2S cluster (Cys) (covalent) 85,90,93,123 predicted 143 complete MAAALSLRAPFSLRAVAPPAPRVALAPAALSLAAAKQVRGARLRAQATYKVKLVTPEGEV ELEVPDDVYILDQAEEEGIDLPYSCRAGSCSSCAGKLVSGEIDQSDQSFLDDDQMEAGWV LTCHAYPKSDIVIETHKEEELTA
FERZ T03738 S03730 JT0223 31-Mar-1989 28-May-1999 16-Jun-2000
ferredoxin [2Fe-2S] I precursor rice rice Oryza sativa Ohmori, K. Doyama, N. Ida, S. Plant Physiol. 1111996348 Molecular cloning of a rice leaf ferredoxin cDNA. T03738 preliminary translated from GB/EMBL/DDBJ mRNA 1-139 EMBLD30763 PIDNBAA06436.1 subsp. Japonica, cv. Kinmaze Kamo, M. Kotani, N. Tsugita, A. He, Y.K. Nozu, Y. Protein Seq. Data Anal. 21989289-293 Amino acid sequences of ferredoxins from rice cultivars, japonica and indica. MUID89367259 S03730 protein 44-139 sequences from cultivars japonica and indica are identical ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 44-139 experimental domain ferredoxin [2Fe-2S] homology 67-121 binding-site 2Fe-2S cluster (Cys) (covalent) 82,87,90,120 predicted 139 complete MAATALSSQVRLPMSLRVATAPAPARVSVLPASNKLGDRLRMQATYNVKLITPDGEVELQ VPDDVYILDQAEEEGIDLPYSCRAGSCSSCAGKVVSGEIDQSDQSFLDDDQVAAGWVLTC HAYPKSDVVIETHKEDDLI
FEFW1 A00236 30-Jun-1979 23-Oct-1981 13-Nov-1998
ferredoxin [2Fe-2S] I Virginian pokeweed Virginian pokeweed Phytolacca americana Wakabayashi, S. Hase, T. Wada, K. Matsubara, H. Suzuki, K. Takaichi, S. J. Biochem. 8319781305-1319 Amino acid sequences of two ferredoxins from pokeweed, Phytolacca americana. MUID78194079 A00236 protein 1-96 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-96 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 96 complete ATYKVTLVTPSGTQTIDCPDDTYVLDAAEEAGLDLPYSCRAGSCSSCTGKVTAGTVDQED QSFLDDDQIEAGFVLTCVAFPKGDVTIETHKEEDIV
FEFWF B00238 A00236 31-Dec-1990 31-Dec-1990 13-Nov-1998
ferredoxin [2Fe-2S] I food pokeweed food pokeweed Phytolacca esculenta Wakabayashi, S. Hase, T. Wada, K. Matsubara, H. Suzuki, K. J. Biochem. 871980227-236 Amino acid sequences of two ferredoxins from Phytolacca esculenta. Gene duplication and speciation. MUID80137361 B00238 protein 1-96 48-Ala and 96-Ala were also found ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-96 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 96 complete ATYKVTLVTPSGTQTIDCPDDTYVLDAAEEAGLDLPYSCRAGSCSSCTGKVTAGTVDQED QSFLDDDQIEAGFVLTCVAYPKGDVTIETHKEEDIV
FEFW2 A00237 30-Jun-1979 30-Jun-1979 13-Nov-1998
ferredoxin [2Fe-2S] II Virginian pokeweed Virginian pokeweed Phytolacca americana Wakabayashi, S. Hase, T. Wada, K. Matsubara, H. Suzuki, K. Takaichi, S. J. Biochem. 8319781305-1319 Amino acid sequences of two ferredoxins from pokeweed, Phytolacca americana. MUID78194079 A00237 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-98 experimental domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 predicted 98 complete AASYKVTFVTPSGTNTITCPADTYVLDAAEESGLDLPYSCRAGACSSCAGKVTAGAVNQE DGSFLEEEQMEAGWVLTCVAYPTSDVTIETHKEEDLTA
FEFW2E A00238 31-Aug-1980 31-Aug-1980 13-Nov-1998
ferredoxin [2Fe-2S] II food pokeweed food pokeweed Phytolacca esculenta Wakabayashi, S. Hase, T. Wada, K. Matsubara, H. Suzuki, K. J. Biochem. 871980227-236 Amino acid sequences of two ferredoxins from Phytolacca esculenta. Gene duplication and speciation. MUID80137361 A00238 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-98 experimental domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 predicted 98 complete AASYKVTFVTPSGTKTITCPADTYVLDAAEDTGLDLPYSCRAGACSSCAGKVTAGSVNQE DGSFLDEEQMEAGWVLTCVAYPTSDVTIETHKEEDLSA
FEFNG A00239 06-Jul-1982 30-Sep-1988 31-Mar-2000
ferredoxin [2Fe-2S] fern (Gleichenia japonica) urajiro Gleichenia japonica Hase, T. Yamanashi, H. Matsubara, H. J. Biochem. 911982341-346 Purification and amino acid sequence of a fern (Gleichenia japonica) ferredoxin. MUID82167301 A00239 protein 1-95 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-95 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 95 complete tentative AIFKVKFLTPDGERTIEVPDDK.FILDAGEEAGLDLPYSCR.AGACSSCTGK.LLDGR.V DQSEQSFLDDDQMAEGFVLTCVAYPAGDITIETHAEEKL
FEEQ1 A00240 30-Jun-1979 08-Oct-1981 13-Nov-1998
ferredoxin [2Fe-2S] I horsetail (Equisetum telmateia) Equisetum telmateia Hase, T. Wada, K. Matsubara, H. J. Biochem. 821977267-276 Horsetail (Equisetum telmateia) ferredoxins I and II. MUID77249491 A00240 protein 1-95 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-95 experimental domain ferredoxin [2Fe-2S] homology 23-77 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,76 predicted 95 complete AYKTVLKTPSGEFTLDVPEGTTILDAAEEAGYDLPFSCRAGACSSCLGKVVSGSVDQSEG SFLDDGQMEEGFVLTCIAIPESDLVIETHKEEELF
FEEQ1F A04609 A00240 31-Dec-1990 31-Dec-1990 15-Sep-2000
ferredoxin [2Fe-2S] I [validated] field horsetail field horsetail Equisetum arvense Hase, T. Wada, K. Matsubara, H. J. Biochem. 821977277-286 Horsetail (Equisetum arvense) ferredoxins I and II. MUID77249492 A04609 protein 1-95 Tsukihara, T. submitted to the Brookhaven Protein Data Bank September1993 PDB1FRR annotation X-ray crystallography, 1.8 angstroms, residues 1-95 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-95 experimental domain ferredoxin [2Fe-2S] homology 23-77 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,76 experimental 95 complete AYKTVLKTPSGEFTLDVPEGTTILDAAEEAGYDLPFSCRAGACSSCLGKVVSGSVDESEG SFLDDGQMEEGFVLTCIAIPESDLVIETHKEEELF
FEEQ2 A00241 30-Jun-1979 08-Oct-1981 13-Nov-1998
ferredoxin [2Fe-2S] II horsetail (Equisetum telmateia) Equisetum telmateia Hase, T. Wada, K. Matsubara, H. J. Biochem. 821977267-276 Horsetail (Equisetum telmateia) ferredoxins I and II. MUID77249491 A00241 protein 1-93 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-93 experimental domain ferredoxin [2Fe-2S] homology 23-76 binding-site 2Fe-2S cluster (Cys) (covalent) 37,42,45,75 predicted 93 complete AYKVTLKTPDGDITFDVEPGERLIDIASEKADLPLSCQAGACSTCLGKIVSGTVDQSEGS FLDDEQIEQGYVLTCIAIPESDVVIETHKEDEL
FEEQ2F B04609 A00241 31-Dec-1990 31-Dec-1990 13-Nov-1998
ferredoxin [2Fe-2S] II field horsetail field horsetail Equisetum arvense Hase, T. Wada, K. Matsubara, H. J. Biochem. 821977277-286 Horsetail (Equisetum arvense) ferredoxins I and II. MUID77249492 B04609 protein 1-93 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-93 experimental domain ferredoxin [2Fe-2S] homology 23-76 binding-site 2Fe-2S cluster (Cys) (covalent) 37,42,45,75 predicted 93 complete AYKVTLKTPDGDITFDVEPGERLIDIGSEKADLPLSCQAGACSTCLGKIVSGTVDQSEGS FLDDEQIEQGYVLTCIAIPESDVVIETHKEDEL
FEPRR A93760 A93759 JT0018 30-Sep-1988 30-Sep-1988 13-Nov-1998
ferredoxin [2Fe-2S] red alga (Palmaria palmata) dulse Palmaria palmata Inoue, K. Hase, T. Matsubara, H. Fitzgerald, M.P. Rogers, L.J. Phytochemistry 231984773-776 Amino acid sequence of a ferredoxin from Rhodymenia palmata, a red alga in the Florideophyceae. A93760 protein 1-97 Andrew, P.W. Rogers, L.J. Haslett, B.G. Boulter, D. Phytochemistry 201981579-583 Partial structure and properties of the ferredoxin from Rhodymenia palmata. A93759 protein 1-48 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-97 experimental domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 predicted 97 complete AVKYTVTLSTPGGVEEIEGDETTYVLDSAEDQGIDLPYSCRAGACSTCAGIVELGTVDQS DQSFLDDDQLNDSFVLTCVAYPTSDCQIKTHQEEKLY
FEKM T08054 S00361 S29222 30-Sep-1990 28-May-1999 11-Jun-1999
ferredoxin [2Fe-2S] precursor, chloroplast Chlamydomonas reinhardtii Chlamydomonas reinhardtii Stein, M. submitted to the EMBL Data Library June1995 T08054 translated from GB/EMBL/DDBJ DNA 1-126 EMBLU29516 NIDg1009713 PIDNAAC49171.1 PIDg1009714 strain CW15 Schmitter, J.M. Jacquot, J.P. de Lamotte-Guery, F. Beauvallet, C. Dutka, S. Gadal, P. Decottignies, P. Eur. J. Biochem. 1721988405-412 Purification, properties and complete amino acid sequence of the ferredoxin from a green alga, Chlamydomonas reinhardtii. MUID88166713 S00361 protein 33-126 Rogers, W.J. Hodges, M. Decottignies, P. Schmitter, J.M. Gadal, P. Jacquot, J.P. FEBS Lett. 3101992240-245 Isolation of a cDNA fragment coding for Chlamydomonas reinhardtii ferredoxin and expression of the recombinant protein in Escherichia coli. MUID93011926 S29222 mRNA 37-38,'S',40-100,'K',102-121 the sequence presented Fig. 1 is not found in GenBank entry CRTRX, release 111.0 although the reference is cited there 59/3 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S chloroplast electron transfer iron-sulfur protein metalloprotein domain transit peptide (chloroplast) 1-32 predicted product ferredoxin [2Fe-2S] 33-126 experimental domain ferredoxin [2Fe-2S] homology 54-108 binding-site 2Fe-2S cluster (Cys) (covalent) 69,74,77,107 experimental 126 complete MAMAMRSTFAARVGAKPAVRGARPASRMSCMAYKVTLKTPSGDKTIECPADTYILDAAEE AGLDLPYSCRAGACSSCAGKVAAGTVDQSDQSFLDDAQMGNGFVLTCVAYPTSDCTIQTH QEEALY
FESC A00242 07-May-1981 07-May-1981 13-Nov-1998
ferredoxin [2Fe-2S] green alga (Scenedesmus quadricauda) Scenedesmus quadricauda Sugeno, K. Matsubara, H. J. Biol. Chem. 24419692979-2989 The amino acid sequence of Scenedesmus ferredoxin. MUID69193756 A00242 protein 1-96 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-96 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 96 complete ATYKVTLKTPSGDQTIECPDDTYILDAAEEAGLDLPYSCRAGACSSCAGKVEAGTVDQSD QSFLDDSQMDGGFVLTCVAYPTSDCTIATHKEEDLF
FEDH1 A00243 30-Apr-1980 30-Apr-1980 31-Mar-2000
ferredoxin [2Fe-2S] I green alga (Dunaliella salina) Dunaliella salina Hase, T. Matsubara, H. Ben-Amotz, A. Rao, K.K. Hall, D.O. Phytochemistry 1919802065-2070 Purification and sequence determination of two ferredoxins from Dunaliella salina. A00243 protein 1-95 3-Gln, 32-Leu, and 50-Leu were also found ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-95 experimental domain ferredoxin [2Fe-2S] homology 23-77 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,76 predicted 95 complete tentative (S)YMVTLKTPSGEQKVEVSPDSYILDAAEEAGVDLPYSCRAGSCSSCAGKVESGTVDQS DQSFLDDDQMD(S,G,F)VLTCVAYATSDCTIVTHQEENLY
FEDH2 A00244 30-Apr-1980 30-Apr-1980 31-Mar-2000
ferredoxin [2Fe-2S] II green alga (Dunaliella salina) Dunaliella salina Hase, T. Matsubara, H. Ben-Amotz, A. Rao, K.K. Hall, D.O. Phytochemistry 1919802065-2070 Purification and sequence determination of two ferredoxins from Dunaliella salina. A00244 protein 1-95 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-95 experimental domain ferredoxin [2Fe-2S] homology 23-77 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,76 predicted 95 complete tentative (A)YKVTLKTPSGDQTIEVSPDAYILDAAEEAGLDLPYSCRAGACSSCAGKVEAGTIDQS DQSFLDDDQQGRGFVLTCVAYATSDCTISTHQEESLY
FEKK A00245 31-May-1979 23-Oct-1981 13-Nov-1998
ferredoxin [2Fe-2S] red alga (Cyanidium caldarium) Cyanidium caldarium Hase, T. Wakabayashi, S. Wada, K. Matsubara, H. Juttner, F. Rao, K.K. Fry, I. Hall, D.O. FEBS Lett. 96197841-44 Cyanidium caldarium ferredoxin: a red algal type? A00245 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ASYKIHLVNKDQGIDETIECPDDQYILDAAEEQGLDLPYSCRAGACSTCAGKLLEGEVDQ SDQSFLDDDQVKAGFVLTCVAYPTSNATILTHQEESLY
FEKT1 S11048 JU0459 T06893 S10427 31-Mar-1991 31-Mar-1991 21-Jan-2000
ferredoxin [2Fe-2S] I Cyanophora paradoxa cyanelle cyanelle Cyanophora paradoxa Neumann-Spallart, C. Brandtner, M. Kraus, M. Jakowitsch, J. Bayer, M.G. Maier, T.L. Schenk, H.E.A. Loeffelhardt, W. FEBS Lett. 268199055-58 The petFI gene encoding ferredoxin I is located close to the str operon on the cyanelle genome of Cyanophora paradoxa. MUID90346172 S11048 DNA 1-99 EMBLX52143 NIDg11389 PIDNCAA36387.1 PIDg11390 strain LB 555UTEX Bryant, D.A. Schluchter, W.M. Stirewalt, V.L. Gene 981991169-175 Ferredoxin and ribosomal protein S10 are encoded on the cyanelle genome of Cyanophora paradoxa. MUID91200662 JU0459 DNA 1-99 GBM35206 NIDg336630 PIDNAAA31699.1 PIDg336631 Stirewalt, V.L. Michalowski, C.B. Luffelhardt, W. Bohnert, H.J. Bryant, D.A. submitted to the EMBL Data Library July1995 Nucleotide sequence of the cyanelle genome from Cyanophora paradoxa. T06893 preliminary translated from GB/EMBL/DDBJ DNA 1-99 EMBLU30821 NIDg1016083 PIDNAAA81236.1 PIDg1016149 strain Pringsheim LB555 petFI petF cyanelle ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S cyanelle electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 2-99 predicted domain ferredoxin [2Fe-2S] homology 27-81 binding-site 2Fe-2S cluster (Cys) (covalent) 42,47,50,80 predicted 99 complete MAVYKVRLICEEQGLDTTIECPDDEYILDAAEEQGIDLPYSCRAGACSTCAGKVVEGTVD QSDQSFLDDAQLAAGYVLTCVAYPSSDCTVKTHQEESLY
FEPRU A00246 31-May-1979 23-Oct-1981 13-Nov-1998
ferredoxin [2Fe-2S] red alga (Porphyra umbilicalis) laver Porphyra umbilicalis Takruri, I. Haslett, B.G. Boulter, D. Andrew, P.W. Rogers, L.J. Biochem. J. 1731978459-466 The amino acid sequence of ferredoxin from the red alga Porphyra umbilicalis. MUID79020768 A00246 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ADYKIHLVSKEEGIDVTFDCSEDTYILDAAEEEGIELPYSCRAGACSTCAGKVTEGTVDQ SDQSFLDDEQMLKGYVLTCIAYPESDCTILTHVEQELY
FEYB6 S76345 A56811 A00247 13-Jun-1983 13-Nov-1998 15-Sep-2000
ferredoxin [2Fe-2S] [validated] Synechocystis sp. Synechocystis sp. Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S76345 DNA 1-97 EMBLD64000 GBAB001339 NIDg1001484 PIDNBAA10197.1 PIDg1001570 strain PCC 6803 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 Bottin, H. Lagoutte, B. Biochim. Biophys. Acta 1101199248-56 Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC 6803. MUID92338182 A56811 protein 2-97 strain PCC 6714 sequence extracted from NCBI backbone (NCBIP:109680) Hase, T. Inoue, K. Matsubara, H. Williams, M.M. Rogers, L.J. J. Biochem. 9219821357-1362 Amino acid sequence of Synechocystis 6714 ferredoxin: a unique structural feature of unicellular blue-green algal ferredoxin. MUID83108768 A00247 protein 2-14,'N',16-97 strain PCC 6714 Lelong, C. Setif, P. Bottin, H. Andre, F. Neumann, J.M. submitted to the Brookhaven Protein Data Bank September1995 PDB1DOX annotation conformation and disulfide bond assignments by (1)H- and (15)N-NMR, without disulfide bond, residues 2-97 Lelong, C. Setif, P. Bottin, H. Andre, F. Neumann, J.M. submitted to the Brookhaven Protein Data Bank September1995 PDB1DOY annotation conformation and disulfide bond assignments by (1)H- and (15)N-NMR, with disulfide bond, residues 2-97 Lelong, C. Setif, P. Bottin, H. Andre, F. Neumann, J.M. Biochemistry 34199514462-14473 (1)H and (15)N NMR sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803. MUID96062510 annotation conformation and disulfide bond assignments by (1)H-NMR ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2s] 2-97 experimental domain ferredoxin [2Fe-2S] homology 25-79 disulfide-bonds 19-86 predicted binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 experimental 97 complete MASYTVKLITPDGESSIECSDDTYILDAAEEAGLDLPYSCRAGACSTCAGKITAGSVDQS DQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEDLY
FEFZ1 A00248 25-Feb-1985 25-Feb-1985 13-Nov-1998
ferredoxin [2Fe-2S] I Aphanizomenon flos-aquae Aphanizomenon flos-aquae Lee, I.S. Hase, T. Matsubara, H. Ho, K.K. Krogmann, D.W. Biochim. Biophys. Acta 744198353-56 Amino acid sequence of ferredoxin from Aphanizomenon flos-aquae. A00248 protein 1-97 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-97 experimental domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 predicted 97 complete ATYKVTLIDAEGTTTTIDCPDDTYILDAAEEAGLDLPYSCRAGACSTCAGKLVTGTIDQS DQSFLDDDQVEAGYVLTCVAYPTSDVTIETHKEEDLY
FESG A00249 07-May-1981 07-May-1981 13-Nov-1998
ferredoxin [2Fe-2S] Spirulina maxima Spirulina maxima Tanaka, M. Haniu, M. Yasunobu, K.T. Rao, K.K. Hall, D.O. Biochemistry 1419755535-5540 Modification of the automated sequence determination as applied to the sequence determination of the Spirulina maxima ferredoxin. MUID76062440 A00249 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ATYKVTLISEAEGINETIDCDDDTYILDAAEEAGLDLPYSCRAGACSTCAGKITSGSIDQ SDQSFLDDDQIEAGYVLTCVAYPTSDCTIQTHQEEGLY
FESGAL A00250 07-May-1981 07-May-1981 15-Sep-2000
ferredoxin [2Fe-2S] [validated] Spirulina platensis Spirulina platensis Tanaka, M. Haniu, M. Yasunobu, K.T. Rao, K.K. Hall, D.O. Biochem. Biophys. Res. Commun. 691976759-765 The complete amino acid sequence of the Spirulina platensis ferredoxin. MUID76184180 A00250 protein 1-98 Fukuyama, K. Tsukihara, T. submitted to the Brookhaven Protein Data Bank April1995 PDB4FXC annotation X-ray crystallography, 2.5 angstroms, residues 1-98 Kakudo, M. Tsukihara, T. Katsube, Y. submitted to the Brookhaven Protein Data Bank December1981 PDB3FXC annotation X-ray crystallography, 2.5 angstroms, residues 1-98 Tsukihara, T. Fukuyama, K. Nakamura, M. Katsube, Y. Tanaka, N. Kakudo, M. Wada, K. Hase, T. Matsubara, H. J. Biochem. 9019811763-1773 X-Ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 angstroms resolution. MUID82142259 annotation X-ray crystallography, 2.5 angstroms ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 experimental 98 complete ATYKVTLINEAEGINETIDCDDDTYILDAAEEAGLDLPYSCRAGACSTCAGTITSGTIDQ SDQSFLDDDQIEAGYVLTCVAYPTSDCTIKTHQEEGLY
FEEF A00251 18-Dec-1981 18-Dec-1981 13-Nov-1998
ferredoxin [2Fe-2S] Chlorogloeopsis fritschii Chlorogloeopsis fritschii Takahashi, Y. Hase, T. Matsubara, H. Hutber, G.N. Rogers, L.J. J. Biochem. 9219821363-1368 Amino acid sequence of Chlorogloeopsis fritschii ferredoxin: taxonomic and evolutionary aspects. MUID83108769 A00251 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ATYKVTLINDAEGLNQTIEVDDDTYILDAAEEAGLDLPYSCRAGACSTCAGKIKSGTVDQ SDQSFLDDDQIEAGYVLTCVAYPTSDCTIETHKEEELY
FEMW A00252 31-May-1979 31-May-1979 13-Nov-1998
ferredoxin [2Fe-2S] Fischerella sp. Fischerella sp. Hase, T. Wakabayashi, S. Matsubara, H. Rao, K.K. Hall, D.O. Widmer, H. Gysi, J. Zuber, H. submitted to the Atlas September1978 A00252 protein 1-98 the source was designated as Mastigocladus laminosus ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ATYKVTLINEAEGLNKTIEVPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKLISGTVDQ SDQSFLDDDQIEAGYVLTCVAYPTSDCVIETHKEEELY
FENM2M A00253 13-Jun-1983 13-Jun-1983 13-Nov-1998
ferredoxin [2Fe-2S] II Nostoc muscorum Nostoc muscorum Hase, T. Matsubara, H. Hutber, G.N. Rogers, L.J. J. Biochem. 9219821347-1355 Amino acid sequences of Nostoc strain MAC ferredoxins I and II. MUID83108767 A00253 protein 1-98 strain mac ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ATYKVRLFNAAEGLDETIEVPDDEYILDAAEEAGLDLPFSCRSGSCSSCNGILKKGTVDQ SDQNFLDDDQIAAGNVLTCVAYPTSNCEIETHREDAIA
FEAH A00254 07-May-1981 07-May-1981 15-Sep-2000
ferredoxin [2Fe-2S] I [validated] Aphanothece sacrum Aphanothece sacrum Hase, T. Wada, K. Matsubara, H. J. Biochem. 791976329-343 Amino acid sequence of the major component of Aphanothece sacrum ferredoxin. MUID76190060 A00254 protein 1-96 Tsukihara, T. submitted to the Brookhaven Protein Data Bank August1990 PDB1FXI annotation X-ray crystallography, 2.2 angstroms, residues 1-96 Tsukihara, T. Fukuyama, K. Mizushima, M. Harioka, T. Kusunoki, M. Katsube, Y. Hase, T. Matsubara, H. J. Mol. Biol. 2161990399-410 Structure of the [2Fe-2S] ferredoxin I from the blue-green alga Aphanothece sacrum at 2.2 angstroms resolution. MUID91073403 annotation X-ray crystallography, 2.2 angstroms ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-96 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 experimental 96 complete ASYKVTLKTPDGDNVITVPDDEYILDVAEEEGLDLPYSCRAGACSTCAGKLVSGPAPDED QSFLDDDQIQAGYILTCVAYPTGDCVIETHKEEALY
FEAH2 A00255 31-May-1979 08-Oct-1981 13-Nov-1998
ferredoxin [2Fe-2S] II Aphanothece sacrum Aphanothece sacrum Hase, T. Wakabayashi, S. Wada, K. Matsubara, H. J. Biochem. 831978761-770 Amino acid sequence of Aphanothece sacrum ferredoxin II (minor component). MUID78150873 A00255 protein 1-99 there is no clear evidence of functional difference between this ferredoxin and ferredoxin I (major component) from this organism the different amino acid compositions suggest they are genetically independent isoenzymes ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] II 1-99 experimental domain ferredoxin [2Fe-2S] homology 26-81 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,80 predicted 99 complete ATYKVTLINEEEGINAILEVADDQTILDAGEEAGLDLPSSCRAGSCSTCAGKLVSGAAPN QDDQAFLDDDQLAAGWVMTCVAYPTGDCTIMTHQESEVL
FENM1M A00256 13-Jun-1983 13-Jun-1983 13-Nov-1998
ferredoxin [2Fe-2S] I Nostoc muscorum Nostoc muscorum Hase, T. Matsubara, H. Hutber, G.N. Rogers, L.J. J. Biochem. 9219821347-1355 Amino acid sequences of Nostoc strain MAC ferredoxins I and II. MUID83108767 A00256 protein 1-98 strain MAC ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ATVYKVTLVDQEGTETTIDVPDDEYILDIAEDQGLDLPYSCRAGACSTCAGKIVSGTVDQ SDQSFLDDDQIEKGYVLTCVAYPTSDLKIETHKEEDLY
FENM A00257 24-Apr-1984 03-Aug-1984 13-Nov-1998
ferredoxin [2Fe-2S] Nostoc muscorum Nostoc muscorum Hase, T. Wada, K. Ohmiya, M. Matsubara, H. J. Biochem. 801976993-999 Amino acid sequence of the major component of Nostoc muscorum ferredoxin. MUID77071433 A00257 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ATFKVTLINEAEGTKHEIEVPDDEYILDAAEEEGYDLPFSCRAGACSTCAGKLVSGTVDQ SDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY
S25233 S25233 28-May-1993 28-May-1993 15-Sep-2000
ferredoxin [2Fe-2S] I [validated] Anabaena sp. (strain PCC 7120) Anabaena sp. Alam, J. Whitaker, R.A. Krogmann, D.W. Curtis, S.E. J. Bacteriol. 16819861265-1271 Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120. MUID87057031 S25233 DNA 1-99 EMBLM14737 NIDg142075 PIDNAAA22021.1 PIDg142076 Rypniewski, W.R. Breiter, D.R. Benning, M.M. Wesenberg, G. Oh, B.H. Markley, J.L. Rayment, I. Holden, H.M. submitted to the Brookhaven Protein Data Bank January1991 PDB1FXA annotation X-ray crystallography, 2.5 angstroms, residues 2-97 Rypniewski, W.R. Breiter, D.R. Benning, M.M. Wesenberg, G. Oh, B.H. Markley, J.L. Rayment, I. Holden, H.M. Biochemistry 3019914126-4131 Crystallization and structure determination to 2.5-Angstroms resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. MUID91214942 annotation X-ray crystallography, 2.5 angstroms petF ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] I 2-99 experimental domain ferredoxin [2Fe-2S] homology 27-81 binding-site 2Fe-2S cluster (Cys) (covalent) 42,47,50,80 experimental 99 complete MATFKVTLINEAEGTKHEIEVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVD QSDQSFLDDDQIEAGYVLTCVAYPTSDVVIQTHKEEDLY
FEAI A25761 S08121 A04618 A00257 31-Dec-1990 06-Feb-1995 11-Jun-1999
ferredoxin [2Fe-2S] ferredoxin II Anabaena variabilis Anabaena variabilis van der Plas, J. de Groot, R.P. Weisbeek, P.J. van Arkel, G.A. Nucleic Acids Res. 1419867803 Coding sequence of a ferredoxin gene from Anabaena variabilis ATCC 29413. MUID87040742 A25761 DNA 1-99 GBX06210 NIDg39246 PIDNCAA29563.1 PIDg39247 van der Plas, J. de Groot, R. Woortman, M. Cremers, F. Borrias, M. van Arkel, G. Weisbeek, P. Photosyn. Res. 181988179-204 Genes encoding ferredoxins from Anabaena sp. PCC 7937 and Synechococcus sp. PCC 7942: structure and regulation. S08121 DNA 1-99 EMBLX14343 NIDg38884 PIDNCAA32528.1 PIDg38885 Chan, T.M. Hermodson, M.A. Ulrich, E.L. Markley, J.L. Biochemistry 2219835988-5995 Nuclear magnetic resonance studies of two-iron-two-sulfur ferredoxins. 2. Determination of the sequence of Anabaena variabilis ferredoxin II, assignment of aromatic resonances in proton spectra, and effects of chemical modification. A04618 protein 2-15,'KHE',19,'E',21-33,'E',35-87,'CV',90-99 the supposed modification of 16-Lys and its effect on the NMR shifts for 17-His are reported petF1 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 2-99 experimental domain ferredoxin [2Fe-2S] homology 27-81 binding-site 2Fe-2S cluster (Cys) (covalent) 42,47,50,80 predicted 99 complete MATFKVTLINEAEGTSNTIDVPDDEYILDAAEEQGYDLPFSCRAGACSTCAGKLVSGTVD QSDQSFLDDDQIEAGYVLTCVAYPTSDVTIQTHKEEDLY
FEYCAL A00258 31-Jan-1980 24-Sep-1981 13-Nov-1998
ferredoxin [2Fe-2S] Synechococcus lividus Synechococcus lividus Borden, D. Margoliash, E. submitted to the Atlas December1979 A00258 protein 1-96 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-96 experimental domain ferredoxin [2Fe-2S] homology 24-78 binding-site 2Fe-2S cluster (Cys) (covalent) 39,44,47,77 predicted 96 complete ATYKVTLVRPDGETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSD QSFLDDDQIEKGFVLTCVAYPRSDCKILTHQEEELY
FEYCT A00259 25-Feb-1985 03-Nov-2000 03-Nov-2000
ferredoxin [2Fe-2S] [validated] Synechococcus sp. Synechococcus sp. Hase, T. Matsubara, H. Koike, H. Katoh, S. Biochim. Biophys. Acta 744198346-52 Amino acid sequence of ferredoxin from a thermophilic blue-green alga, Synechococcus sp. A00259 protein 1-97 Hatanaka, H. Tanimura, R. Katoh, S. Inagaki, F. submitted to the Brookhaven Protein Data Bank February1997 PDB2CJN annotation conformation (1)H-NMR, residues 1-97 the source is designated as Synechococcus elongatus Roesch, P. Baumann, B. Sticht, H. Sutter, M. Haehnel, W. submitted to the Brookhaven Protein Data Bank November1995 PDB1ROE annotation conformation (1)H-NMR, residues 1-97 the source is designated as Synechococcus elongatus ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-97 experimental domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 experimental 97 complete ATYKVTLVRPDGSETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQS DQSFLDDDQIEKGFVLTCVAYPRSDCKILTNQEEELY
FEYO S07452 30-Sep-1991 30-Sep-1991 13-Nov-1998
ferredoxin [2Fe-2S] green alga (Bryopsis maxima) Bryopsis maxima Minami, Y. Sugimura, Y. Wakabayashi, S. Wada, K. Takahashi, Y. Matsubara, H. Physiol. Veg. 231985669-678 Isolation, properties, and amino acid sequence of a ferredoxin from a multinuclear, unicellular green alga, Bryopsis marina. S07452 protein 1-98 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 predicted 98 complete ASYKVTLKLDDGSEAVIDCDEDSFILDVAEEEGIDIPFSCRSGSCSTCAGKIEGGTVDQS EQTFLDDDQMEEGYVLTCVAYPTSDCTILTHQEEEMIG
FEBF2 A28857 30-Sep-1991 30-Sep-1991 13-Nov-1998
ferredoxin [2Fe-2S] yellow-green alga (Bumilleriopsis filiformis) Bumilleriopsis filiformis Inoue, K. Hase, T. Boeger, P. Matsubara, H. J. Biochem. 9419831451-1455 Amino acid sequence of a ferredoxin from Bumilleriopsis filiformis, a yellow-green alga: relationship with red algae, protoflorideophyceae, and filamentous blue-green algae. MUID84087800 A28857 protein 1-98 1-Ala was also found ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-98 experimental domain ferredoxin [2Fe-2S] homology 26-80 binding-site 2Fe-2S cluster (Cys) (covalent) 41,46,49,79 predicted 98 complete ETYSVTLVNEEKNINAVIKCPDDQFILDAAEEQGIELPYSCRAGACSTCAGKVLSGTIDQ SEQSFLDDDQMGAGFLLTCVAYPTSDCKVQTHAEDDLY
FEDQ A30036 30-Sep-1991 30-Sep-1991 13-Nov-1998
ferredoxin [2Fe-2S] dinoflagellate (Peridinium bipes) Peridinium bipes Uchida, A. Ebata, S. Wada, K. Matsubara, H. Ishida, Y. J. Biochem. 1041988700-705 Complete amino acid sequence of ferredoxin from Peridinium bipes (Dinophyceae). MUID89174497 A30036 protein 1-93 Peridinium is a dinoflagellate, a unicellular alga. ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-93 experimental domain ferredoxin [2Fe-2S] homology 22-76 binding-site 2Fe-2S cluster (Cys) (covalent) 37,42,45,75 predicted 93 complete FKVTLDTPDGKKSFECPGDSYILDKAEEEGLELPYSCRAGSCSSCAGKVLTGSIDQSDQA FLDDDQGGDGYCLTCVTYPTSDVTIKTHCESEL
FELV A24126 30-Sep-1991 30-Sep-1991 13-Nov-1998
ferredoxin [2Fe-2S] liverwort (Marchantia polymorpha) Marchantia polymorpha Minami, Y. Wakabayashi, S. Imoto, S. Ohta, Y. Matsubara, H. J. Biochem. 981985649-655 Ferredoxin from a liverwort, Marchantia polymorpha. Purification and amino acid sequence. MUID86111669 A24126 protein 1-95 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 1-95 experimental domain ferredoxin [2Fe-2S] homology 23-77 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,76 predicted 95 complete TFKVTLNTPTGQSVIDVEDDEYILDAAEEAGLSLPYSCRAGACSSCAGKVTAGEVDQSDE SFLDDDQMDEGYVLTCIAYPTSDLTIDTHQEEALI
FEYC2 S10833 S00605 30-Jun-1990 30-Jun-1990 11-Jun-1999
ferredoxin [2Fe-2S] II Synechococcus sp. (strain PCC 6301) Synechococcus sp. Cozens, A.L. Walker, J.E. J. Mol. Biol. 1941987359-383 The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin of chloroplasts. MUID87311713 S10833 DNA 1-105 EMBLX05302 NIDg48009 PIDNCAA28930.1 PIDg48019 Cozens, A.L. Walker, J.E. Biochem. J. 2521988563-569 Expression of a gene encoding a novel ferredoxin in the cyanobacterium Synechococcus 6301. MUID88326273 S00605 DNA 1-105 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein respiratory chain product ferredoxin [2Fe-2S] II 2-105 predicted domain ferredoxin [2Fe-2S] homology 25-79 binding-site 2Fe-2S cluster (Cys) (covalent) 40,45,48,78 predicted 105 complete MATYQVEVIYQGQSQTFTADSDQSVLDSAQAAGVDLPASCLTGVCTTCAARILSGEVDQP DAMGVGPEPAKQGYTLLCVAYPRSDLKIETHKEDELYALQFGQPG
FERFND JN0887 S18916 S44466 28-Aug-1985 27-Jan-1995 11-Jun-1999
ferredoxin [2Fe-2S]-like protein, fdxD Rhodobacter capsulatus Rhodobacter capsulatus Willison, J.C. Pierrard, J. Huebner, P. Gene 133199339-46 Sequence and transcript analysis of the nitrogenase structural gene operon (nifHDK) of Rhodobacter capsulatus: evidence for intramolecular processing of nifHDK mRNA. MUID94040794 JN0887 DNA 1-123 EMBLX63352 NIDg550144 PIDNCAA44953.1 PIDg550145 Willison, J.C. Pierrard, J. Huebner, P. Chabert, J. Vignais, P.M. submitted to the EMBL Data Library November1991 Northern blot analysis of the nitrogenase structural gene operon (nifHDK) of Rhodobacter capsulatus and identification of a ferredoxin-like gene (fdxD) upstream of nifHDK. S18916 DNA 1-52,'DL',55-123 Armengaud, J. Meyer, C. Jouanneau, Y. Biochem. J. 3001994413-418 Recombinant expression of the fdxD gene of Rhodobacter capsulatus and characterization of its product, a [2Fe-2S] ferredoxin. MUID94271155 S44466 preliminary DNA 1-123 fdxD ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S]-like protein, fdxD 2-123 predicted domain ferredoxin [2Fe-2S] homology 27-103 atypical binding-site 2Fe-2S cluster (Cys) (covalent) 42,47,50,102 predicted 123 complete MPNITFTSPIMKKDKTIYAVAGNTATILALAKEHAIPIPFECGDGDCASCLIEVTHLDNK PAMAMMLTEKEKARLKELQMITAEEIEAAEVSDLPPRFRLACQFIPRDEDVMVHFTGTPG GSV
FERFNC S08393 B39857 A39519 S39897 31-Dec-1990 27-Jan-1995 11-Jun-1999
ferredoxin [2Fe-2S] ferredoxin IV plant-type ferredoxin Rhodobacter capsulatus Rhodobacter capsulatus Saeki, K. Miyatake, Y. Young, D.A. Marrs, B.L. Matsubara, H. Nucleic Acids Res. 1819901060 A plant-ferredoxin-like gene is located upstream of ferredoxin I gene (fdxN) of Rhodobacter capsulatus. MUID90192101 S08393 DNA 1-95 EMBLX51316 NIDg46141 PIDNCAA35698.1 PIDg46142 Saeki, K. Suetsugu, Y. Tokuda, K. Miyatake, Y. Young, D.A. Marrs, B.L. Matsubara, H. J. Biol. Chem. 266199112889-12895 Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus. MUID91302301 B39857 DNA 1-95 GBX51316 GBS42008 NIDg46141 PIDNCAA35698.1 PIDg46142 Grabau, C. Schatt, E. Jouanneau, Y. Vignais, P.M. J. Biol. Chem. 26619913294-3299 A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia coli. MUID91131639 A39519 DNA 1-95 GBM59855 GBJ05743 NIDg151915 PIDNAAA26109.1 PIDg151916 Schmehl, M. Jahn, A. Meyer zu Vilsendorf, A. Hennecke, S. Masepohl, B. Schuppler, M. Marxer, M. Oelze, J. Klipp, W. Mol. Gen. Genet. 2411993602-615 Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. MUID94088454 S39897 preliminary DNA 1-95 EMBLX72888 NIDg435523 PIDNCAA51403.1 PIDg435529 fdxC ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product ferredoxin [2Fe-2S] 2-95 predicted domain ferredoxin [2Fe-2S] homology 23-82 binding-site 2Fe-2S cluster (Cys) (covalent) 38,43,46,81 predicted 95 complete MDKATLTFTDVSITVNVPTGTRIIEMSEKVGSGITYGCREGECGTCMTHILEGSENLSEP TALEMRVLEENLGGKDDRLACQCRVLGGAVKVRPA
A36003 A36003 B36003 21-Dec-1990 27-Jan-1995 13-Nov-1998
ferredoxin [2Fe-2S] precursor, hydrogenosomal Trichomonas vaginalis Trichomonas vaginalis host Homo sapiens (man) Johnson, P.J. d'Oliveira, C.E. Gorrell, T.E. Mueller, M. Proc. Natl. Acad. Sci. U.S.A. 8719906097-6101 Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis. MUID90349562 A36003 DNA 1-101 GBM33717 strain C1 (ATCC 30001) B36003 protein 9-70,'X',72-79,'X',81,'X',83-101 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein domain transit peptide (hydrogenosome) 1-8 predicted product ferredoxin [2Fe-2S] 9-101 experimental domain ferredoxin [2Fe-2S] homology 34-87 binding-site 2Fe-2S cluster (Cys) (covalent) 46,52,55,86 predicted 101 complete MLSQVCRFGTITAVKGGVKKQLKFEDDQTLFTVLTEAGLMSADDTCQGNKACGKCICKHV SGKVAAAEDDEKEFLEDQPANARLACAITLSGENDGAVFEL
AXHU A31853 A28999 A29920 A34586 S06400 S09484 03-Feb-1994 03-Feb-1994 19-Jan-2001
adrenodoxin precursor [validated] adrenal ferredoxin ferredoxin [2Fe-2S] 1 placental ferredoxin human man Homo sapiens Chang, C.Y. Wu, D.A. Lai, C.C. Miller, W.L. Chung, B.C. DNA 71988609-615 Cloning and structure of the human adrenodoxin gene. MUID89152748 A31853 DNA 1-184 GBM23665 NIDg340999 Picado-Leonard, J. Voutilainen, R. Kao, L. Chung, B. Strauss III, J.F. Miller, W.L. J. Biol. Chem. 26319883240-3244 Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. MUID88139395 A28999 mRNA 1-184 GBJ03548 NIDg178085 PIDNAAA96806.1 PIDg178086 this sequence has been revised in reference A29920 the revised sequence is shown Picado-Leonard, J. Voutilainen, R. Kao, L. Chung, B. Strauss III, J.F. Miller, W.L. J. Biol. Chem. 263198811016 erratum: addition of residues 4-7 and revision of residues 28 and 55 A29920 mRNA 1-184 GBJ03548 NIDg178085 PIDNAAA96806.1 PIDg178086 Chang, C.Y. Wu, D.A. Mohandas, T.K. Chung, B.C. DNA Cell Biol. 91990205-212 Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family. MUID90253614 A34586 mRNA 1-184 GBM34788 NIDg182495 PIDNAAA35829.1 PIDg182496 partial genomic sequences from two expressed genes and two pseudogenes were also determined Mittal, S. Zhu, Y.Z. Vickery, L.E. Arch. Biochem. Biophys. 2641988383-391 Molecular cloning and sequence analysis of human placental ferredoxin. MUID88292950 S06400 mRNA 1-184 GBM18003 NIDg182493 PIDNAAA76853.1 PIDg182494 Coghlan, V.M. Cupp, J.R. Vickery, L.E. Arch. Biochem. Biophys. 2641988376-382 Purification and characterization of human placental ferredoxin. MUID88292949 S09484 protein 61-68;182-184 placenta GDBFDX1 GDBFDX GDBADX GDB119657 OMIM103260 11q22-11q23 62/2; 104/1; 147/2 GDBFDX2 GDB128254 11q22-11q23 62/2; 104/1; 147/2 there are two functional genes on chromosome 11 there is disagreement about the position of FDX2 an electron transfer intermediate between ferredoxin--NADP+ reductase (adrenodoxin reductase) and mitochondrial forms of cytochrome P450 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein mitochondrion domain transit peptide (mitochondrion) 1-60 predicted product adrenodoxin 61-184 experimental domain ferredoxin [2Fe-2S] homology 89-153 binding-site 2Fe-2S cluster (Cys) (covalent) 106,112,115,152 predicted 184 complete MAAAGGARLLRAASAVLGGPAGRWLHHAGSRAGSSGLLRNRGPGGSAEASRSLSVSARAR SSSEDKITVHFINRDGETLTTKGKVGDSLLDVVVENNLDIDGFGACEGTLACSTCHLIFE DHIYEKLDAITDEENDMLDLAYGLTDRSRLGCQICLTKSMDNMTVRVPETVADARQSIDV GKTS
AXBO JX0094 A28069 B28441 A00260 JN0409 A28776 S06486 S21113 24-Apr-1984 31-Mar-1993 13-Nov-1998
adrenodoxin precursor adrenal ferredoxin ferredoxin [2Fe-2S] hepatoredoxin bovine cattle Bos primigenius taurus Sagara, Y. Sawae, H. Kimura, A. Sagara-Nakano, Y. Morohashi, K. Miyoshi, K. Horiuchi, T. J. Biochem. 107199077-83 Structural organization of the bovine adrenodoxin gene. MUID90236984 JX0094 DNA 1-186 GBD00468 Kagimoto, M. Kagimoto, K. Simpson, E.R. Waterman, M.R. J. Biol. Chem. 26319888925-8928 Transcription of the bovine adrenodoxin gene produces two species of mRNA of which only one is translated into adrenodoxin. MUID88243758 A28069 DNA 1-101 EMBLD00467 Okamura, T. Kagimoto, M. Simpson, E.R. Waterman, M.R. J. Biol. Chem. 262198710335-10338 Multiple species of bovine adrenodoxin mRNA. Occurrence of two different mitochondrial precursor sequences associated with the same mature sequence. MUID87280062 B28441 mRNA 23,'V',25-70 Tanaka, M. Haniu, M. Yasunobu, K.T. Kimura, T. J. Biol. Chem. 24819731141-1157 The amino acid sequence of bovine adrenodoxin. MUID73097075 A00260 protein 59-61,'Q',63-129,'N',131-133,'N',135-172 Chashchin, V.L. Lapko, V.N. Adamovich, T.B. Kirillova, N.M. Lapko, A.G. Akhrem, A.A. Bioorg. Khim. 1219861286-1289 The primary structure of hepatoredoxin from bovine liver mitochondria. MUID87048987 JN0409 protein 84-175 Sakihama, N. Hiwatashi, A. Miyatake, A. Shin, M. Ichikawa, Y. Arch. Biochem. Biophys. 264198823-29 Isolation and purification of mature bovine adrenocortical ferredoxin with an elongated carboxyl end. MUID88280262 A28776 protein 171-185 this protein purification yielded a form complete at the carboxyl end except for a single amino acid it is unclear whether the absence represents processing in vivo or an artifact of purification these results contradict the evidence for a carboxyl-terminal propeptide in reference JN0409 Driscoll, W.J. Omdahl, J.L. Eur. J. Biochem. 1851989181-187 Characterization and N-terminal amino acid sequence of multiple ferredoxins in kidney and adrenal mitochondria. MUID90032674 S06486 protein 59-76 Adrenodoxin is a component of the steroid hydroxylating system in adrenal cortex mitochondria. A minor (10%) component of adrenodoxin mRNA includes a defective alternate first exon that contains a stop codon and cannot lead to expression of the mature protein. 60/2; 100/1; 145/2 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S alternative splicing electron transfer iron-sulfur protein metalloprotein mitochondrion domain transit peptide (mitochondrion) 1-58 predicted product (or 59-185) adrenodoxin 59-186 experimental domain ferredoxin [2Fe-2S] homology 87-151 binding-site 2Fe-2S cluster (Cys) (covalent) 104,110,113,150 predicted 186 complete MAARLLRVASAALGDTAGRWRLLARPRAGAGGLRGSRGPGLGGGAVATRTLSVSGRAQSS SEDKITVHFINRDGETLTTKGKIGDSLLDVVVQNNLDIDGFGACEGTLACSTCHLIFEQH IFEKLEAITDEENDMLDLAYGLTDRSRLGCQICLTKAMDNMTVRVPDAVSDARESIDMGM NSSKIE
AXPG S20332 A00261 S06485 31-Jul-1979 07-Jun-1996 13-Nov-1998
adrenodoxin precursor adrenal ferredoxin ferredoxin [2Fe-2S] renodoxin pig domestic pig Sus scrofa domestica Omdahl, J.L. Wilson, K. Swerdlow, H. Driscoll, W.J. Arch. Biochem. Biophys. 2931992213-218 Molecular cloning and immunological characterization of porcine kidney ferredoxin. MUID92161799 S20332 preliminary not compared with conceptual translation mRNA 1-186 Akhrem, A.A. Lapko, A.G. Lapko, V.N. Morozova, L.A. Repin, V.A. Tishchenko, I.V. Chashchin, V.L. Bioorg. Khim. 41978462-475 Adrenodoxin. A00261 protein 59-175 Driscoll, W.J. Omdahl, J.L. Eur. J. Biochem. 1851989181-187 Characterization and N-terminal amino acid sequence of multiple ferredoxins in kidney and adrenal mitochondria. MUID90032674 S06485 protein 59-76 ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein mitochondrion domain transit peptide (mitochondrion) 1-58 predicted product adrenodoxin 59-186 predicted domain ferredoxin [2Fe-2S] homology 87-151 binding-site 2Fe-2S cluster (Cys) (covalent) 104,110,113,150 predicted 186 complete MAVRLLRVASAALGDTAVRWQPLVGPRAGNRGPGGSIWLGLGGRAAAARTLSLSARAWSS SEDKITVHFINRDGKTLTTQGKVGDSLLDVVIENNLDIDGFGACEGTLACSTCHLIFEDH IFEKLEAITDEENDMLDLAYGLTDRSRLGCQICLTKAMDNMTVRVPEAVADARESIDLGK NSSKLE
A39553 A39553 JC4538 PC4124 10-Sep-1999 10-Sep-1999 10-Sep-1999
adrenodoxin precursor adrenal ferredoxin ferredoxin [2Fe-2S] rat Norway rat Rattus norvegicus Mellon, S.H. Kushner, J.A. Vaisse, C. DNA Cell Biol. 101991339-347 Expression and regulation of adrenodoxin and P450-scc mRNA in rodent tissues. MUID91321737 A39553 preliminary not compared with conceptual translation mRNA 1-188 Sagara, Y. Watanabe, Y. Kawamura, K. Yubisui, T. Biol. Pharm. Bull. 19199639-41 Cloning and sequence analysis of a full-length cDNA of rat adrenodoxin. MUID96418123 JC4538 not compared with conceptual translation mRNA 1-126,'M',128-188 GBD50436 NIDg801871 PC4124 protein 65-79 adrenal gland Adrenodoxin is located in the mitochondrial matrix of steroidogenic tissues and functions as the common electron transporter from NADPH-adrenodoxin reductase to mitochondrial cytochromes P-450 which catalyze steroid hormone biosynthesis. ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S adrenal gland electron transfer iron-sulfur protein metalloprotein mitochondrion domain transit peptide (mitochondrion) 1-64 predicted product adrenodoxin 65-188 predicted domain ferredoxin [2Fe-2S] homology 93-157 binding-site 2Fe-2S cluster (Cys) (covalent) 110,116,119,156 predicted 188 complete MAAAPGARLLRAACASVAFRGLDCRRLLVCGTRAGPAVPQWTPSPHTLAEAGPGRPLSVS ARARSSSEDKVTVHFKNRDGETLTTKGKVGDSLLDVVIENNLDIDGFGACEGTLACSTCH LIFEDHIYEKLDAITDEENDMLDLAFGLTNRSRLGCQVCLTKAMDNMTVRVPEAVADVRQ SVDMSKNS
S53524 S53524 S60451 S60452 10-Sep-1999 10-Sep-1999 16-Jun-2000
adrenodoxin precursor adrenal ferredoxin cytochrome P450-linked ferredoxin mouse house mouse Mus musculus Stromstedt, M. Watermann, M.R. Biochim. Biophys. Acta 12611995126-128 A full-length cDNA encoding mouse adrenodoxin. MUID95200960 S53524 mRNA 1-188 EMBLL29123 NIDg457297 PIDNAAA74303.1 PIDg457298 Itoh, S. Iemura, O. Yamada, E. Yoshimura, T. Tsujikawa, K. Kohama, Y. Mimura, T. Biochim. Biophys. Acta 12631995173-178 Mouse cytochrome P-450 linked ferredoxin: its cDNA cloning and inducibility by dibutyryladenosine 3',5'-cyclic monophosphate and forskolin. MUID95367595 S60451 mRNA 1-188 EMBLD43689 NIDg1065599 PIDNBAA07786.1 PIDg1769821 clone F1-1 S60452 mRNA 1-188 EMBLD43690 NIDg1065600 PIDNBAA07787.1 PIDg1769822 clone F41-1 nuclear ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein mitochondrion domain transit peptide (mitochondrion) 1-64 predicted product adrenodoxin 65-188 predicted domain ferredoxin [2Fe-2S] homology 93-157 binding-site 2Fe-2S cluster (Cys) (covalent) 110,116,119,156 predicted 188 complete MAAAPGARLLRAACASVPFRGLDRCRLLVCGTGAGTAISPWTPSPRLHAEAGPGRPLSVS ARARSSSEDKITVHFKNRDGETLTTKGKIGDSLLDVVIENNLDIDGFGACEGTLACSTCH LIFEDHIYEKLDAITDEENDMLDLAFGLTDRSRLGCQVCLTKAMDNMTVRVPEAVADVRQ SVDMSKNS
PXPSEP JX0079 B35226 A00262 24-Apr-1984 06-Feb-1995 15-Sep-2000
putidaredoxin [validated] Pseudomonas putida Pseudomonas putida Koga, H. Yamaguchi, E. Matsunaga, K. Aramaki, H. Horiuchi, T. J. Biochem. 1061989831-836 Cloning and nucleotide sequences of NADH-putidaredoxin reductase gene (camA) and putidaredoxin gene (camB) involved in cytochrome P-450cam hydroxylase of Pseudomonas putida. MUID90130389 JX0079 DNA 1-107 GBD00528 NIDg216870 PIDNBAA00414.1 PIDg216873 strain PpGl ATCC17453 Peterson, J.A. Lorence, M.C. Amarneh, B. J. Biol. Chem. 26519906066-6073 Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins. MUID90202873 B35226 DNA 1-107 GBJ05406 NIDg151111 PIDNAAA25759.1 PIDg151113 Tanaka, M. Haniu, M. Yasunobu, K.T. Dus, K. Gunsalus, I.C. J. Biol. Chem. 24919743689-3701 The amino acid sequence of putidaredoxin, an iron-sulfur protein from Pseudomonas putida. MUID74268163 A00262 protein 2-14,'Q',16-107 Pochapsky, T.C. Ye, X.M. Ratnaswamy, G. Lyons, T.A. submitted to the Brookhaven Protein Data Bank July1994 PDB1PUT annotation conformation by (1)H-NMR, residues 2-14,'Q',16-107 Pochapsky, T.C. Ye, X.M. Ratnaswamy, G. Lyons, T.A. Biochemistry 3319946424-6432 An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. MUID95274325 annotation conformation by (1)H-NMR Putidaredoxin, which is involved in camphor hydroxylation, is distantly related to adrenodoxin from adrenal mitochondria and to the 2Fe-2S ferredoxin from Halobacterium halobium. The gene is located in a bacterial plasmid. camB ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product putidaredoxin 2-107 experimental domain ferredoxin [2Fe-2S] homology 24-88 binding-site 2Fe-2S cluster (Cys) (covalent) 40,46,49,87 experimental 107 complete MSKVVYVSHDGTRRELDVADGVSLMQAAVSNGIYDIVGDCGGSASCATCHVYVNEAFTDK VPAANEREIGMLECVTAELKPNSRLCCQIIMTPELDGIVVDVPDRQW
E42971 E42971 S27655 04-Mar-1993 17-May-1996 11-Jun-1999
terpredoxin Pseudomonas sp. Pseudomonas sp. Peterson, J.A. Lu, J.Y. Geisselsoder, J. Graham-Lorence, S. Carmona, C. Witney, F. Lorence, M.C. J. Biol. Chem. 267199214193-14203 Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. MUID92332528 E42971 DNA protein 1-106 EMBLM91440 NIDg151584 PIDNAAA25998.1 PIDg151589 submitted to the EMBL Data Library, April 1992 sequence extracted from NCBI backbone (NCBIP:108477) and corrected to correspond with the published sequence ferredoxin [2Fe-2S] ferredoxin [2Fe-2S] homology 2Fe-2S electron transfer iron-sulfur protein metalloprotein product terpredoxin 2-106 experimental domain ferredoxin [2Fe-2S] homology 24-88 binding-site 2Fe-2S cluster (Cys) (covalent) 40,46,49,87 predicted 106 complete MPRVVFIDEQSGEYAVDAQDGQSLMEVATQNGVPGIVAECGGSCVCATCRIEIEDAWVEI VGEANPDENDLLQSTGEPMTAGTRLSCQVFIDPSMDGLIVRVPLPA
FEPE A00196 24-Apr-1984 23-Mar-1995 20-Apr-2000
ferredoxin 2[4Fe-4S] [validated] Peptostreptococcus asaccharolyticus Peptostreptococcus asaccharolyticus Tsunoda, J.N. Yasunobu, K.T. Whiteley, H.R. J. Biol. Chem. 24319686262-6272 Non-heme iron proteins. IX. The amino acid sequence of ferredoxin from Micrococcus aerogenes. MUID69054261 the source is designated as Micrococcus aerogenes A00196 protein 1-21,23-24,'Q',26-55 Backes, G. Mino, Y. Loehr, T.M. Meyer, T.E. Cusanovich, M.A. Sweeney, W.V. Adman, E.T. Sanders-Loehr, J. J. Am. Chem. Soc. 11319912055-2064 The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy. annotation X-ray crystallography, 2.0 angstroms sequence revision sequence correction confirmed by peptide sequencing Adman, E.T. Sieker, L.C. Jensen, L.H. submitted to the Brookhaven Protein Data Bank August1976 PDB1FDX annotation X-ray crystallography, 2.0 angstroms, residues 1-21,'I',23-24,26-55 Adman, E.T. Sieker, L.C. Jensen, L.H. J. Biol. Chem. 25119763801-3806 Structure of Peptococcus aerogenes ferredoxin. Refinement at 2 angstroms resolution. MUID76213238 annotation X-ray crystallography, 2.0 angstroms Adman, E.T. Sieker, L.C. Jensen, L.H. J. Biol. Chem. 24819733987-3996 The structure of a bacterial ferredoxin. MUID73187389 annotation X-ray crystallography, 2.8 angstroms ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-54 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,46 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 18,36,39,42 experimental 55 complete AYVINDSCIACGACKPECPVNCIQEGSIYAIDADSCIDCGSCASVCPVGAPNPED
FEQFR A00197 14-Nov-1983 14-Nov-1983 18-Sep-1998
ferredoxin 2[4Fe-4S] Rhodospirillum rubrum Rhodospirillum rubrum Matsubara, H. Inoue, K. Hase, T. Hiura, H. Kakuno, T. Yamashita, J. Horio, T. J. Biochem. 9319831385-1390 Structure of the extracellular ferredoxin from Rhodospirillum rubrum: close similarity to clostridial ferredoxins. MUID83290779 A00197 protein 1-55 this is one of the four ferredoxins, most likely ferredoxin I, of R. rubrum ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-55 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,47 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,43 predicted 55 complete AYKIEETCISCGACAAECPVNAIEQGDTIFVVNADTCIDCGNCANVCPVGAPVAE
FECLCP A94028 A90550 A00198 07-May-1981 14-Nov-1997 20-Apr-2000
ferredoxin 2[4Fe-4S] [validated] Clostridium pasteurianum Clostridium pasteurianum Graves, M.C. Mullenbach, G.T. Rabinowitz, J.C. Proc. Natl. Acad. Sci. U.S.A. 8219851653-1657 Cloning and nucleotide sequence determination of the Clostridium pasteurianum ferredoxin gene. MUID85166189 A94028 DNA 1-56 GBM11214 GBM13633 GBM13682 NIDg144805 PIDNAAA83524.1 PIDg144806 ATCC:6013; soil spore initiator Met not shown Tanaka, M. Nakashima, T. Benson, A.M. Mower, H.F. Yasunobu, K.T. Biochemistry 519661666-1680 The amino acid sequence of Clostridium pasteurianum ferredoxin. MUID67120720 A90550 protein 2-56 Bertini, I. Donaire, A. Feinberg, B.A. Luchinat, C. Piccioli, M. Yuan, H. submitted to the Brookhaven Protein Data Bank June1995 PDB1CLF annotation conformation by (1)H-NMR, residues 2-56 Bertini, I. Donaire, A. Feinberg, B.A. Luchinat, C. Piccioli, M. Yuan, H. Eur. J. Biochem. 2321995192-205 Solution structure of the oxidized 2[4Fe-4S] ferredoxin from Clostridium pasteurianum. MUID96048047 annotation conformation by (1)H-NMR Scrofani, S.D.B. Brereton, P.S. Hamer, A.M. Lavery, M.J. McDowall, S.G. Vincent, G.A. Brownlee, R.T.C. Hoogenraad, N.J. Sadek, M. Wedd, A.G. Biochemistry 33199414486-14495 Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2[Fe-4-S-4] ferredoxin from Clostridium pasteurianum. MUID95072020 annotation conformation by (1)H-NMR ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] 2-56 experimental domain ferredoxin 2[4Fe-4S] homology 2-56 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,48 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 19,38,41,44 experimental 56 complete MAYKIADSCVSCGACASECPVNAISQGDSIFVIDADTCIDCGNCANVCPVGAPVQE
FECLCB A00199 07-May-1981 07-May-1981 18-Sep-1998
ferredoxin 2[4Fe-4S] Clostridium butyricum Clostridium butyricum Benson, A.M. Mower, H.F. Yasunobu, K.T. Proc. Natl. Acad. Sci. U.S.A. 5519661532-1535 The amino acid sequence of Clostridium butyricum ferredoxin. MUID67125829 A00199 protein 1-55 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-55 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,47 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,43 predicted 55 complete AFVINDSCVSCGACAGECPVSAITQGDTQFVIDADTCIDCGNCANVCPVGAPNQE
FECLCE A00200 07-May-1981 07-May-1981 18-Sep-1998
ferredoxin 2[4Fe-4S] Clostridium sp. Clostridium sp. Tanaka, M. Haniu, M. Yasunobu, K.T. Jones, J.B. Stadtman, T.C. Biochemistry 1319745284-5289 Amino acid sequence determination of the Clostridium M-E ferredoxin and a comment on the role of the aromatic residues in the clostridial ferredoxins. MUID75054829 A00200 protein 1-55 strain M-E ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-55 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,47 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,43 predicted 55 complete AYKITDGCINCGACEPECPVEAISESDAVRVIDADKCIDCGACANTCPVDAIVEG
FECLCU S36790 A00201 24-Apr-1984 22-Apr-1995 20-Apr-2000
ferredoxin 2[4Fe-4S] [validated] Clostridium acidiurici Clostridium acidiurici Meyer, J. Moulis, J.M. Scherrer, N. Gagnon, J. Ulrich, J. Biochem. J. 2941993622-623 Sequences of clostridial ferredoxins: determination of the Clostridium sticklandii sequence and correction of the Clostridium acidurici sequence. MUID93384542 S36790 protein 1-55 Rall, S.C. Bolinger, R.E. Cole, R.D. Biochemistry 819692486-2496 The amino acid sequence of ferredoxin from Clostridium acidi-urici. MUID69253175 A00201 protein 1-14,'D',16-20,'D',22-24,'Q',26-27,'S',29-55 Duee, E. Fanchon, E. Vicat, J. Sieker, L.C. Meyer, J. Moulis, J.M. submitted to the Brookhaven Protein Data Bank March1994 PDB1FDN annotation X-ray crystallography, 1.84 angstroms, residues 1-55 ATCC:7906 Tranqui, D. Jesior, J.C. submitted to the Brookhaven Protein Data Bank September1994 PDB1FCA annotation X-ray crystallography, 1.8 angstroms, residues 1-20,'D',22-24,'Q',26,'GS',29-55 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-55 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,47 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,43 experimental 55 complete AYVINEACISCGACEPECPVNAISSGDDRYVIDADTCIDCGACAGVCPVDAPVQA
FECLCT A92138 A92086 A00202 24-Apr-1984 04-Dec-1986 18-Sep-1998
ferredoxin 2[4Fe-4S] Clostridium thermosaccharolyticum Clostridium thermosaccharolyticum, Clostridium tartarivorum Tanaka, M. Haniu, M. Yasunobu, K.T. Himes, R.H. Akagi, J.M. J. Biol. Chem. 24819735215-5217 The primary structure of the Clostridium thermosaccharolyticum ferredoxin, a heat-stable ferredoxin. MUID74071583 A92138 protein 1-55 Tanaka, M. Haniu, M. Matsueda, G. Yasunobu, K.T. Himes, R.H. Akagi, J.M. Barnes, E.M. Devanathan, T. J. Biol. Chem. 24619713953-3960 The primary structure of the Clostridium tartarivorum ferredoxin, a heat-stable ferredoxin. MUID71259897 A92086 protein 1-30,'Q',32-43,'Q',45-55 the authors considered C. tartarivorum to be a separate species ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-55 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,47 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,43 predicted 55 complete AHIITDECISCGACAAECPVEAIHEGTGKYEVDADTCIDCGACEAVCPTGAVKAE
FEME A00203 13-Jul-1981 13-Jul-1981 18-Sep-1998
ferredoxin 2[4Fe-4S] Megasphaera elsdenii Megasphaera elsdenii Azari, P. Glantz, M. Tsunoda, J. Yasunobu, K.T. unpublished results, cited by Yasunobu, K.T., and Tanaka, M., Syst. Zool. 22, 570-589 1973 A00203 protein 1-54 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-54 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,46 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,36,39,42 predicted 54 complete MHVISDECVKCGACASTCPTGAIEEGETKYVVTDSCIDCGACEAVCPTGAISAE
FEMZB A00204 05-Apr-1983 05-Apr-1983 18-Sep-1998
ferredoxin 2[4Fe-4S] Methanosarcina barkeri Methanosarcina barkeri Hausinger, R.P. Moura, I. Moura, J.J.G. Xavier, A.V. Santos, M.H. LeGall, J. Howard, J.B. J. Biol. Chem. 257198214192-14197 Amino acid sequence of a 3Fe:3S ferredoxin from the "archaebacterium" Methanosarcina barkeri (DSM 800). MUID83056954 A00204 protein 1-59 strain DSM 800 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 2-58 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,50 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 19,40,43,46 predicted 59 complete PATVNADECSGCGTCVDECPNDAITLDEEKGIAVVDNDECVECGACEEACPNQAIKVEE
FECI A00206 07-May-1981 07-May-1981 18-Sep-1998
ferredoxin 2[4Fe-4S] I Chlorobium limicola Chlorobium limicola Tanaka, M. Haniu, M. Yasunobu, K.T. Evans, M.C.W. Rao, K.K. Biochemistry 1319742953-2959 Amino acid sequence of ferredoxin from a photosynthetic green bacterium, Chlorobium limicola. MUID74271985 A00206 protein 1-60 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-60 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,52 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,48 predicted 60 complete ALYITEECTYCGACEPECPVTAISAGDDIYVIDANTCNECAGLDEQACVAVCPAECIVQG
FECF A00207 30-Jun-1979 23-Oct-1981 18-Sep-1998
ferredoxin 2[4Fe-4S] Chlorobium sp. Chlorobium sp. Hase, T. Wakabayashi, S. Matsubara, H. Evans, M.C.W. Jennings, J.V. J. Biochem. 8319781321-1325 Amino acid sequence of a ferredoxin from Chlorobium thiosulfatophilum strain Tassajara, a photosynthetic green sulfur bacterium. MUID78194080 A00207 protein 1-61 strain Tassajara the source was designated as Chlorobium thiosulfatophilum ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-61 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,53 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,49 predicted 61 complete ALYITEECTYCGACEPECPTNAISAGSEIYVIDAAGCTECVGFADAPACAAVCPAECIVQ G
FECI2 A00208 07-May-1981 07-May-1981 18-Sep-1998
ferredoxin 2[4Fe-4S] II Chlorobium limicola Chlorobium limicola Tanaka, M. Haniu, M. Yasunobu, K.T. Evans, M.C.W. Rao, K.K. Biochemistry 1419751938-1943 The amino acid sequence of ferredoxin II from Chlorobium limicola, a photosynthetic green bacterium. MUID75146531 A00208 protein 1-61 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-61 binding-site 4Fe-4S cluster (Cys) (covalent) 8,11,14,53 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 18,37,40,49 predicted 61 complete AHRITEECTYCAACEPECPVNAISAGDEIYIVDESVCTDCEGYYDEPACVAVCPVDCIIK V
FERF1P A00209 28-May-1986 28-May-1986 18-Sep-1998
ferredoxin 2[4Fe-4S] I Rhodopseudomonas palustris Rhodopseudomonas palustris Minami, Y. Wakabayashi, S. Yamada, F. Wada, K. Zumft, W.G. Matsubara, H. J. Biochem. 961984585-592 Ferredoxins from the photosynthetic purple non-sulfur bacterium Rhodopseudomonas palustris. Isolation and amino acid sequence of ferredoxin I. MUID85054727 A00209 protein 1-63 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S duplication electron transfer iron-sulfur protein metalloprotein photosynthesis domain ferredoxin 2[4Fe-4S] homology 2-62 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,54 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 19,38,41,50 predicted 63 complete AYKIITSQCTVCGACEFECPNAAIAMKRGTYVIDAVKCTECEGHFDKPQCVAVCPVDNTC VPA
FERF1C A33498 S08394 C39857 B39519 S39898 JX0133 27-Feb-1990 27-Jan-1995 24-Sep-1999
ferredoxin 2[4Fe-4S] I Rhodobacter capsulatus Rhodobacter capsulatus Schatt, E. Jouanneau, Y. Vignais, P.M. J. Bacteriol. 17119896218-6226 Molecular cloning and sequence analysis of the structural gene of ferredoxin I from the photosynthetic bacterium Rhodobacter capsulatus. MUID90036712 A33498 DNA 1-65 GBM31073 NIDg151918 PIDNAAA26111.1 PIDg151919 Saeki, K. Miyatake, Y. Young, D.A. Marrs, B.L. Matsubara, H. Nucleic Acids Res. 1819901060 A plant-ferredoxin-like gene is located upstream of ferredoxin I gene (fdxN) of Rhodobacter capsulatus. MUID90192101 S08394 DNA 1-65 EMBLX51316 NIDg46141 PIDNCAA35699.1 PIDg46143 Saeki, K. Suetsugu, Y. Tokuda, K. Miyatake, Y. Young, D.A. Marrs, B.L. Matsubara, H. J. Biol. Chem. 266199112889-12895 Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus. MUID91302301 C39857 DNA 1-65 GBX51316 GBS42008 NIDg46141 PIDNCAA35699.1 PIDg46143 Grabau, C. Schatt, E. Jouanneau, Y. Vignais, P.M. J. Biol. Chem. 26619913294-3299 A new [2Fe-2S] ferredoxin from Rhodobacter capsulatus. Coexpression with a 2[4Fe-4S] ferredoxin in Escherichia coli. MUID91131639 B39519 DNA 1-8 GBM59855 GBJ05743 NIDg151915 PIDNAAA26110.1 PIDg151917 Schmehl, M. Jahn, A. Meyer zu Vilsendorf, A. Hennecke, S. Masepohl, B. Schuppler, M. Marxer, M. Oelze, J. Klipp, W. Mol. Gen. Genet. 2411993602-615 Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. MUID94088454 S39898 preliminary DNA 1-65 EMBLX72888 NIDg435523 PIDNCAA51404.1 PIDg435530 Saeki, K. Suetsugu, Y. Yao, Y. Horio, T. Marrs, B.L. Matsubara, H. J. Biochem. 1081990475-482 Two distinct ferredoxins from Rhodobacter capsulatus: complete amino acid sequences and molecular evolution. MUID91115797 JX0133 protein 2-65 fdxN ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] I 2-65 experimental domain ferredoxin 2[4Fe-4S] homology 3-63 binding-site 4Fe-4S cluster (Cys) (covalent) 10,13,16,55 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,51 predicted 65 complete MAMKIDPELCTSCGDCEPVCPTNAIAPKKGVYVINADTCTECEGEHDLPQCVNACMTDNC INPAA
FERMN C32361 JE0034 S04411 21-May-1990 27-Jan-1995 11-Jun-1999
ferredoxin 2[4Fe-4S] Rhizobium meliloti Rhizobium meliloti Mulligan, M.E. Buikema, W.J. Haselkorn, R. J. Bacteriol. 17019884406-4410 Bacterial-type ferredoxin genes in the nitrogen fixation regions of the cyanobacterium Anabaena sp. strain PCC 7120 and Rhizobium meliloti. MUID88314954 C32361 DNA 1-64 GBM21841 NIDg152194 PIDNAAA26268.1 PIDg152195 Klipp, W. Reilaender, H. Schlueter, A. Krey, R. Puehler, A. Mol. Gen. Genet. 2161989293-302 The Rhizobium meliloti fdxN gene encoding a ferredoxin-like protein is necessary for nitrogen fixation and is cotranscribed with nifA and nifB. MUID89313667 JE0034 DNA 1-64 GBX52662 NIDg288340 PIDNCAA36890.1 PIDg288342 strain 2011 fdxN ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] I 2-64 predicted domain ferredoxin 2[4Fe-4S] homology 3-63 binding-site 4Fe-4S cluster (Cys) (covalent) 10,13,16,55 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,51 predicted 64 complete MAFKIIASQCTQCGACEFECPRGAVNFKGEKYVIDPTKCNECKGGFDTQQCASVCPVSNT CVPA
FEKRV S72167 S78121 A00210 13-Jul-1981 30-Jan-1998 20-Apr-2000
ferredoxin 2[4Fe-4S] [validated] Chromatium vinosum Chromatium vinosum Moulis, J.M. Biochim. Biophys. Acta 1308199612-14 Molecular cloning and expression of the gene encoding Chromatium vinosum 2[4Fe-4S] ferredoxin. MUID96328257 S72167 nucleic acid sequence not shown DNA 1-83 EMBLU45327 NIDg1518925 PIDNAAC44333.1 PIDg1518927 S78121 protein 2-18 Hase, T. Matsubara, H. Evans, M.C.W. J. Biochem. 8119771745-1749 Amino acid sequence of Chromatium vinosum ferredoxin: revisions. MUID77249448 A00210 protein 2-7,'Q',9-12,'N',14-15,'Q',17-83 Dauter, Z. Wilson, K.S. Sieker, L.C. Moulis, J.M. submitted to the Brookhaven Protein Data Bank April1996 PDB1BLU annotation X-ray crystallography, 2.1 angstroms, residues 2-81 Huber, J.G. Gaillard, J. Moulis, J.M. Biochemistry 341995194-205 NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters. MUID95118987 annotation conformation by (1)H-NMR and (13)C-NMR ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] 2-83 experimental domain ferredoxin 2[4Fe-4S] homology 2-62 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,54 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 19,38,41,50 experimental 83 complete MALMITDECINCDVCEPECPNGAISQGDETYVIEPSLCTECVGHYETSQCVEVCPVDCII KDPSHEETEDELRAKYERITGEG
E64554 E64554 20-Apr-2000 20-Apr-2000 21-Jul-2000
ferredoxin 2[4Fe-4S] HP0277 [similarity] Helicobacter pylori (strain 26695) Helicobacter pylori Tomb, J.F. White, O. Kerlavage, A.R. Clayton, R.A. Sutton, G.G. Fleischmann, R.D. Ketchum, K.A. Klenk, H.P. Gill, S. Dougherty, B.A. Nelson, K. Quackenbush, J. Zhou, L. Kirkness, E.F. Peterson, S. Loftus, B. Richardson, D. Dodson, R. Khalak, H.G. Glodek, A. McKenney, K. Fitzegerald, L.M. Lee, N. Adams, M.D. Hickey, E.K. Berg, D.E. Gocayne, J.D. Utterback, T.R. Peterson, J.D. Kelley, J.M. Cotton, M.D. Weidman, J.M. Fujii, C. Bowman, C. Watthey, L. Wallin, E. Hayes, W.S. Borodovsky, M. Karpk, P.D. Smith, H.O. Fraser, C.M. Venter, J.C. Nature 3881997539-547 The complete genome sequence of the gastric pathogen Helicobacter pylori. MUID97394467 E64554 nucleic acid sequence not shown translation not shown DNA 1-84 GBAE000546 GBAE000511 NIDg2313363 PIDNAAD07340.1 PIDg2313367 TIGRHP0277 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 2-63 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,55 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 19,38,41,51 predicted 84 complete MSLLVNDECIACDACREECPSEAIEEGDPIYNIDPDRCTECYGYDDDEPRCVSVCPVDAI LPDPNNAESKEELKYKYESLKEQD
E71954 E71954 20-Apr-2000 20-Apr-2000 21-Jul-2000
ferredoxin 2[4Fe-4S] jhp0262 [similarity] Helicobacter pylori (strain J99) Helicobacter pylori strain J99 Alm, R.A. Ling, L.S.L. Moir, D.T. King, B.L. Brown, E.D. Doig, P.C. Smith, D.R. Noonan, B. Guild, B.C. deJonge, B.L. Carmel, G. Tummino, P.J. Caruso, A. Uria-Nickelsen, M. Mills, D.M. Ives, C. Gibson, R. Merberg, D. Mills, S.D. Jiang, Q. Taylor, D.E. Vovis, G.F. Trust, T.J. Nature 3971999176-180 Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori. MUID99120557 E71954 DNA 1-84 GBAE001463 GBAE001439 NIDg4154775 PIDNAAD05841.1 PIDg4154783 strain J99 jhp0262 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 2-63 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,55 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 19,38,41,51 predicted 84 complete MSLLVNDECIACDACREECPSEAIEEGDPIYSIDPDRCTECYGYDDDEPRCVSVCPVDAI LPDPNNAESKEELKYKYEILKEQD
FEAIN A32361 B34443 21-May-1990 27-Jan-1995 11-Jun-1999
ferredoxin 2[4Fe-4S] fdxN Anabaena sp. (strain PCC 7120) Anabaena sp. Mulligan, M.E. Buikema, W.J. Haselkorn, R. J. Bacteriol. 17019884406-4410 Bacterial-type ferredoxin genes in the nitrogen fixation regions of the cyanobacterium Anabaena sp. strain PCC 7120 and Rhizobium meliloti. MUID88314954 A32361 DNA 1-116 GBJ05111 NIDg142034 PIDNAAA22005.1 PIDg142036 Mulligan, M.E. Haselkorn, R. J. Biol. Chem. 264198919200-19207 Nitrogen fixation (nif) genes of the cyanobacterium Anabaena species strain PCC 7120. The nifB-fdxN-nifS-nifU operon. MUID90037054 B34443 DNA 98-116 GBJ05111 GBJ01538 GBM21840 GBX05593 GBX05595 fdxN ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] fdxN 2-116 predicted domain ferredoxin 2[4Fe-4S] homology 2-64 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,56 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 19,39,42,52 predicted 116 complete MAYTITSQCISCKLCSSVCPTGAIKIAENGQHWIDSELCTNCVDTVYTVPQCKAGCPTCD GCVKVPSDYWEGWFANYNRVIAKLTKKQDYWERWFNCYSQKFSEQLQKHQGEILGV
FERF3C B32308 A46701 08-Dec-1989 27-Jan-1995 11-Jun-1999
ferredoxin 2[4Fe-4S] III dimeric ferredoxin Rhodobacter capsulatus Rhodobacter capsulatus Moreno-Vivian, C. Hennecke, S. Puehler, A. Klipp, W. J. Bacteriol. 17119892591-2598 Open reading frame 5 (ORF5), encoding a ferredoxinlike protein, and nifQ are cotranscribed with nifE, nifN, nifX, and ORF4 in Rhodobacter capsulatus. MUID89213944 B32308 DNA 1-102 GBM26323 NIDg341472 PIDNAAA26146.1 PIDg516637 Jouanneau, Y. Meyer, C. Gaillard, J. Forest, E. Gagnon, J. J. Biol. Chem. 268199310636-10644 Purification and characterization of a novel dimeric ferredoxin (FdIII) from Rhodobacter capsulatus. MUID93252956 A46701 protein 3-102 strain B10 sequence extracted from NCBI backbone (NCBIP:131349) homodimer ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S homodimer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] III 3-102 experimental domain ferredoxin 2[4Fe-4S] homology 20-99 binding-site 4Fe-4S cluster (Cys) (covalent) 27,30,33,91 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 37,81,84,87 predicted 102 complete MMPTVAYTRGGAEYTPVYLMKIDEQKCIGCGRCFKVCGRDVMSLHGLTEDGQVVAPGTDE WDEVEDEIVKKVMALTGAENCIGCGACARVCPSECQTHAALS
FERMX D26952 A26933 05-Oct-1988 27-Jan-1995 11-Jun-1999
ferredoxin [4Fe-4S] Rhizobium meliloti Rhizobium meliloti Earl, C.D. Ronson, C.W. Ausubel, F.M. J. Bacteriol. 16919871127-1136 Genetic and structural analysis of the Rhizobium meliloti fixA, fixB, fixC, and fixX genes. MUID87137267 D26952 DNA 1-98 GBM15546 NIDg340664 PIDNAAA21771.1 PIDg551201 strain 1021 Dusha, I. Kovalenko, S. Banfalvi, Z. Kondorosi, A. J. Bacteriol. 16919871403-1409 Rhizobium meliloti insertion element ISRm2 and its use for identification of the fixX gene. MUID87165742 A26933 DNA 1-61,'I',63-96,'S',98 GBM15787 NIDg152228 PIDNAAA26282.1 PIDg152229 strain 41 the authors translated the codon TCC for residue 97 as Phe fixX ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin [4Fe-4S] 2-98 predicted domain ferredoxin 2[4Fe-4S] homology 29-84 binding-site 4Fe-4S cluster (Cys) (covalent) 46,66,69,72 predicted 98 complete MKTAIAERIEDKLYQNRYLVDAGRPHITVRPHRSPSLNLLALTRVCPAKCYELNETGQVE VTADGCMECGTCRVLCEANGDVEWSYPRGGFGVLFKFG
JC1001 B25878 JC1001 03-Dec-1999 20-Apr-2000 20-Apr-2000
ferredoxin [4Fe-4S] fixX Rhizobium leguminosarum plasmid pRL6JI Rhizobium leguminosarum Gronger, P. Manian, S.S. Reilander, H. O'Connell, M. Priefer, U.B. Puhler, A. Nucleic Acids Res. 15198731-49 Organization and partial sequence of a DNA region of the Rhizobium leguminosarum symbiotic plasmid pRL6JI containing the genes fixABC, nifA, nifB and a novel open reading frame. MUID87146339 B25878 DNA 1-98 GBX05049 NIDg46199 PIDNCAA28722.1 PIDg46201 Ni, F.D. Hong, G.F. Acta Biochim. Biophys. Sin. 231991458-462 DNA sequence study of the Fix X gene of Rhizobium leguminosarum 248. JC1001 DNA 1,'R',3-4,'I',6-22,'G',24-37,'N',39-52,'L',54-62,'P',64-75,'C',77-98 article in Chinese with English abstract the authors translated the codon AGG for residue 2 as Lys fixX plasmid ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 29-84 binding-site 4Fe-4S cluster (Cys) (covalent) 46,66,69,72 predicted 98 complete MKATTIERIEDKLYQNRYLVDTRRPHITVRPHRSPSPSLLALTQICPAKCYEVNEIGQVA IVSDGCLECGTCRVLAEASGDIKWNYPRGGFGVLFKFG
A27510 A27510 10-Sep-1999 10-Sep-1999 10-Sep-1999
ferredoxin 2[4Fe-4S]-like protein Rhizobium leguminosarum bv. trifolii Rhizobium leguminosarum bv. trifolii Iismaa, S.E. Watson, J.M. Nucleic Acids Res. 1519873180 A gene upstream of the Rhizobium trifolii nifA gene encodes a ferredoxin-like protein. MUID87174837 A27510 DNA 1-98 GBX05257 NIDg46456 PIDNCAA28879.1 PIDg46457 strain ANU843 FixX ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology electron transfer domain ferredoxin 2[4Fe-4S] homology 29-84 98 complete MKAIVKRRVEDKLYQNRYLVDPGRPHISVRKHLFPTPNLIALTQVCPAKCYQLNDRRQVI IVSDGCLECGTCNVLCGPDGDIEWTYPRGGFGVLFKFG
S04185 S04185 10-Sep-1999 10-Sep-1999 10-Sep-1999
ferredoxin [4Fe-4S] fixX ferredoxin homolog Bradyrhizobium japonicum Bradyrhizobium japonicum Gubler, M. Zuercher, T. Hennecke, H. Mol. Microbiol. 31989141-148 The Bradyrhizobium japonicum fixBCX operon: identification of fixX and of a 5' mRNA region affecting the level of the fixBCX transcript. MUID89343618 S04185 DNA 1-98 EMBLX13144 NIDg39519 PIDNCAA31540.1 PIDg39521 fixX ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 29-84 binding-site 4Fe-4S cluster (Cys) (covalent) 46,66,69,72 predicted 98 complete MNVEPSVRVEDKLYYNRYLVDAGHPHVRVRAHKTPSPQLLTLLKACPARCYELNDNGQVE VTVDGCIECGTCRVIAEPTGDIEWSHPRGGYGVLFKFG
FEPSTV A30025 08-Mar-1989 27-Jan-1995 18-Sep-1998
ferredoxin [3Fe-4S][4Fe-4S] Pseudomonas stutzeri Pseudomonas stutzeri Saeki, K. Wakabayashi, S. Zumft, W.G. Matsubara, H. J. Biochem. 1041988242-246 Pseudomonas stutzeri ferredoxin: close similarity to Azotobacter vinelandii and Pseudomonas ovalis ferredoxins. MUID89034013 A30025 protein 1-106 The identity of the iron-sulfur clusters is uncertain; [3Fe-4S][4Fe-4S] clusters have been assigned on the basis of similarity with Azotobacter vinelandii ferredoxin [3Fe-4S][4Fe-4S] (see PIR:JS0191). ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-57 binding-site 3Fe-4S cluster (Cys) (covalent) 8,16,49 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,45 predicted 106 complete TFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEV PEDQQEFIELNADLAEVWPNITEKKDALADAEEWDGVKDKLQYLER
FEAV A29936 A00218 17-Dec-1982 31-Mar-1992 20-Apr-2000
ferredoxin [3Fe-4S][4Fe-4S] [validated] ferredoxin I Azotobacter vinelandii Azotobacter vinelandii Morgan, T.V. Lundell, D.J. Burgess, B.K. J. Biol. Chem. 26319881370-1375 Azotobacter vinelandii ferredoxin I: cloning, sequencing, and mutant analysis. MUID88087274 A29936 DNA 1-107 GBJ03521 NIDg142303 PIDNAAA22125.1 PIDg142304 Howard, J.B. Lorsbach, T.W. Ghosh, D. Melis, K. Stout, C.D. J. Biol. Chem. 2581983508-522 Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues. MUID83082915 sequence X-ray crystallography, 2 angstroms A00218 protein 2-107 Stout, C.D. submitted to the Brookhaven Protein Data Bank June1993 PDB1FDA annotation X-ray crystallography, 2.1 angstroms, oxidized, pH 6, residues 2-107 Stout, C.D. submitted to the Brookhaven Protein Data Bank June1993 PDB1FDB annotation X-ray crystallography, 2.2 angstroms, reduced, pH 6, residues 2-107 Stout, C.D. submitted to the Brookhaven Protein Data Bank June1993 PDB5FD1 annotation X-ray crystallography, 1.9 angstroms, oxidized, pH 8, residues 2-107 Stout, C.D. submitted to the Brookhaven Protein Data Bank June1993 PDB1FDC annotation X-ray crystallography, 2.1 angstroms, reduced, pH 8, residues 2-107 Merritt, E.A. Stout, G.H. Turley, S. Sieker, L.C. Jensen, L.H. Orme-johnson, W.H. submitted to the Brookhaven Protein Data Bank September1992 PDB1FER annotation X-ray crystallography, 2.3 angstroms, residues 2-107 Stout, G.H. Turley, S. Sieker, L.C. Jensen, L.H. Proc. Natl. Acad. Sci. U.S.A. 8519881020-1022 Structure of ferredoxin I from Azotobacter vinelandii. MUID88124966 annotation X-ray crystallography Stout, C.D. J. Mol. Biol. 2051989545-555 Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 Angstroms resolution. MUID89178673 annotation X-ray crystallography, 1.9 angstroms Stout, C.D. J. Biol. Chem. 26319889256-9260 7-Iron ferredoxin revisited. MUID88243805 annotation X-ray crystallography, 2.7 angstroms fdxA ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin [3Fe-4S][4Fe-4S] 2-107 experimental domain ferredoxin 2[4Fe-4S] homology 2-58 binding-site 3Fe-4S cluster (Cys) (covalent) 9,17,50 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 21,40,43,46 experimental 107 complete MAFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDE VPEDMQEFIQLNAELAEVWPNITEKKDPLPDAEDWDGVKGKLQHLER
FEPSFV A00217 31-May-1979 08-Oct-1981 18-Sep-1998
ferredoxin [3Fe-4S][4Fe-4S] Pseudomonas putida Pseudomonas putida Hase, T. Wakabayashi, S. Matsubara, H. Ohmori, D. Suzuki, K. FEBS Lett. 911978315-319 Pseudomonas ovalis ferredoxin: similarity to Azotobacter and Chromatium ferredoxins. MUID78239082 A00217 protein 1-106 the source was designated as Pseudomonas ovalis The identity of the iron-sulfur clusters is uncertain; [3Fe-4S][4Fe-4S] cluster have been assigned on the basis of similarity with Azotobacter vinelandii ferredoxin [3Fe-4S][4Fe-4S] (see PIR:JS0191). ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-57 binding-site 3Fe-4S cluster (Cys) (covalent) 8,16,49 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,45 predicted 106 complete TFVVTDNCIKCKYTDCVEVCPVDCFYEGPNFLVIHPDECIDCALCEPECPAQAIFSEDEV PSGMENFIELNAELAEIWPNITERKDALPDAEEWDGKPGKIADLER
FETWT A00216 13-Aug-1986 13-Aug-1986 03-Nov-2000
ferredoxin [3Fe-4S][4Fe-4S] Thermus aquaticus Thermus aquaticus Sato, S. Nakazawa, K. Hon-Nami, K. Oshima, T. Biochim. Biophys. Acta 6681981277-289 Purification, some properties and amino acid sequence of Thermus thermophilus HB8 ferredoxin. MUID81184605 A00216 protein 1-69;97-105 strain HB8; ATCC 27634 Hille, R. Yoshida, T. Tarr, G.E. Williams Jr., C.H. Ludwig, M.I. Fee, J.A. Kent, T.A. Huynh, B.H. Munck, E. J. Biol. Chem. 258198313008-13013 Studies of the ferredoxin from Thermus thermophilus. MUID84032522 annotation composition we have positioned residues 70-96 by homology with other Azotobacter-type ferredoxins strain ATCC 696 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S duplication electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-57 binding-site 3Fe-4S cluster (Cys) (covalent) 8,16,49 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,45 predicted 105 complete tentative PHVICQPCIGVKDQSCVEVCPVECIYDGGDQFYIHPEECIDCGACVPACPVNAIYPEEDV PEQWKSYIE(L.N.A.E.L.A.E.I.W.P.N.I.T.E.R.K.D.V.L.P.D.A.E.H.W. D.G)KNRKLAGLE
FERF2C S10976 A34968 A39857 JX0134 30-Jun-1991 30-Jun-1991 11-Jun-1999
ferredoxin [3Fe-4S][4Fe-4S] ferredoxin II Rhodobacter capsulatus Rhodobacter capsulatus Duport, C. Jouanneau, Y. Vignais, P.M. Nucleic Acids Res. 1819904618 Nucleotide sequence of fdxA encoding a 7Fe ferredoxin of Rhodobacter capsulatus. MUID90356425 S10976 DNA 1-112 EMBLX53300 NIDg46011 PIDNCAA37388.1 PIDg46012 A34968 protein 2-31 Saeki, K. Suetsugu, Y. Tokuda, K. Miyatake, Y. Young, D.A. Marrs, B.L. Matsubara, H. J. Biol. Chem. 266199112889-12895 Genetic analysis of functional differences among distinct ferredoxins in Rhodobacter capsulatus. MUID91302301 A39857 DNA 1-112 GBM64555 NIDg151913 PIDNAAA26108.1 PIDg151914 Saeki, K. Suetsugu, Y. Yao, Y. Horio, T. Marrs, B.L. Matsubara, H. J. Biochem. 1081990475-482 Two distinct ferredoxins from Rhodobacter capsulatus: complete amino acid sequences and molecular evolution. MUID91115797 JX0134 protein 2-112 fdxA ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin [3Fe-4S][4Fe-4S] 2-112 experimental domain ferredoxin 2[4Fe-4S] homology 2-58 binding-site 3Fe-4S cluster (Cys) (covalent) 9,17,50 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,40,43,46 predicted 112 complete MTYVVTDNCIACKYTDCVEVCPVDCFYEGENTLVIHPDECIDCGVCEPECPADAIRPDTE PGMEDWVEFNRTYASQWPVITIKKDPMPDHKKYDGETGKREKYFSPNPGTGD
FEBSA A00215 13-Aug-1986 13-Aug-1986 18-Sep-1998
ferredoxin [3Fe-4S][4Fe-4S] Alicyclobacillus acidocaldarius Alicyclobacillus acidocaldarius Schlatter, D. Waldvogel, S. Zulli, F. Suter, F. Portmann, W. Zuber, H. Biol. Chem. Hoppe-Seyler 3661985223-231 Purification, amino-acid sequence and some properties of the ferredoxin isolated from Bacillus acidocaldarius. MUID85225952 A00215 protein 1-78 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S duplication electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-57 binding-site 3Fe-4S cluster (Cys) (covalent) 8,16,49 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,45 predicted 78 complete PFVITSPCIGEKAADCVETCPVDAIHEGPDQYYIDPDLCIDCAACEPVCPVNAIYQEEFV PEDEKEFIEKNRNFFRNR
FEDV2N A00213 13-Jun-1983 13-Jun-1983 18-Sep-1998
ferredoxin 2[4Fe-4S] II Desulfovibrio desulfuricans Desulfovibrio desulfuricans Guerlesquin, F. Bruschi, M. Bovier-Lapierre, G. Bonicel, J. Couchoud, P. Biochimie 65198343-47 Primary structure of the two (4 Fe-4 S) clusters ferredoxin from Desulfovibrio desulfuricans (strain Norway 4). MUID83153918 A00213 protein 1-59 strain Norway 4 the active protein is a dimer of identical chains, each containing two 4Fe-4S clusters ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] II 2-59 experimental domain ferredoxin 2[4Fe-4S] homology 5-59 binding-site 4Fe-4S cluster (Cys) (covalent) 12,15,18,52 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 22,42,45,48 predicted 59 complete MGYSVIVDSDKCIGCGECVDVCPVEVYELQNGKAVPVNEEECLGCESCIEVCPQNAIVE
FEDV3A S07149 30-Sep-1991 30-Sep-1991 18-Sep-1998
ferredoxin [3Fe-4S][4Fe-4S] III Desulfovibrio africanus Desulfovibrio africanus Bovier-Lapierre, G. Bruschi, M. Bonicel, J. Hatchikian, E.C. Biochim. Biophys. Acta 913198720-26 Amino-acid sequence of Desulfovibrio africanus ferredoxin III: a unique structural feature for accommodating iron-sulfur clusters. S07149 protein 1-61 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 4-59 binding-site 3Fe-4S cluster (Cys) (covalent) 11,17,51 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,41,44,47 predicted 61 complete GYKITIDTDKCTGDGECVDVCPVEVYELQDGKAVAVNEDECLGCESCVEVCEQDALTVEE N
A30024 A30024 A41412 08-Mar-1989 02-May-1994 18-Sep-1998
ferredoxin [3Fe-4S][4Fe-4S] I Desulfovibrio vulgaris Desulfovibrio vulgaris Okawara, N. Ogata, M. Yagi, T. Wakabayashi, S. Matsubara, H. J. Biochem. 1041988196-199 Amino acid sequence of ferredoxin I from Desulfovibrio vulgaris Miyazaki. MUID89034004 A30024 protein 1-61 strain Miyazaki Ogata, M. Kondo, S. Okawara, N. Yagi, T. J. Biochem. 1031988121-125 Purification and characterization of ferredoxin from Desulfovibrio vulgaris Miyazaki. MUID88198088 A41412 protein 1-15 Ferredoxin I mediates electron transfer between pyruvate dehydrogenase and the hydrogenase-cytochrome c3 system. Ferredoxin I has two distinguishable iron-sulfur clusters. ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer homodimer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 4-59 binding-site 3Fe-4S cluster (Cys) (covalent) 11,17,51 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,41,44,47 predicted 61 complete GWTVTVDTDKCTGDGECVDVCPVEVYELQDGKAVPVDEEECLGCESCVEVCEAGAITVEE N
FEMYFS A00219 30-Nov-1979 30-Nov-1979 18-Sep-1998
ferredoxin [3Fe-4S][4Fe-4S] Mycobacterium smegmatis Mycobacterium smegmatis Hase, T. Wakabayashi, S. Matsubara, H. Imai, T. Matsumoto, T. Tobari, J. FEBS Lett. 1031979224-228 Mycobacterium smegmatis ferredoxin: a unique distribution of cysteine residues constructing iron--sulfur clusters. MUID79236790 A00219 protein 1-106 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 1-57 binding-site 3Fe-4S cluster (Cys) (covalent) 8,16,49 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 20,39,42,45 predicted 106 complete TYVIAEPCVDVKDKACIEECPVDCIYEGARMLYIHPDECVDCGACEPVCPVEAIYYEDDV PDQWSSYAQANADFFAELGSPGGASKVGQTDNDPQAIKDLPPQGED
FEDVFG S48666 A90216 A00211 S17118 28-Feb-1980 19-Oct-1995 15-Sep-2000
ferredoxin [4Fe-4S] I [validated] ferredoxin [3Fe-4S] II Desulfovibrio gigas Desulfovibrio gigas Chen, B. Menon, N.K. Dervertarnian, L. Moura, J.J.G. Przybyla, A.E. FEBS Lett. 3511994401-404 Cloning, sequencing and overexpression of the Desulfovibrio gigas ferredoxin gene in E. coli. MUID94364513 S48666 DNA 1-59 tetrameric ferredoxin [3Fe-4S] II interconverts with dimeric ferredoxin [4Fe-4S] I Bruschi, M. Biochem. Biophys. Res. Commun. 911979623-628 Amino acid sequence of Desulfovibrio gigas ferredoxin: revisions. MUID80087755 A90216 protein 2-56,58-59 Kissinger, C.R. Sieker, L.C. Adman, E.T. Jensen, L.H. submitted to the Brookhaven Protein Data Bank April1991 PDB1FXD annotation X-ray crystallography, 1.7 angstroms, residues 2-56,'V',58-59 Kissinger, C.R. Sieker, L.C. Adman, E.T. Jensen, L.H. J. Mol. Biol. 2191991693-715 Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 A. MUID91278096 annotation X-ray crystallography, 1.7 angstroms evidence for residue 57, modeled as Val Travis, J. Newman, D.J. Legall, J. Peck Jr., H.D. Biochem. Biophys. Res. Commun. 451971452-458 The amino acid sequence of ferredoxin from the sulfate reducing bacterium, Desulfovibrio gigas. MUID72117540 annotation this sequence differs from that shown at a number of positions homotetramer ferredoxin [3Fe-4S] II; homodimer ferredoxin [4Fe-4S] I ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer homodimer homotetramer iron-sulfur protein metalloprotein product ferredoxin [4Fe-4S] I 2-59 experimental domain ferredoxin 2[4Fe-4S] homology 2-59 binding-site 3Fe-4S cluster (Cys) (covalent) 9,15,51 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,51 predicted modified-site cysteine derivative (Cys) (probably cysteine methyl disulfide) 12 experimental disulfide-bonds 19-43 experimental 59 complete MPIEVNDDCMACEACVEICPDVFEMNEEGDKAVVINPDSDLDCVEEAIDSCPAEAIIRS
FEDV2V S07154 30-Sep-1991 30-Sep-1991 18-Sep-1998
ferredoxin [4Fe-4S] II Desulfovibrio vulgaris Desulfovibrio vulgaris Okawara, N. Ogata, M. Yagi, T. Wakabayashi, S. Matsubara, H. Biochimie 7019881815-1820 Characterization and complete amino acid sequence of ferredoxin II from Desulfovibrio vulgaris Miyazaki. MUID89274328 S07154 protein 1-63 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer homodimer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 4-61 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,53 predicted 63 complete AKYLYLDQDECMACESCVELCPEAFRMSSAGEYAEVIDPNTTAECVEDAISTCPVECIEW REE
FEDV1A A56050 A00212 S50183 15-Oct-1982 12-May-1995 15-Sep-2000
ferredoxin [4Fe-4S] I [validated] Desulfovibrio africanus Desulfovibrio africanus Sery, A. Housset, D. Serre, L. Bonicel, J. Hatchikian, C. Frey, M. Roth, M. Biochemistry 33199415408-15417 Crystal structure of the ferredoxin I from Desulfovibrio africanus at 2.3 angstrom resolution. MUID95101634 A56050 protein 1-64 X-ray crystallography, 2.3 angstroms correction confirmed by protein sequencing Bruschi, M. Hatchikian, E.C. Biochimie 641982503-507 Non-heme iron proteins of Desulfovibrio: the primary structure of ferredoxin I from Desulfovibrio africanus. MUID83023363 A00212 protein 1-57,'S',59,'EE' strain Benghazi, NCIB 8401 Davy, S.L. Breton, J. Osborne, M.J. Thomson, A.J. Thurgood, A.P. Lian, L.Y. Petillot, Y. Hatchikian, C. Moore, G.R. Biochim. Biophys. Acta 1209199433-39 MCD and (1)H-NMR spectroscopic studies of Desulfovibrio africanus ferredoxin I: revised amino-acid sequence and identification of secondary structure. MUID95035051 S50183 protein 1-64 conformation by (1)H-NMR Frey, M. Roth, M. submitted to the Brookhaven Protein Data Bank November1994 PDB1FXR annotation X-ray crystallography, 2.3 angstroms, residues 1-64 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin [4Fe-4S] I 1-64 experimental domain ferredoxin 2[4Fe-4S] homology 4-62 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,54 experimental 64 complete ARKFYVDQDECIACESCVEIAPGAFAMDPEIEKAYVKDVEGASQEEVEEAMDTCPVQCIH WEDE
FEDV1V A25273 25-Oct-1987 27-Jan-1995 18-Sep-1998
ferredoxin [4Fe-4S] I Desulfovibrio desulfuricans Desulfovibrio desulfuricans Bruschi, M.H. Guerlesquin, F.A. Bovier-Lapierre, G.E. Bonicel, J.J. Couchoud, P.M. J. Biol. Chem. 26019858292-8296 Amino acid sequence of the [4Fe-4S] ferredoxin isolated from Desulfovibrio desulfuricans Norway. MUID85234535 A25273 protein 1-59 strain Norway ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 2-59 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,51 predicted 59 complete TIVIDHEECIGCESCVELCPEVFAMIDGEEKAMVTAPDSTAECAQDAIDACPVEAISKE
B44203 B44203 19-Feb-1999 19-Feb-1999 19-Feb-1999
ferredoxin [3Fe-4S] Thermococcus litoralis Thermococcus litoralis Howard, J.B. Park, J.B. Zhai, Z.H. Adams, M.W.W. unpublished results, cited by Busse, S.C., La Mar, G.N., Yu, L.P., Howard, J.B., Smith, E.T., Zhou, Z.H., Adams, M.W.W., Biochemistry 31, 11952-11962 1992 B44203 protein 1-59 Wang, P.L. Donaire, A. Zhou, Z.H. Adams, M.W.W. La Mar, G.N. Biochemistry 35199611319-11328 Molecular model of the solution structure for the paramagnetic four-iron ferredoxin from the hyperthermophilic archaeon Thermococcus litoralis. MUID96378623 annotation conformation by (1)H-NMR This ferredoxin can form a 4Fe-4S cluster but it readily converts to a stable 3Fe-4S cluster. ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin [3Fe-4S] 1-59 experimental product ferredoxin [4Fe-4S] 1-59 experimental domain ferredoxin 2[4Fe-4S] homology 3-59 binding-site 3Fe-4S cluster (Cys) (covalent) 10,16,51 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 10,13,16,51 experimental disulfide-bonds 20-43 experimental 59 complete MKVSVDKDACIGCGVCASICPDVFEMDDDGKAKALVAETDLECAKEAAESCPTGAITVE
FECLC A00205 15-Oct-1982 15-Oct-1982 18-Sep-1998
ferredoxin [4Fe-4S] Clostridium thermaceticum Clostridium thermaceticum Elliott, J.I. Yang, S.S. Ljungdahl, L.G. Travis, J. Reilly, C.F. Biochemistry 2119823294-3298 Complete amino acid sequence of the 4Fe-4S, thermostable ferredoxin from Clostridium thermoaceticum. MUID83000247 A00205 protein 1-63 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 3-63 binding-site 4Fe-4S cluster (Cys) (covalent) 10,13,16,55 predicted 63 complete MKVTVDQDLCIACGTCIDLCPSVFDWDDEGLSHVIVDEVPEGAEDSCARESVNECPTEAI KEV
FEBSFF A00214 07-May-1981 07-May-1981 18-Sep-1998
ferredoxin [4Fe-4S] Bacillus stearothermophilus Bacillus stearothermophilus Hase, T. Ohmiya, N. Matsubara, H. Mullinger, R.N. Rao, K.K. Hall, D.O. Biochem. J. 159197655-63 Amino acid sequence of four-iron-four-sulphur ferredoxin isolated from Bacillus stearothermophilus. MUID77065140 A00214 protein 1-81 ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein product ferredoxin [4Fe-4S] 1-81 experimental domain ferredoxin 2[4Fe-4S] homology 4-69 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,61 predicted 81 complete PKYTIVDKETCIACGACGAAAPDIYDYDEDGIAYVTLDDNQGIVEVPDILIDDMMDAFEG CPTESIKVADEPFDGDPNKFD
A55790 A55790 23-Mar-1995 23-Mar-1995 15-Sep-2000
ferredoxin [4Fe-4S] [validated] Bacillus "thermoproteolyticus" Bacillus "thermoproteolyticus" Fukuyama, K. Nagahara, Y. Tsukihara, T. Katsube, Y. Hase, T. Matsubara, H. J. Mol. Biol. 1991988183-193 Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin. Evolutionary implications for bacterial ferredoxins. MUID88172459 sequence X-ray crystallography, 2.3 angstroms A55790 protein 1-81 Fukuyama, K. Tsukihara, T. Katsube, Y. submitted to the Brookhaven Protein Data Bank February1990 PDB2FXB annotation X-ray crystallography, 2.3 angstroms, residues 1-81 Fukuyama, K. Matsubara, H. Tsukihara, T. Katsube, Y. J. Mol. Biol. 2101989383-398 Structure of [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus refined at 2.3 angstrom resolution. Structural comparisons of bacterial ferredoxins. MUID90096160 annotation X-ray crystallography, 2.3 angstroms ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 4-69 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,61 experimental 81 complete PKYTIVDKETCIACGACGAAAPDIYDYDEDGIAYVTLDDNQGIVEVPDILIDDMMDAFEG CPTDSIKVADEPFDGDPNKFE
FELVA S01527 A00224 30-Jun-1987 30-Jun-1987 11-Jun-1999
photosystem I iron-sulfur protein psaC photosystem I iron-sulfur protein frxA liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Kohchi, T. Shirai, H. Fukuzawa, H. Sano, T. Komano, T. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988353-372 Structure and organization of Marchantia polymorpha chloroplast genome. IV. Inverted repeat and small single copy regions. MUID89068688 S01527 not compared with conceptual translation DNA 1-81 GBX04465 GBY00686 NIDg11640 PIDNCAA28135.1 PIDg11724 Ohyama, K. submitted to the EMBL Data Library October1986 A00224 DNA 1-81 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features frxA chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid product photosystem I iron-sulfur protein psaC 2-81 predicted domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MAHAVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKANQIASAPRTEDCVGCKRCESRCPT DFLSVRVYLGNETTRSMGLSY
FERZA JQ0290 S05169 31-Mar-1990 31-Mar-1990 11-Jun-1999
photosystem I iron-sulfur protein psaC photosystem I protein C rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0290 DNA 1-81 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05169 nucleic acid sequence not shown translation not shown DNA 1-81 EMBLX15901 NIDg11957 PIDNCAA33954.1 PIDg12051 cv. Nihonbare psaC CP108265-108020 chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid product photosystem I iron-sulfur protein psaC 2-81 predicted domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPT DFLSVRVYLGPETTRSMALSY
FEWT1 S04034 JU0006 30-Sep-1991 30-Sep-1991 11-Jun-1999
photosystem I iron-sulfur protein psaC photosystem I 8K protein wheat chloroplast common wheat chloroplast Triticum aestivum Dunn, P.P.J. Gray, J.C. Plant Mol. Biol. 111988311-319 Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA. S04034 DNA 1-81 EMBLX13158 NIDg12349 PIDNCAA31555.1 PIDg12350 psaC chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid product photosystem I iron-sulfur protein psaC 2-81 predicted domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPT DFLSVRVYLGPETTRSMALSY
FEZM1C JU0008 30-Jun-1992 30-Jun-1992 11-Jun-1999
photosystem I iron-sulfur protein psaC maize chloroplast maize chloroplast Zea mays Schantz, R. Bogorad, L. Plant Mol. Biol. 111988239-247 Maize chloroplast genes ndhD, ndhE, and psaC. Sequences, transcripts and transcript pools. JU0008 DNA 1-81 GBX13159 NIDg12421 PIDNCAA31557.1 PIDg12423 psaC chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid product photosystem I iron-sulfur protein psaC 2-81 predicted domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MSHSVKIYDTCIGCTHCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPT DFLSVRVYLGPETTRSMALSY
FEPM1S S04033 S00319 JU0007 30-Sep-1991 30-Sep-1991 11-Jun-1999
photosystem I iron-sulfur protein psaC photosystem I 8K protein garden pea chloroplast garden pea chloroplast Pisum sativum Dunn, P.P.J. Gray, J.C. Plant Mol. Biol. 111988311-319 Localization and nucleotide sequence of the gene for the 8 kDa subunit of photosystem I in pea and wheat chloroplast DNA. S04033 DNA 1-81 EMBLX13157 NIDg12169 PIDNCAA31554.1 PIDg12170 Dunn, P.P.J. Packman, L.C. Pappin, D. Gray, J.C. FEBS Lett. 2281988157-161 N-terminal amino acid sequence analysis of the subunits of pea photosystem I. MUID88137587 S00319 protein 2-44,'X',46-47,'X',49,'XX',52 psaC chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid product photosystem I iron-sulfur protein psaC 2-81 experimental domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWGGCKAKQIASAPRTEDCVGCKRCESACPT DFLSVRVYLWHETTRSMGLAY
FEAI1C S20851 S18052 31-Mar-1992 31-Mar-1992 11-Jun-1999
photosystem I iron-sulfur protein psaC photosystem I 9K protein photosystem I apoprotein FA/FB Anabaena sp. (strain PCC 7120) Anabaena sp. Mulligan, M.E. Jackman, D.M. Plant Mol. Biol. 181992803-808 Nucleotide sequence and expression of the gene for the 9 kDa F(A)/F(B) component of photosystem I from the cyanobacterium Anabaena sp. PCC7120. MUID92216058 S20851 DNA 1-81 EMBLX61369 NIDg39046 PIDNCAA43645.1 PIDg39047 psaC ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S duplication electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MSHTVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAAQVASSPRTEDCVGCKRCETACPT DFLSIRVYLGAETTRSMGLAY
FEAICV S14475 31-Dec-1992 31-Dec-1992 11-Jun-1999
photosystem I iron-sulfur protein psaC photosystem I apoprotein FA/FB Anabaena variabilis Anabaena variabilis Mannan, M.R. Pakrasi, H.B. submitted to the EMBL Data Library January1991 S14475 DNA 1-81 EMBLX57153 NIDg39044 PIDNCAA40443.1 PIDg39045 psaC ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S duplication electron transfer iron-sulfur protein membrane-associated complex metalloprotein photosynthesis photosystem I thylakoid domain ferredoxin 2[4Fe-4S] homology 4-66 binding-site 4Fe-4S cluster (Cys) (covalent) 11,14,17,58 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 21,48,51,54 predicted 81 complete MSHTVKIYDTCIGCTQCVRACPTDVLEMVPWDGCKAAQVASSPRTEDCVGCKRCETACPT DFLSIRVYLGAETTRSMGLAY
FENTB A00225 S11956 30-Jun-1987 30-Jun-1987 18-Sep-1998
ferredoxin 2[4Fe-4S] frxB common tobacco chloroplast common tobacco chloroplast Nicotiana tabacum Sugiura, M. submitted to the EMBL Data Library August1986 A00225 DNA 1-167 cv. Bright Yellow 4 Shinozaki, K. Ohme, M. Tanaka, M. Wakasugi, T. Hayashida, N. Matsubayashi, T. Zaita, N. Chunwongse, J. Obokata, J. Yamaguchi-Shinozaki, K. Ohto, C. Torazawa, K. Meng, B.Y. Sugita, M. Deno, H. Kamogashira, T. Yamada, K. Kusuda, J. Takaiwa, F. Kato, A. Tohdoh, N. Shimada, H. Sugiura, M. EMBO J. 519862043-2049 The complete nucleotide sequence of the tobacco chloroplast genome: its gene organization and expression. annotation gene organization, sites, features Lin, C.H. Wu, M. Plant Mol. Biol. 151990449-455 A ferredoxin-type iron-sulfur protein gene, frx B, is expressed in the chloroplasts of tobacco and spinach. MUID91355892 S11956 DNA 1-167 frxB chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 57-122 binding-site 4Fe-4S cluster (Cys) (covalent) 64,67,70,114 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 74,104,107,110 predicted 167 complete MLPMITEFINYGQQTIRAARYIGQGFMITLSHANRLPVTIQYPYEKLITSERFRGRIHFE FDKCIACEVCVRVCPIDLPVVDWKLETDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLS MTEEYELSTYDRHELNYNQIALGRLPMSVIDDYTIRTISNLPQIKNE
FELVB S01524 A00226 30-Jun-1987 30-Jun-1987 11-Jun-1999
ferredoxin 2[4Fe-4S] frxB liverwort (Marchantia polymorpha) chloroplast chloroplast Marchantia polymorpha Kohchi, T. Shirai, H. Fukuzawa, H. Sano, T. Komano, T. Umesono, K. Inokuchi, H. Ozeki, H. Ohyama, K. J. Mol. Biol. 2031988353-372 Structure and organization of Marchantia polymorpha chloroplast genome. IV. Inverted repeat and small single copy regions. MUID89068688 S01524 DNA 1-183 GBX04465 GBY00686 NIDg11640 PIDNCAA28138.1 PIDg11727 Ohyama, K. Fukuzawa, H. Kohchi, T. Shirai, H. Sano, T. Sano, S. Umesono, K. Shiki, Y. Takeuchi, M. Chang, Z. Aota, S. Inokuchi, H. Ozeki, H. Nature 3221986572-574 Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. annotation gene organization, sites, features frxB chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 57-122 binding-site 4Fe-4S cluster (Cys) (covalent) 64,67,70,114 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 74,104,107,110 predicted 183 complete MFSIINGLKNYNQQAIQAARYIGQGFLVTLDHMNRLPTTIQYPYEKLIPSERFRGRIHFE FDKCIACEVCVRVCPINLPVVDWELKKTIKKKQLKNYSIDFGVCIFCGNCVEYCPTNCLS MTEEYELSTYNRHELNYDQIALGRLPISIIEDSTIENIFNLTSLPKGKIEGHIYSRNITN IVN
FERZB JQ0294 S05172 31-Mar-1990 31-Mar-1990 11-Jun-1999
ferredoxin 2[4Fe-4S] frxB rice chloroplast rice chloroplast Oryza sativa Shimada, H. Whittier, R.F. Hiratsuka, J. Maeda, Y. Hirai, A. Sugiura, M. submitted to JIPID December1989 JQ0294 DNA 1-178 cv. Nihonbare Hiratsuka, J. Shimada, H. Whittier, R. Ishibashi, T. Sakamoto, M. Mori, M. Kondo, C. Honji, Y. Sun, C.R. Meng, B.Y. Li, Y.Q. Kanno, A. Nishizawa, Y. Hirai, A. Shinozaki, K. Sugiura, M. Mol. Gen. Genet. 2171989185-194 The complete sequence of the rice (Oryza sativa) chloroplast genome: intermolecular recombination between distinct tRNA genes accounts for a major plastid DNA inversion during the evolution of the cereals. MUID89364698 S05172 nucleic acid sequence not shown translation not shown DNA 1-178 EMBLX15901 NIDg11957 PIDNCAA33909.1 PIDg12054 cv. Nihonbare frxB rps15 CP110536-110000 chloroplast ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S chloroplast electron transfer iron-sulfur protein metalloprotein product ferredoxin 2[4Fe-4S] frxB 2-178 predicted domain ferredoxin 2[4Fe-4S] homology 55-120 binding-site 4Fe-4S cluster (Cys) (covalent) 62,65,68,112 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 72,102,105,108 predicted 178 complete MFPMVTGFMGQQTIRAARYIGQSFIITLSHTNRLPITIHYPYEKSITSERFRGRIHFEFD KCIACEVCVRVCPIDLPLVDWRFEKDIKRKQLLNYSIDFGVCIFCGNCVEYCPTNCLSMT EEYELSTYDRHELNYNQIALSRLPISIMGDYTIQTIRNSTQSKIDEEKSWNSRTITDY
FEYBQI S27973 S34479 S76037 S18047 31-Mar-1992 31-Mar-1992 16-Jun-2000
NADH dehydrogenase (ubiquinone) (EC 1.6.5.3) chain ndhI ferredoxin 2[4Fe-4S] Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Ellersiek, U. Steinmueller, K. Plant Mol. Biol. 2019921097-1110 Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803. MUID93099260 S27973 DNA 1-193 EMBLX62517 NIDg47554 PIDNCAA44375.1 PIDg47556 Berger, S. Ellersiek, U. Kinzelt, D. Steinmueller, K. FEBS Lett. 3261993246-250 Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803. MUID93314795 S34479 preliminary protein 1-25 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S76037 preliminary DNA 1-193 EMBLD64006 GBAB001339 NIDg1001291 PIDNBAA10884.1 PIDg1001394 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 ndhI ferredoxin 2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S electron transfer iron-sulfur protein metalloprotein NAD oxidoreductase domain ferredoxin 2[4Fe-4S] homology 58-123 binding-site 4Fe-4S cluster (Cys) (covalent) 65,68,71,115 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 75,105,108,111 predicted 193 complete MFNNILKQVGDYAKESLQAAKYIGQGLAVTFDHMSRRPITVQYPYEKLIPSERFRGRIHF EFDKCIACEVCVRVCPINLPVVDWEFNKAVKKKELKHYSIDFGVCIFCGNCVEYCPTNCL SMTEEYELAAYDRHDLNYDNVALGRLPYKVTEDPMVTPLRELGYLPKGVIEPHNLPKGSQ RAGQHPEDLVKAE
FEUC A00223 S63479 28-Aug-1985 11-Jun-1999 20-Apr-2000
ferredoxin [3Fe-4S][4Fe-4S], zinc-containing [validated] Sulfolobus acidocaldarius (strain DSM 639) Sulfolobus acidocaldarius DSM 639 Minami, Y. Wakabayashi, S. Wada, K. Matsubara, H. Kerscher, L. Oesterhelt, D. J. Biochem. 971985745-753 Amino acid sequence of a ferredoxin from thermoacidophilic archaebacterium, Sulfolobus acidocaldarius. Presence of an N(6)-monomethyllysine and phyletic consideration of archaebacteria. MUID85261163 A00223 protein 1-8,'H',10-15,'S',17-103 Breton, J.L. Duff, J.L.C. Butt, J.N. Armstrong, F.A. George, S.J. Petillot, Y. Forest, E. Schaefer, G. Thomson, A.J. Eur. J. Biochem. 2331995937-946 Identification of the iron-sulfur clusters in a ferredoxin from the archaeon Sulfolobus acidocaldarius: evidence for a reduced [3Fe-4S] cluster with pH-dependent electronic properties. MUID96085161 S63479 protein 1-30 DSM 639 Originally thought to have 2 4Fe-4S clusters, this ferredoxin has been shown to be of the [3Fe-4S][4Fe-4S] type. Sulfolobus zinc-containing ferredoxin ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S duplication electron transfer iron-sulfur protein metalloprotein methylated amino acid zinc domain ferredoxin 2[4Fe-4S] homology 38-101 binding-site zinc (His, His, His, Asp) 16,19,34,76 predicted modified-site N6-methyllysine (Lys) 29 experimental binding-site 3Fe-4S cluster (Cys) (covalent) 45,51,93 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 55,83,86,89 predicted 103 complete GIDPNYRTSKPVVGDHSGHKIYGPVESPKVLGVHGTIVGVDFDLCIADGSCITACPVNVF QWYETPGHPASEKKADPVNQQACIFCMACVNVCPVAAIDVKPP
JC4907 JC4907 S78038 PC2290 04-Feb-2000 04-Feb-2000 23-Mar-2001
ferredoxin [3Fe-4S][4Fe-4S], zinc-containing, precursor [validated] Sulfolobus sp. (strain 7) Sulfolobus sp. strain 7 Wakagi, T. Fujii, T. Oshima, T. Biochem. Biophys. Res. Commun. 2251996489-493 Molecular cloning, sequencing, and heterologous expression of a novel zinc-containing ferredoxin gene from a thermoacidophilic Archaeon Sulfolobus sp. strain 7. MUID96354813 JC4907 DNA 1-104 GBD78179 NIDg2467370 strain 7 S78038 protein 2-5,'Q',7-39;64-65,'N',67-70,'A',72-75,'A',77-82,'P',84-87 strain 7 Iwasaki, T. Fujii, T. Wakagi, T. Oshima, T. Biochem. Biophys. Res. Commun. 2061995563-569 Alternative form of the dicluster ferredoxin from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. MUID95126955 PC2290 protein 2-25,'L',27-31 Iwasaki, T. Wakagi, T. Isogai, Y. Tanaka, K. Iizuka, T. Oshima, T. J. Biol. Chem. 269199429444-29450 Functional and evolutionary implications of a [3Fe-4S] cluster of the dicluster-type ferredoxin from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. MUID95050783 annotation reclassification of source species characterization of iron-sulfur clusters Fujii, T. Hata, Y. Moriyama, H. Wakagi, T. Tanaka, N. Oshima, T. submitted to the Brookhaven Protein Data Bank August1996 PDB1XER annotation X-ray crystallography, 2.0 angstroms, residues 2-104 Fujii, T. Hata, Y. Wakagi, T. Tanaka, N. Oshima, T. Nat. Struct. Biol. 31996834-837 Novel zinc-binding centre in thermoacidophilic archaeal ferredoxins. MUID96433069 annotation X-ray crystallography, 2.0 angstroms Sulfolobus zinc-containing ferredoxin ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein methylated amino acid zinc product ferredoxin 2-103 experimental domain ferredoxin 2[4Fe-4S] homology 39-102 binding-site zinc (His, His, His, Asp) 17,20,35,77 experimental modified-site N6-methyllysine (Lys) 30 experimental binding-site 3Fe-4S cluster (Cys) (covalent) 46,52,94 experimental binding-site 3Fe-4S cluster (Cys) (covalent) 56,84,90 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 56,84,87,90 predicted 104 complete MGIDPNYRTNRQVVGEHSGHKVYGPVEPPKVLGIHGTIVGVDFDLCIADGSCINACPVNV FQWYDTPGHPASEKKADPVNEQACIFCMACVNVCPVAAIDVKPP
FEYTA T37333 A00222 19-Feb-1984 04-Feb-2000 16-Jun-2000
ferredoxin [3Fe-4S][4Fe-4S], zinc-containing [validated] Thermoplasma acidophilum Thermoplasma acidophilum Cosper, N.J. Stalhandske, C.M.V. Iwasaki, H. Oshima, T. Scott, R.A. Iwasaki, T. J. Biol. Chem. 274199923160-23168 Structural conservation of the isolated zinc site in archaeal zinc-containing ferredoxins as revealed by X-ray absorption spectroscopic analysis and its evolutionary implications. MUID99367440 T37333 translated from GB/EMBL/DDBJ DNA 1-143 EMBLAB023294 NIDg5689050 PIDNBAA82797.1 PIDg5689051 strain HO-62 Wakabayashi, S. Fujimoto, N. Wada, K. Matsubara, H. Kerscher, L. Oesterhelt, D. FEBS Lett. 162198321-24 Amino acid sequence of a ferredoxin from thermoacidophilic archaebacteria, Thermoplasma acidophilum. A00222 protein 2-101,'Q',103-105,'E',107-143 strain DSM 1728 the authors believe this ferredoxin has two 4Fe-4S clusters Iwasaki, T. Suzuki, T. Kon, T. Imai, T. Urushiyama, A. Ohmori, D. Oshima, T. J. Biol. Chem. 27219973453-3458 Novel zinc-containing ferredoxin family in thermoacidophilic archaea. MUID97166191 annotation metal binding sites the protein is shown to have one zinc, one 3Fe-4S cluster and one 4Fe-4S cluster For the structure of a closely related sequence with [3Fe-4S][4Fe-4S] clusters, see PIR:JC4907. zfx Sulfolobus zinc-containing ferredoxin ferredoxin 2[4Fe-4S] homology 3Fe-4S 4Fe-4S electron transfer iron-sulfur protein metalloprotein zinc product ferredoxin [3Fe-4S][4Fe-4S] 2-143 experimental domain ferredoxin 2[4Fe-4S] homology 62-142 binding-site zinc (His, His, His, Asp) 31,34,58,117 experimental binding-site 3Fe-4S cluster (Cys) (covalent) 69,75,134 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 79,124,127,130 experimental 143 complete MVKLEELDFKPKPIDEHFLENDKDYPVTGQHNGHDVRAEGMQRLDADGKPYPTKLGIHGT HVAVDWDCCIADGACMDVCPVNLYEWNLNPGKSGTGNDHKIEKGSAEWNKYRTDKCDPVR ESDCIFCMACESVCPVRAIKITP
C37777 C37777 10-Sep-1999 10-Sep-1999 10-Sep-1999
polyferredoxin 6x2[4Fe-4S] Methanothermus fervidus Methanothermus fervidus Steigerwald, V.J. Beckler, G.S. Reeve, J.N. J. Bacteriol. 17219904715-4718 Conservation of hydrogenase and polyferredoxin structures in the hyperthermophilic archaebacterium Methanothermus fervidus. MUID90330590 C37777 preliminary DNA 1-412 GBM34016 NIDg149803 PIDNAAA72833.1 PIDg149806 polyferredoxin 6x2[4Fe-4S] ferredoxin 2[4Fe-4S] homology electron transfer domain ferredoxin 2[4Fe-4S] homology 2-55 domain ferredoxin 2[4Fe-4S] homology 68-125 domain ferredoxin 2[4Fe-4S] homology 139-195 domain ferredoxin 2[4Fe-4S] homology 209-263 domain ferredoxin 2[4Fe-4S] homology 277-342 domain ferredoxin 2[4Fe-4S] homology 358-412 412 complete MIVINKEDCIRCGACQGVCPTGAISVKPEDVIYCDMCGGEPKCVEACPNDALRHEDITLE GGIKKKKITYSPEKCDKCGECVKVCPPGILKLVNDGKASRVPLEGFCVLCQQCVNVCPIE VIGIEGVKEPARVEIKIDKPIYIVDCVGCGLCVPECPVNAITLPKYGESIEIDEEKCIKC GICAQTCPWNSVYISGKKPQKSSRTIENFTLDKEECIGCNTCVEICPGGFIEPKSDLTVS LPEICPACGLCEKLCPTDAIELEVKLGPAKPVTEEGIVYNDENCKFCGRCALNCPNEAIR VVSPKGRVFPGLKKVDEKESYTICTTCGACTTVCPTGALKLVEVSKKVNGETVKRNRIQY NPSLCDKCGNCVDVCPYGILKLTDDEKLPVKGFCILCEKCIDACRFNALLIK
G30315 G30315 H69017 S20413 10-Sep-1999 10-Sep-1999 10-Sep-1999
polyferredoxin 6x2[4Fe-4S] mvhB Methanobacterium thermoautotrophicum (strains Delta H and Marburg) Methanobacterium thermoautotrophicum Reeve, J.N. Beckler, G.S. Cram, D.S. Hamilton, P.T. Brown, J.W. Krzycki, J.A. Kolodziej, A.F. Alex, L. Orme-Johnson, W.H. Walsh, C.T. Proc. Natl. Acad. Sci. U.S.A. 8619893031-3035 A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain delta-H encodes a polyferredoxin. MUID89240669 G30315 DNA 1-388,'A',390-412 GBJ04540 NIDg149730 strain Delta H the sequence is revised in GenBank entry MBFMVRH, release 109.0, (PID:g149734) Smith, D.R. Doucette-Stamm, L.A. Deloughery, C. Lee, H. Dubois, J. Aldredge, T. Bashirzadeh, R. Blakely, D. Cook, R. Gilbert, K. Harrison, D. Hoang, L. Keagle, P. Lumm, W. Pothier, B. Qiu, D. Spadafora, R. Vicaire, R. Wang, Y. Wierzbowski, J. Gibson, R. Jiwani, N. Caruso, A. Bush, D. Safer, H. Patwell, D. Prabhakar, S. McDougall, S. Shimer, G. Goyal, A. Pietrokovski, S. Church, G.M. Daniels, C.J. Mao, J. Rice, P. Noelling, J. Reeve, J.N. J. Bacteriol. 17919977135-7155 Complete genome sequence of Methanobacterium thermoautotrophicum Delta H: functional analysis and comparative genomics. MUID98037514 H69017 nucleic acid sequence not shown translation not shown DNA 1-95,'G',97-412 GBAE000883 GBAE000666 NIDg2622231 PIDNAAB85622.1 PIDg2622237 strain Delta H Hedderich, R. Albracht, S.P.J. Linder, D. Koch, J. Thauer, R.K. FEBS Lett. 298199265-68 Isolation and characterization of polyferredoxin from Methanobacterium thermoautotrophicum. The mvhB gene product of the methylviologen-reducing hydrogenase operon. MUID92183831 S20413 protein 1-2,'V',4-28 PIDNAAB21772.1 PIDg247131 strain Marburg, DSM 2133 mvhB MTH1133 polyferredoxin 6x2[4Fe-4S] ferredoxin 2[4Fe-4S] homology 4Fe-4S iron-sulfur protein metalloprotein domain ferredoxin 2[4Fe-4S] homology 2-55 domain ferredoxin 2[4Fe-4S] homology 69-125 domain ferredoxin 2[4Fe-4S] homology 139-195 domain ferredoxin 2[4Fe-4S] homology 209-264 domain ferredoxin 2[4Fe-4S] homology 278-343 domain ferredoxin 2[4Fe-4S] homology 359-412 binding-site 4Fe-4S cluster (Cys) (covalent) 9,12,15,47 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 19,34,37,43 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 76,79,82,117 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 86,107,110,113 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 146,149,152,187 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 156,177,180,183 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 216,219,222,256 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 226,246,249,252 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 285,291,335 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 295,325,328,331 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 366,369,372,404 predicted binding-site 4Fe-4S cluster (Cys) (covalent) 376,394,397,400 predicted 412 complete MIIVNKEDCIRCGACQGTCPTAAIEVTPEDVIYCDICGGEPKCVDICPTGALKLEDLVVD EAGNTQGRIVFNPDKCNECGDCVEVCPPQILKLDEAKVKKVPLQGFCVMCQKCVDICPVG VIGVEGIKEPAKVELEIEGPIFIADCVGCGMCVPECPVDAITLDKVGGVIEIDEDTCIKC GVCAQTCPWNAVYISGRKPEKRAKEIKKFELDEDACIGCNTCVEACPGDFIVPRTSNLTV ELPAICTACGLCEQLCPVDAIDLEVELGPAKPASEEGLVWDEEKCDFIGACANICPNDAI RVVTKEGMKVPDNEKVDEEPSFAMCTRCGACTVACPKGALSLVDMDKVVDGEVVKRKRVQ YNPALCDQCGDCIEACPYDMLKLTDEKVPLKGFCILCDQCIPACPKGALSLK
S24802 S24802 10-Sep-1999 18-Aug-2000 19-Jan-2001
polyferredoxin 6x2[4Fe-4S] vhuB [similarity] Methanococcus voltae Methanococcus voltae Halboth, S. Klein, A. submitted to the EMBL Data Library August1991 Methanococcus voltae harbors two gene groups each of homologous (NiFe)- and (NiFeSe)- hydrogenases which reduce cofactor F420 or only electron accepting dyes. S24802 DNA 1-398 EMBLX61204 NIDg1747406 PIDNCAA43512.1 PIDg1747410 strain PS(DSM1537) Halboth, S. Klein, A. Mol. Gen. Genet. 2331992217-224 Methanococcus voltae harbors four gene clusters potentially encoding two [NiFe] and two [NiFeSe] hydrogenases, each of the cofactor F420-reducing or F420-non-reducing types. MUID92293118 annotation vhuB polyferredoxin 6x2[4Fe-4S] ferredoxin 2[4Fe-4S] homology domain ferredoxin 2[4Fe-4S] homology 4-52 domain ferredoxin 2[4Fe-4S] homology 56-109 domain ferredoxin 2[4Fe-4S] homology 125-179 domain ferredoxin 2[4Fe-4S] homology 192-247 domain ferredoxin 2[4Fe-4S] homology 261-329 domain ferredoxin 2[4Fe-4S] homology 341-395 398 complete MAGIKIQEDACLVCNACSKACPTEAIEIAPFKTCTLCFSCASACPTGALVENNGKLIYNS SKCIKCGNCATACPTGIKKVDDRFPYSKGHCVLCEKCVDACPIDIISIPGKIDKPEREVT IPQEPIKVTEACVGCSECVPVCPVDAISIEDELAVIDTEKCIYCSVCAQTCPWNAIYVAG KKPSKRQKEIKSFTVTEECIGCEKCVEVCPGDMITYNREDLIVKLPEACPACHLCEQNCP VDAISLEVEYGSAKPVTEEGLVWYEDKCNYCGPCAIKCPLCPTNAINMINQKGLALPSRT KTDKDPEFRMCIRCGACVMKCPTGALKMGKITHEGKEYNRIEFSPALCNECGECVDVCPQ DTLKLTGDEKKPLEGYCILCLKCIEACAKTKRNALGLQ
IHKREV A92330 A92143 A00263 24-Apr-1984 24-Oct-1997 15-Sep-2000
high potential iron-sulfur protein [validated] HiPIP Chromatium vinosum Chromatium vinosum Tedro, S.M. Meyer, T.E. Bartsch, R.G. Kamen, M.D. J. Biol. Chem. 2561981731-735 Primary structures of high potential, four-iron-sulfur ferredoxins from the purple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and Chromatium gracile. MUID81094036 A92330 protein 1-73,'D',75-85 Dus, K. Tedro, S. Bartsch, R.G. J. Biol. Chem. 24819737318-7331 The complete amino acid sequence of Chromatium high potential iron sulfur protein. MUID74012043 A92143 protein 1-10,'N',12-44,'D',46-85 strain D Banci, L. Bertini, I. Dikiy, A. Kastrau, D.H.W. Luchinat, C. Sompornpisut, P. submitted to the Brookhaven Protein Data Bank January1995 PDB1HRQ annotation conformation by (1)H-NMR, reduced form, residues 1-85 Bertini, I. Dikiy, A. Kastrau, D.H.W. Luchinat, C. Sompornpisut, P. submitted to the Brookhaven Protein Data Bank December1995 PDB1NEH annotation conformation by (1)H-NMR, oxidized form, residues 1-85 Backes, G. Mino, Y. Loehr, T.M. Meyer, T.E. Cusanovich, M.A. Sweeney, W.V. Adman, E.T. Sanders-Loehr, J. J. Am. Chem. Soc. 11319912055-2064 The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy. annotation X-ray crystallography, 2.0 angstroms assignment of Raman spectra frequencies and hydrogen bonds around the iron-sulfur cluster Carter Jr., C.W. Kraut, J. Freer, S.T. Xuong, N.H. Alden, R.A. Bartsch, R.G. J. Biol. Chem. 24919744212-4225 Two-angstrom crystal structure of oxidized Chromatium high potential iron protein. MUID74309824 annotation X-ray crystallography, 2.0 angstroms Carter Jr., C.W. Kraut, J. Freer, S.T. Alden, R.A. J. Biol. Chem. 24919746339-6346 Comparison of oxidation-reduction site geometries in oxidized and reduced Chromatium high potential iron protein and oxidized Peptococcus aerogenes ferredoxin. MUID75019502 annotation X-ray crystallography structures of the oxidized and reduced forms are compared with each other and with oxidized bacterial ferredoxin high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 43,46,63,77 experimental 85 complete SAPANAVAADDATAIALKYNQDATKSERVAAARPGLPPEEQHCANCQFMQADAAGATDEW KGCQLFPGKLINVNGWCASWTLKAG
IHTFER A00264 31-Mar-1981 31-Mar-1981 31-Mar-2000
high potential iron-sulfur protein Thiocapsa roseopersicina Thiocapsa roseopersicina Tedro, S.M. Meyer, T.E. Bartsch, R.G. Kamen, M.D. J. Biol. Chem. 2561981731-735 Primary structures of high potential, four-iron-sulfur ferredoxins from the purple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and Chromatium gracile. MUID81094036 A00264 protein 1-85 high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 43,46,63,77 predicted 85 complete tentative EAPANAVAANDPTAVALK.YNADATK.SDR.LAAAR.PGLPPAEQHC.ANC.QFHLDDVA GATEEWHGC.SLFPGK.LINVDGWC.ASWTLK.AG
IHKREG A00265 31-Mar-1981 31-Mar-1981 31-Mar-2000
high potential iron-sulfur protein Chromatium gracile Chromatium gracile Tedro, S.M. Meyer, T.E. Bartsch, R.G. Kamen, M.D. J. Biol. Chem. 2561981731-735 Primary structures of high potential, four-iron-sulfur ferredoxins from the purple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and Chromatium gracile. MUID81094036 A00265 protein 1-83 high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 43,46,61,75 predicted 83 complete tentative EVPANAVTESDPTAVALK.YHR.NAEASER.VAAAR.PGLPPEEQHCENC.QFMLPDQGA DEWR.GC.SLFPGK.LINLDGWC.ASWTLR.AG
IHTF A00266 07-May-1981 07-May-1981 18-Sep-1998
high potential iron-sulfur protein Thiocapsa pfennigii Thiocapsa pfennigii Tedro, S.M. Meyer, T.E. Kamen, M.D. J. Biol. Chem. 24919741182-1188 Primary structure of a high potential iron-sulfur protein from the photosynthetic bacterium Thiocapsa pfennigii. MUID74107423 A00266 protein 1-81 strain KIMG 8816 high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 43,46,59,73 predicted 81 complete EDLPHVDAATNPIAQSLHYIEDANASERNPVTKTELPGSEQFCHNCSFIQADSGAWRPCT LYPGYTVSEDGWCLSWAHKTA
IHPC A00267 31-May-1979 23-Oct-1981 18-Sep-1998
high potential iron-sulfur protein Paracoccus sp. Paracoccus sp. Tedro, S.M. Meyer, T.E. Kamen, M.D. J. Biol. Chem. 25219777826-7833 Primary structure of a high potential iron-sulfur protein from a moderately halophilic denitrifying coccus. MUID78026535 A00267 protein 1-71 ATCC 12084 Paracoccus sp. is a halotolerant species isolated from decaying whale meat. high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein pyroglutamic acid modified-site pyrrolidone carboxylic acid (Gln) 1 experimental binding-site 4Fe-4S cluster (Cys) (covalent) 37,40,50,64 predicted 71 complete QDLPPLDPSAEQAQALNYVKDTAEAADHPAHQEGEQCDNCMFFQADSQGCQLFPQNSVEP AGWCQSWTAQN
IHRFG A00268 13-Jul-1981 13-Jul-1981 18-Sep-1998
high potential iron-sulfur protein Rhodocyclus gelatinosus Rhodocyclus gelatinosus Tedro, S.M. Meyer, T.E. Kamen, M.D. J. Biol. Chem. 2511976129-136 Primary structure of a high potential iron-sulfur protein from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas gelatinosa. MUID76069285 A00268 protein 1-74 strain C.B. van Niel ATH 2.2.1, ATCC 17011 high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 36,39,53,67 predicted 74 complete APVDEKNPQAVALGYVSDAAKADKAKYKQFVAGSHCGNCALFQGKATDAVGGCPLFAGKQ VANKGWCSAWAKKA
IHQFT A00269 30-Jun-1979 30-Jun-1979 18-Sep-1998
high potential iron-sulfur protein Rhodocyclus tenuis Rhodocyclus tenuis Tedro, S.M. Meyer, T.E. Kamen, M.D. J. Biol. Chem. 25419791495-1500 Primary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue. MUID79109745 A00269 protein 1-63 strain 3761 the identities of Asp-47 and Gln-49 are tentative high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 23,26,41,56 predicted 63 complete GTNASMRKAFNYQEVSKTAGKNCANCAQFIPGASASAAGACKVIPGDSQIQPTGYCDAYI VKK
IHER1 S48703 A00270 04-Dec-1986 10-Oct-1997 15-Sep-2000
high potential iron-sulfur protein 1 [validated] high-redox-potential ferredoxin I HiPIP Ectothiorhodospira halophila Ectothiorhodospira halophila Bertini, I. Felli, I.C. Kastrau, D.H.W. Luchinat, C. Piccioli, M. Viezzoli, M.S. Eur. J. Biochem. 2251994703-714 Sequence-specific assignment of the (1)H and (15)N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila. MUID95045521 S48703 protein 'AS',1-33;35-71 sequenced by (1)H and (15)N NMR modified sequence expressed in E. coli Tedro, S.M. Meyer, T.E. Kamen, M.D. Arch. Biochem. Biophys. 2411985656-664 Amino acid sequence of high-redox-potential ferrodoxin (HiPIP) isozymes from the extremely halophilic purple phototrophic bacterium, Ectothiorhodospira halophila. MUID85305760 A00270 protein 1-18,'PSHG',24-71 Breiter, D.R. Meyer, T.E. Rayment, I. Holden, H.M. submitted to the Brookhaven Protein Data Bank June1991 PDB2HIP annotation X-ray crystallography, 2.5 angstroms, residues 1-71 Breiter, D.R. Meyer, T.E. Rayment, I. Holden, H.M. J. Biol. Chem. 266199118660-18667 The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-Angstrom resolution. MUID92011624 annotation X-ray crystallography, 2.5 angstroms sequence revision sequence correction peptide sequencing not performed high reduction potential electron transfer high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 31,34,48,64 predicted 71 complete EPRAEDGHAHDYVNEAADASGHPRYQEGQLCENCAFWGEAVQDGWGRCTHPDFDEVLVKA EGWCSVYAPAS
IHER2 A00271 04-Dec-1986 04-Dec-1986 18-Sep-1998
high potential iron-sulfur protein II high-redox-potential ferredoxin 2 HiPIP Ectothiorhodospira halophila Ectothiorhodospira halophila Tedro, S.M. Meyer, T.E. Kamen, M.D. Arch. Biochem. Biophys. 2411985656-664 Amino acid sequence of high-redox-potential ferrodoxin (HiPIP) isozymes from the extremely halophilic purple phototrophic bacterium, Ectothiorhodospira halophila. MUID85305760 A00271 protein 1-76 The high potential iron-sulfur protein (HiPIP) are a class of high-redox-potential 4Fe-4S proteins distinct from ferrdoxins. They function in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. In E. halophila, an extremely halophilic, purple, sulfur, photosynthetic bacterium, two HiPIP forms are found. high potential iron-sulfur protein 4Fe-4S electron transfer iron-sulfur protein metalloprotein binding-site 4Fe-4S cluster (Cys) (covalent) 38,41,54,70 predicted 76 complete GLPDGVEDLPKAEDDHAHDYVNDAADTDHARFQEGQLCENCQFWVDYVNGWGYCQHPDFT DVLVRGEGWCSVYAPA
RUPE A00272 13-Jul-1981 13-Jul-1981 24-Oct-1997
rubredoxin Peptostreptococcus asaccharolyticus Peptostreptococcus asaccharolyticus Bachmayer, H. Benson, A.M. Yasunobu, K.T. Garrard, W.T. Whiteley, H.R. Biochemistry 71968986-996 Nonheme iron proteins. IV. Structural studies of Micrococcus aerogenes rubredoxin. MUID68311179 A00272 protein 1-53 the source was designated as Peptococcus aerogenes rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-48 binding-site iron (Cys) 6,9,38,41 predicted 53 complete MQKFECTLCGYIYDPALVGPDTPDQDGAFEDVSENWVCPLCGAGKEDFEVYED
RUCLEP S29120 A00273 24-Apr-1984 19-May-1995 15-Sep-2000
rubredoxin [validated] Clostridium pasteurianum Clostridium pasteurianum Mathieu, I. Meyer, J. Moulis, J.M. Biochem. J. 2851992255-262 Cloning, sequencing and expression in Escherichia coli of the rubredoxin gene from Clostridium pasteurianum. MUID92344580 S29120 DNA 1-54 EMBLM60116 NIDg144905 PIDNAAA23279.1 PIDg144909 the amidation states of residues 14, 22, and 48 were confirmed by protein sequencing of the protein from Clostridium pasteurianum the amino end of the mature protein from Clostridium pasteurianum is blocked, but that expressed by Escherichia coli is not McCarthy, K.F. Ph.D. thesis, George Washington University 1972 The primary structure of Clostridium pasteurianum rubredoxin. A00273 protein 1-13,'D',15-21,'D',23-47,'E',49-54 peptides for which chemical overlaps were not determined were positioned on the basis of X-ray crystallographic data Dauter, Z. Wilson, K.S. Sieker, L.C. Moulis, J.M. Meyer, J. submitted to the Brookhaven Protein Data Bank December1995 PDB1IRO annotation X-ray crystallography, 1.1 angstroms, residues 1-53 Dauter, Z. Wilson, K.S. Sieker, L.C. Moulis, J.M. Meyer, J. submitted to the Brookhaven Protein Data Bank December1995 PDB1IRN annotation X-ray crystallography, 1.2 angstroms, residues 1-53 Watenpaugh, K.D. Sieker, L.C. Jensen, L.H. J. Mol. Biol. 1381980615-633 Crystallographic refinement of rubredoxin at 1.2 Angstroms resolution. MUID81009589 annotation X-ray crystallography, 1.2 angstroms Watenpaugh, K.D. Siecker, L.C. Herriott, J.R. Jensen, L.H. Acta Crystallogr. B291973943-956 Refinement of the model of a protein: rubredoxin at 1.5 angstrom resolution. annotation X-ray crystallography, 1.5 angstroms rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 modified-site N-formylmethionine 1 experimental binding-site iron (Cys) 6,9,39,42 experimental 54 complete MKKYTCTVCGYIYNPEDGDPDNGVNPGTDFKDIPDDWVCPLCGVGKDQFEEVEE
JU0074 JU0074 28-Feb-1990 22-Jul-1994 24-Oct-1997
rubredoxin Clostridium perfringens Clostridium perfringens Seki, Y. Seki, S. Satoh, M. Ikeda, A. Ishimoto, M. J. Biochem. 1061989336-341 Rubredoxin from Clostridium perfringens: complete amino acid sequence and participation in nitrate reduction. MUID90036784 JU0074 protein 1-54 The protein is reduced with NADH in the presence of a specific NAD(P)H oxidoreductase. rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 binding-site iron (Cys) 6,9,39,42 predicted 54 complete MKKFICDVCGYIYDPAVGDPDNGVEPGTEFKDIPDDWVCPLCGVDKSQFSETEE
JU0127 JU0127 31-Mar-1990 22-Jul-1994 24-Oct-1997
rubredoxin "Butyribacterium methylotrophicum" "Butyribacterium methylotrophicum" Saeki, K. Yao, Y. Wakabayashi, S. Shen, G.J. Zeikus, J.G. Matsubara, H. J. Biochem. 1061989656-662 Ferredoxin and rubredoxin from Butyribacterium methylotrophicum: complete primary structures and construction of phylogenetic trees. MUID90110065 JU0127 protein 1-53 Rubredoxin is a nonheme iron protein and substitutes for ferredoxin in some enzymatic reactions. rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 binding-site iron (Cys) 6,9,39,42 predicted 53 complete MQKYVCDICGYVYDPAVGDPDNGVAPGTAFADLPEDWVCPECGVSKDEFSPEA
A33173 A33173 30-Apr-1991 24-Oct-1997 16-Jun-2000
rubredoxin [validated] Clostridium thermosaccharolyticum Clostridium thermosaccharolyticum, Clostridium tartarivorum Meyer, J. Gagnon, J. Sieker, L.C. Van Dorsselaer, A. Moulis, J.M. Biochem. J. 2711990839-841 Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data. MUID91058526 A33173 protein 1-52 rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 modified-site N-formylmethionine 1 experimental binding-site iron (Cys) 6,9,39,42 predicted 52 complete MEKWQCTVCGYIYDPEVGDPTQNIPPGTKFEDLPDDWVCPDCGVGKDQFEKI
A27537 A27537 05-Jun-1988 22-Jul-1994 24-Oct-1997
rubredoxin Chlorobium limicola f.sp. thiosulfatophilum Chlorobium limicola f.sp. thiosulfatophilum Woolley, K.J. Meyer, T.E. Eur. J. Biochem. 1631987161-166 The complete amino acid sequence of rubredoxin from the green phototrophic bacterium Chlorobium thiosulphatophilum strain PM. MUID87133563 Chlorobium thiosulphatophilum A27537 protein 1-53 rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 binding-site iron (Cys) 6,9,39,42 predicted 53 complete MQKYVCSVCGYVYDPADGEPDDPIDPGTGFEDLPEDWVCPVCGVDKDLFEPES
A33182 A33182 03-Feb-1994 03-Feb-1994 24-Oct-1997
rubredoxin Clostridium sticklandii Clostridium sticklandii Meyer, J. Gagnon, J. Moulis, J.M. submitted to the Protein Sequence Database April1991 A33182 protein 1-53 ATCC 12662 rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 modified-site N-formylmethionine 1 experimental binding-site iron (Cys) 6,9,39,42 predicted 53 complete MTKYVCTVCGYVYDPEVGDPDNNINPGTSFQDIPEDWVCPLCGVGKDQFEEEA
RUDV B33962 A00274 24-Apr-1984 30-Jun-1991 15-Sep-2000
rubredoxin [validated] Desulfovibrio vulgaris (strain Hildenborough) Desulfovibrio vulgaris strain Hildenborough Brumlik, M.J. Voordouw, G. J. Bacteriol. 17119894996-5004 Analysis of the transcriptional unit encoding the genes for rubredoxin (rub) and a putative rubredoxin oxidoreductase (rbo) in Desulfovibrio vulgaris Hildenborough. MUID89359139 B33962 DNA 1-52 GBM28848 NIDg342028 PIDNAAA64798.1 PIDg758677 Bruschi, M. Biochim. Biophys. Acta 43419764-17 Non-heme iron proteins. The amino acid sequence of rubredoxin from Desulfovibrio vulgaris. MUID76232334 A00274 protein 1-20,'T',22-52 strain Hildenborough Adman, E.T. Sieker, L.C. Jensen, L.H. submitted to the Brookhaven Protein Data Bank May1990 PDB7RXN annotation X-ray crystallography, 1.5 angstroms, residues 1-52 Adman, E.T. Seiker, L.C. Jensen, L.H. J. Mol. Biol. 2171991337-352 Structure of rubredoxin from Desulfovibrio vulgaris at 1.5 A resolution. MUID91124457 annotation X-ray crystallography, 1.5 angstroms Dauter, Z. Sieker, L. Wilson, K. submitted to the Brookhaven Protein Data Bank August1991 PDB8RXN annotation X-ray crystallography, 1.0 angstroms, residues 1-52 rub rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 binding-site iron (Cys) 6,9,39,42 experimental 52 complete MKKYVCTVCGYEYDPAEGDPDNGVKPGTSFDDLPADWVCPVCGAPKSEFEAA
JX0241 JX0241 10-Jun-1993 22-Jul-1994 24-Oct-1997
rubredoxin Desulfovibrio vulgaris (strain Miyazaki) Desulfovibrio vulgaris Shimizu, F. Ogata, M. Yagi, T. Wakabayashi, S. Matsubara, H. Biochimie 7119891171-1177 Amino acid sequence and function of rubredoxin from Desulfovibrio vulgaris Miyazaki. MUID90234754 JX0241 protein 1-52 rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-49 modified-site N-formylmethionine (partial) 1 experimental binding-site iron (Cys) 6,9,39,42 predicted 52 complete MKKYVCTVCGYEYDPAEGDPDNGVKPGTAFEDVPADWVCPICGAPKSEFEPA
RUDVEG A00275 07-May-1981 07-May-1981 15-Sep-2000
rubredoxin [validated] Desulfovibrio gigas Desulfovibrio gigas Bruschi, M. Biochem. Biophys. Res. Commun. 701976615-621 The amino acid sequence of rubredoxin from the sulfate reducing bacterium, Desulfovibrio gigas. MUID76231572 A00275 protein 1-52 Frey, M. Sieker, L.C. Payan, F. submitted to the Brookhaven Protein Data Bank March1988 PDB1RDG annotation X-ray crystallography, 1.4 angstroms, residues 1-52 Frey, M. Sieker, L. Payan, F. Haser, R. Bruschi, M. Pepe, G. LeGall, J. J. Mol. Biol. 1971987525-541 Rubredoxin from Desulfovibrio gigas. A molecular model of the oxidized form at 1.4 angstroms resolution. MUID88155649 annotation X-ray crystallography, 1.4 angstroms rubredoxin rubredoxin homology blocked amino end electron transfer iron metalloprotein domain rubredoxin homology 3-49 modified-site N-formylmethionine 1 experimental binding-site iron (Cys) 6,9,39,42 experimental 52 complete MDIYVCTVCGYEYDPAKGDPDSGIKPGTKFEDLPDDWACPVCGASKDAFEKQ
RUDVD A00276 04-Dec-1986 04-Dec-1986 15-Sep-2000
rubredoxin [validated] Desulfovibrio desulfuricans Desulfovibrio desulfuricans Hormel, S. Walsh, K.A. Prickril, B.C. Titani, K. LeGall, J. Sieker, L.C. FEBS Lett. 2011986147-150 Amino acid sequence of rubredoxin from Desulfovibrio desulfuricans strain 27774. MUID86220785 A00276 protein 1-45 Stenkamp, R.E. Sieker, L.C. Jensen, L.H. submitted to the Brookhaven Protein Data Bank January1990 PDB6RXN annotation X-ray crystallography, 1.5 angstroms Sieker, L.C. Stenkamp, R.E. Jensen, L.H. Prickril, B. LeGall, J. FEBS Lett. 208198673-76 Structure of rubredoxin from the bacterium Desulfovibrio desulfuricans. MUID87030959 annotation X-ray crystallography, 1.5 angstroms Rubredoxin, found mostly in anaerobic bacteria, is a small, nonheme, iron protein lacking acid-labile sulfide. rubredoxin rubredoxin homology blocked amino end electron transfer iron metalloprotein domain rubredoxin homology 3-42 modified-site N-formylmethionine 1 experimental binding-site iron (Cys) 6,9,32,35 experimental 45 complete MQKYVCNVCGYEYDPAEHDNVPFDQLPDDWCCPVCGVSKDQFSPA
RUME A00277 13-Jul-1981 13-Jul-1981 24-Oct-1997
rubredoxin Megasphaera elsdenii Megasphaera elsdenii Bachmayer, H. Yasunobu, K.T. Peel, J.L. Mayhew, S. J. Biol. Chem. 24319681022-1030 Non-heme iron proteins. V. The amino acid sequence of rubredoxin from Peptostreptococcus elsdenii. MUID68161650 A00277 protein 1-52 rubredoxin rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 3-48 binding-site iron (Cys) 6,9,38,41 predicted 52 complete MDKYECSICGYIYDEAEGDDGNVAAGTKFADLPADWVCPTCGADKDAFVKMD
RUPF T44570 A41189 30-Jun-1992 20-Apr-2000 21-Jul-2000
rubredoxin [validated] Pyrococcus furiosus Pyrococcus furiosus Jenney Jr., F.E. Verhagen, M.F. Cui, X. Adams, M.W. Science 2861999306-309 Anaerobic microbes: oxygen detoxification without superoxide dismutase. MUID99445924 T44570 preliminary translated from GB/EMBL/DDBJ DNA 1-54 EMBLAF156097 NIDg6066235 PIDNAAF03228.1 PIDg6066243 Blake, P.R. Park, J.B. Bryant, F.O. Aono, S. Magnuson, J.K. Eccleston, E. Howard, J.B. Summers, M.F. Adams, M.W.W. Biochemistry 30199110885-10895 Determinants of protein hyperthermostability: purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR. MUID92031546 A41189 protein 2-54 Day, M.W. Hsu, B.T. Joshua-tor, L. Park, J.B. Zhou, Z.H. Adams, M.W.W. Rees, D.C. submitted to the Brookhaven Protein Data Bank May1992 PDB1CAA annotation X-ray crystallography, 1.8 angstroms, oxidized form, residues 1-53 Day, M.W. Hsu, B.T. Joshua-tor, L. Park, J.B. Zhou, Z.H. Adams, M.W.W. Rees, D.C. submitted to the Brookhaven Protein Data Bank May1992 PDB1CAD annotation X-ray crystallography, 1.8 angstroms, reduced form, residues 1-53 Day, M.W. Hsu, B.T. Joshua-tor, L. Park, J.B. Zhou, Z.H. Adams, M.W.W. Rees, D.C. Protein Sci. 119921494-1507 X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. MUID93271899 annotation X-ray crystallography, 1.8 angstroms Blake, P.R. Park, J.B. Zhou, Z.H. Hare, D.R. Adams, M.W.W. Summers, M.F. submitted to the Brookhaven Protein Data Bank July1992 PDB1ZRP annotation conformation by (1)H-NMR, residues 1-53 Blake, P.R. Park, J.B. Zhou, Z.H. Hare, D.R. Adams, M.W.W. Summers, M.F. Protein Sci. 119921508-1521 Solution-state structure by NMR of zinc-substituted rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. MUID93271900 annotation conformation by (1)H-NMR rubredoxin rubredoxin homology electron transfer iron metalloprotein product rubredoxin 2-54 experimental domain rubredoxin homology 3-49 binding-site iron (Cys) 6,9,39,42 experimental 54 complete MAKWVCKICGYIYDEDAGDPDNGISPGTKFEELPDDWVCPICGAPKSEFEKLED
RUPSO1 A32850 S27991 B31266 30-Sep-1993 30-Sep-1993 11-Jun-1999
rubredoxin I Pseudomonas oleovorans plasmid OCT Pseudomonas oleovorans Kok, M. Oldenhuis, R. van der Linden, M.P.G. Meulenberg, C.H.C. Kingma, J. Witholt, B. J. Biol. Chem. 26419895442-5451 The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. MUID89174582 A32850 DNA 1-132 GBX65936 GBJ04618 NIDg49078 PIDNCAA46734.1 PIDg49080 GBJ04619 van Beilen, J.B. Eggink, G. Enequist, H. Bos, R. Witholt, B. Mol. Microbiol. 619923121-3136 DNA sequence determination and functional characterization of the OCT-plasmid-encoded alkJKL genes of Pseudomonas oleovorans. MUID93086421 S27991 nucleic acid sequence not shown translation not shown DNA 1-132 EMBLX65936 NIDg49078 PIDNCAA46734.1 PIDg49080 the nucleotide sequence was submitted to the EMBL Data Library, April 1992 alkF plasmid OCT Pseudomonas rubredoxin I rubredoxin homology electron transfer hydrocarbon hydroxylation iron metalloprotein domain rubredoxin homology 3-48 binding-site iron (Cys) 6,9,39,42 predicted 132 complete MSRYQCPDCQYIYDENKGEPHEGFHPNTSWNDIPKDWACPDCAVRDKVDFIFLADSPSKE TQLGVNSQLANSESGISDATPTGMAVLAAELVIPLNQENKNEGCAAKTEVLDQASTPQVV RKSSTRKKMRNK
RUPSEO B32850 A00278 S27992 C31266 24-Apr-1984 30-Sep-1993 21-Jul-2000
rubredoxin II Pseudomonas oleovorans plasmid OCT Pseudomonas oleovorans Kok, M. Oldenhuis, R. van der Linden, M.P.G. Meulenberg, C.H.C. Kingma, J. Witholt, B. J. Biol. Chem. 26419895442-5451 The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. MUID89174582 B32850 DNA 1-173 GBJ04618 GBJ04619 Benson, A. Tomoda, K. Chang, J. Matsueda, G. Lode, E.T. Coon, M.J. Yasunobu, K.T. Biochem. Biophys. Res. Commun. 421971640-646 Evolutionary and phylogenetic relationships of rubredoxin-containing microbes. MUID71113196 A00278 protein 2-37,'D',39-40,'C',42-106,'E',108-113,'E',115-132,'W',133-153,155,'D',156-157,'WCBP',161-165,'N',167-173 van Beilen, J.B. Eggink, G. Enequist, H. Bos, R. Witholt, B. Mol. Microbiol. 619923121-3136 DNA sequence determination and functional characterization of the OCT-plasmid-encoded alkJKL genes of Pseudomonas oleovorans. MUID93086421 S27992 nucleic acid sequence not shown translation not shown DNA 'MVMS',1-173 EMBLX65936 NIDg49078 PIDNCAA46735.1 PIDg49081 the nucleotide sequence was submitted to the EMBL Data Library, April 1992 alkG plasmid OCT Pseudomonas rubredoxin II rubredoxin homology duplication electron transfer hydrocarbon hydroxylation iron metalloprotein product rubredoxin II 2-173 experimental domain rubredoxin homology 3-48 domain middle 56-119 domain rubredoxin homology 121-167 binding-site iron (Cys) 6,9,39,42 predicted binding-site iron (Cys) 124,127,157,160 predicted 173 complete MASYKCPDCNYVYDESAGNVHEGFSPGTPWHLIPEDWCCPDCAVRDKLDFMLIESGVGEK GVTSTHTSPNLSEVSGTSLTAEAVVAPTSLEKLPSADVKGQDLYKTQPPRSDAQGGKAYL KWICITCGHIYDEALGDEAEGFTPGTRFEDIPDDWCCPDCGATKEDYVLYEEK
S25690 S32946 S25690 A38532 04-Dec-1992 13-Mar-1997 03-Mar-2000
hupJ protein Rhodobacter capsulatus Rhodobacter capsulatus Colbeau, A. Richaud, P. Toussaint, B. Caballero, F.J. Elster, C. Delphin, C. Smith, R.L. Chabert, J. Vignais, P.M. Mol. Microbiol. 8199315-29 Organization of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two hyp regulatory mutants. MUID93268090 S32946 preliminary DNA 1-278 EMBLZ15089 NIDg313868 PIDNCAA78802.1 PIDg581495 the authors translated the initiation codon TTG for residue 1 as Leu the authors translated the codon ATA for residue 34 as B Toussaint, B. submitted to the EMBL Data Library September1992 S25690 DNA 26-278 EMBLZ15089 Xu, H.W. Wall, J.D. J. Bacteriol. 17319912401-2405 Clustering of genes necessary for hydrogen oxidation in Rhodobacter capsulatus. MUID91177833 A38532 DNA 172-250,'PGPRRWRNRRGGG' GBM55089 NIDg151949 PIDNAAA72923.1 PIDg151950 hupJ TTG part of an operon containing 18 genes involved in hydrogenase activity and expression Rhodobacter hupJ protein rubredoxin homology electron transfer iron metalloprotein domain rubredoxin homology 25-71 binding-site iron (Cys) 28,31,61,64 predicted 278 complete MSGPTRAGFEGSYLGANDRISDLAIMECKICWTPYDPASGDEFRQVLPGTPFTALPEDWH CPNCDAPKAQFIVQSDPGAPALLEQNRVDAQVSALVADFREIWHSKMRDVPLVNKALSIE AVGFRSHEGRGLGVLVSPWFMNLIQLPAAGEDWSGLIPGVKEDLEFPSGLYEFIHNRREM VGGYKACSLYPTMGDFQTQMQAVDLARAVMIELFKAENRAETDRAAEIRASRTAELAALE AAEAEKAETAARAEAMAQPTRRRLISAGLAGEDEGAAE
SDDVEG A37857 A00279 31-Oct-1979 31-Mar-1993 03-Mar-2000
desulforedoxin Desulfovibrio gigas Desulfovibrio gigas Brumlik, M.J. Leroy, G. Bruschi, M. Voordouw, G. J. Bacteriol. 17219907289-7292 The nucleotide sequence of the Desulfovibrio gigas desulforedoxin gene indicates that the Desulfovibrio vulgaris rbo gene originated from a gene fusion event. MUID91072291 A37857 DNA 1-37 GBM62784 NIDg145084 PIDNAAA23365.1 PIDg145085 Bruschi, M. Moura, I. Le Gall, J. Xavier, A.V. Sieker, L.C. Biochem. Biophys. Res. Commun. 901979596-605 The amino acid sequence of desulforedoxin, a new type of non heme iron protein from Desulfovibrio gigas. MUID80064861 A00279 protein 2-37 Desulforedoxin, a nonheme iron protein, is a dimer with two iron atoms linked to eight cysteine residues. dsr desulforedoxin desulforedoxin homology electron transfer homodimer iron metalloprotein domain desulforedoxin homology 1-36 product desulforedoxin 2-37 experimental binding-site iron (Cys) 10,13,29,30 predicted 37 complete MANEGDVYKCELCGQVVKVLEEGGGTLVCCGEDMVKQ
S29861 S29861 10-Sep-1999 28-Jul-2000 28-Jul-2000
hybrid cluster [4Fe-2S-3O] protein [validated] prismane [6Fe-6S] protein [misnomer] Desulfovibrio vulgaris Desulfovibrio vulgaris Stokkermans, J.P.W.G. Pierik, A.J. Wolbert, R.B.G. Hagen, W.R. van Dongen, W.M.A.M. Veeger, C. Eur. J. Biochem. 2081992435-442 The primary structure of a protein containing a putative [6Fe-6S] prismane cluster from Desulfovibrio vulgaris (Hildenborough). MUID92394141 S29861 DNA 1-201,'GRR',205-553 EMBLZ11707 NIDg40832 PIDg40833 this sequence has been corrected in reference A58942 Pierik, A.J. Hagen, W.R. Dunham, W.R. Sands, R.H. Eur. J. Biochem. 2061992705-719 Multi-frequency EPR and high-resolution Moessbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). MUID92298998 annotation evidence for a 6Fe-6S cluster Arendsen, A.F. Hadden, J. Card, G. McAlpine, A.S. Bailey, S. Zaitsev, V. Duke, E.H.M. Lindley, P.F. Kroeckel, M. Trautwein, A.X. Feiters, M.C. Charnock, J.M. Garner, C.D. Marritt, S.J. Thomson, A.J. Kooter, I.M. Johnson, M.K. van den Berg, W.A.M. van Dongen, W.M.A.M. Hagen, W.R. J. Biol. Inorg. Chem. 3199881-95 The "prismane" protein resolved: X-ray structure at 1.7 angstroms and multiple spectroscopy of two novel 4Fe clusters. annotation sequence correction X-ray crystallography, 1.7 angstroms EPR, Moessbauer, and MCD spectrographic analysis because of model inconsistencies with sequence, the authors redetermined the nucleotide sequence and found residues 202-204 should be Ala-Gly-Gly The name "prismane" for this protein is a now known to be a misnomer. The structure for the metal clusters determined by X-ray consists of one four iron/four sulfur cluster and one four iron cluster with mixed ligands. For a description of the 4Fe-2S-3O cluster, see RESID:AA0268. Desulfovibrio hybrid cluster [4Fe-2S-3O] protein hybrid cluster [4Fe-2S-3O] homology 4Fe-2S-3O 4Fe-4S electron transfer iron-sulfur protein metalloprotein domain hybrid cluster [4Fe-2S-3O] homology 221-516 binding-site 4Fe-4S cluster (Cys) (covalent) 3,6,15,21 experimental binding-site 4Fe-2S-3O cluster (His, Glu, Cys, Cys, Cys, Cys, Glu) (covalent) 244,268,312,406,434,459,494 experimental modified-site cysteine persulfide (Cys) 406 experimental 553 complete MFCFQCQETAKNTGCTVKGMCGKPEETANLQDLLIFVLRGIAIYGEKLKELGQPDRSNDD FVLQGLFATITNANWDDARFEAMISEGLARRDKLRNAFLAVYKAKNGKDFSEPLPEAATW TGDSTAFAEKAKSVGILATENEDVRSLRELLIIGLKGVAAYAEHAAVLGFRKTEIDEFML EALASTTKDLSVDEMVALVMKAGGMAVTTMALLDEANTTTYGNPEITQVNIGVGKNPGIL ISGHDLKDMAELLKQTEGTGVDVYTHGEMLPANYYPAFKKYPHFVGNYGGSWWQQNPEFE SFNGPILLTTNCLVPLKKENTYLDRLYTTGVVGYEGAKHIADRPAGGAKDFSALIAQAKK CPPPVEIETGSIVGGFAHHQVLALADKVVEAVKSGAIKRFVVMAGCDGRQKSRSYYTEVA ENLPKDTVILTAGCAKYRYNKLNLGDIGGIPRVLDAGQCNDSYSLAVIALKLKEVFGLDD INDLPVSYDIAWYEQKAVAVLLALLFLGVKGIRLGPTLPAFLSPNVAKVLVENFNIKPIG TVQDDIAAMMAGK
JH0568 JH0568 S04106 S44375 A31993 PT0079 A60749 A38922 S53453 A60870 30-Jun-1992 26-May-1994 15-Sep-2000
thioredoxin [validated] ATL-derived factor (ADF) eosinophil cytotoxicity-enhancing factor thioredoxin-related surface protein SASP human man Homo sapiens Tonissen, K.F. Wells, J.R.E. Gene 1021991221-228 Isolation and characterization of human thioredoxin-encoding genes. MUID91340156 JH0568 DNA 1-105 EMBLX54539 NIDg37455 PIDNCAA38410.1 PIDg825724 EMBLX54540 EMBLX54541 Tagaya, Y. Maeda, Y. Mitsui, A. Kondo, N. Matsui, H. Hamuro, J. Brown, N. Arai, K.I. Yokota, T. Wakasugi, H. Yodoi, J. EMBO J. 81989757-764 ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. MUID89251607 S04106 mRNA 1-105 GBX77584 NIDg453963 PIDNCAA54687.1 PIDg453964 this sequence has been revised in reference S44375 Tagaya, Y. Maeda, Y. Mitsui, A. Kando, N. Matsui, H. Hamuro, J. Brown, N. Arai, K. Tokota, T. Wakasugi, H. Yodoi, J. EMBO J. 1319942244 MUID94244626 erratum S44375 mRNA 1-105 EMBLX77584 NIDg453963 PIDNCAA54687.1 PIDg453964 Wollman, E.E. d'Auriol, L. Rimsky, L. Shaw, A. Jacquot, J.P. Wingfield, P. Graber, P. Dessarps, F. Robin, P. Galibert, F. Bertoglio, J. Fradelizi, D. J. Biol. Chem. 263198815506-15512 Cloning and expression of a cDNA for human thioredoxin. MUID89008454 A31993 mRNA 1-38,'N',40-73,'T',75-105 GBJ04026 NIDg339648 PIDNAAA74596.1 PIDg339649 Martin, H. Dean, M. Biochem. Biophys. Res. Commun. 1751991123-128 Identification of a thioredoxin-related protein associated with plasma membranes. MUID91151337 PT0079 protein 2-13,'X',15 Silberstein, D.S. Ali, M.H. Baker, S.L. David, J.R. J. Immunol. 1431989979-983 Human eosinophil cytotoxicity-enhancing factor. Purification, physical characteristics, and partial amino acid sequence of an active polypeptide. MUID89309777 A60749 protein 2-12,'K',14-15,'XX',18-19,'X',21-22 the abstract is inconsistent with figure 4 in having one undetermined residue after 15-Leu rather than two Rimsky, L. Wakasugi, H. Ferrara, P. Robin, P. Capdevielle, J. Tursz, T. Fradelizi, D. Bertoglio, J. J. Immunol. 13619863304-3310 Purification to homogeneity and NH-2-terminal amino acid sequence of a novel interleukin 1 species derived from a human B cell line. MUID86169684 A38922 protein 2-16 Dean, M.F. Martin, H. Sansom, P.A. Biochem. J. 3041994861-867 Characterization of a thioredoxin-related surface protein. MUID95118305 S53453 protein 1-21;38-57 described to be a surface-associated thioredoxin Wakasugi, H. Rimsky, L. Mahe, Y. Kamel, A.M. Fradelizi, D. Tursz, T. Bertoglio, J. Proc. Natl. Acad. Sci. U.S.A. 841987804-808 Epstein-Barr virus-containing B-cell line produces an interleukin 1 that it uses as a growth factor. MUID87118252 annotation Weichsel, A. Gasdaska, J.R. Powis, G. Montfort, W.R. submitted to the Brookhaven Protein Data Bank February1996 PDB1ERT annotation X-ray crystallography, 1.7 angstroms, reduced form, residues 1-105 Weichsel, A. Gasdaska, J.R. Powis, G. Montfort, W.R. submitted to the Brookhaven Protein Data Bank February1996 PDB1ERU annotation X-ray crystallography, 2.1 angstroms, oxidized form, residues 1-105 Forman-Kay, J.D. Clore, G.M. Gronenborn, A.M. submitted to the Brookhaven Protein Data Bank December1990 PDB4TRX annotation conformation by (1)H-NMR, residues 1-73,'T',75-105 Forman-Kay, J.D. Clore, G.M. Wingfield, P.T. Gronenborn, A.M. Biochemistry 3019912685-2698 High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. MUID91159399 annotation conformation by (1)H- and (15)N-NMR This small ubiquitous protein functions in many intracellular biological pathways. GDBTXN GDB120475 OMIM187700 9q31-9q31 8/3; 43/3; 63/3; 85/3 thioredoxin thioredoxin homology redox-active disulfide product thioredoxin 2-105 experimental domain thioredoxin homology 9-92 disulfide-bonds redox-active 32-35 experimental 105 complete MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVD DCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
JS0667 JS0667 30-Jun-1992 26-May-1994 11-Jun-1999
thioredoxin rhesus macaque rhesus macaque Macaca mulatta An, G. Wu, R. Biochem. Biophys. Res. Commun. 1831992170-175 Thioredoxin gene expression is transcriptionally up-regulated by retinol in monkey conducting airway epithelial cells. MUID92181438 JS0667 mRNA 1-105 GBM84643 NIDg342338 PIDNAAA36921.1 PIDg342339 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-92 disulfide-bonds redox-active 32-35 predicted 105 complete MVKQIESKAAFQEALDDAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVVFLEVDVD DCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
A28086 A28086 30-Jun-1989 26-May-1994 19-Oct-1995
thioredoxin rabbit domestic rabbit Oryctolagus cuniculus Johnson, R.S. Mathews, W.R. Biemann, K. Hopper, S. J. Biol. Chem. 26319889589-9597 Amino acid sequence of thioredoxin isolated from rabbit bone marrow determined by tandem mass spectrometry. MUID88257078 A28086 protein 1-104 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 8-91 disulfide-bonds redox-active 31-34 predicted 104 complete VKQIESKSAFQEVLDSAGDKLVVVDFSATWCGPCKMIKPFFHALSEKFNNVVFIEVDVDD CKDIAAECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELL
S04352 S04352 S66372 31-Mar-1990 26-May-1994 11-Jun-1999
thioredoxin thioredoxin-related surface protein SASP rat Norway rat Rattus norvegicus Tonissen, K.F. Robins, A.J. Wells, J.R.E. Nucleic Acids Res. 1719893973 Nucleotide sequence of a cDNA encoding rat thioredoxin. MUID89282399 S04352 mRNA 1-105 EMBLX14878 NIDg57385 PIDNCAA33019.1 PIDg57386 Dean, M.F. Martin, H. Sansom, P.A. Biochem. J. 3041994861-867 Characterization of a thioredoxin-related surface protein. MUID95118305 S66372 protein 2-21 12-Lys, 15-Gly, 16-Leu, 17-Gln, and 18-Leu were also found described to be a surface-associated thioredoxin thioredoxin thioredoxin homology redox-active disulfide product thioredoxin 2-105 experimental domain thioredoxin homology 9-92 disulfide-bonds redox-active 32-35 predicted 105 complete MVKLIESKEAFQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVD DCQDVAADCEVKCMPTFQFYKKGQKVGEFSGANKEKLEATITEFA
S04107 JC4068 S44376 S04107 21-Nov-1993 17-Oct-1997 11-Jun-1999
thioredoxin ATL-derived factor (ADF) mouse house mouse Mus musculus Matsui, M. Taniguchi, Y. Hirota, K. Taketo, M. Yodoi, J. Gene 1521995165-171 Structure of the mouse thioredoxin-encoding gene and its processed pseudogene. MUID95137382 JC4068 DNA 1-105 DDBJD21855 NIDg517128 Tagaya, Y. Maeda, Y. Mitsui, A. Kando, N. Matsui, H. Hamuro, J. Brown, N. Arai, K. Tokota, T. Wakasugi, H. Yodoi, J. EMBO J. 1319942244 MUID94244626 erratum S44376 mRNA 1-105 EMBLX77585 NIDg453971 PIDNCAA54688.1 PIDg453972 Tagaya, Y. Maeda, Y. Mitsui, A. Kondo, N. Matsui, H. Hamuro, J. Brown, N. Arai, K.I. Yokota, T. Wakasugi, H. Yodoi, J. EMBO J. 81989757-764 ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. MUID89251607 S04107 mRNA 1-93,'N',94-96,'ALT',100-104,'S' GBX77585 This small ubiquitous protein functions in many intracellular biological pathways. MGITxn MGI36258 4:24.6 29/2; 44/1; 84/2 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-92 disulfide-bonds redox-active 32-35 predicted 105 complete MVKLIESKEAFQEALAAAGDKLVVVDFSATWCGPCKMIKPFFHSLCDKYSNVVFLEVDVD DCQDVAADCEVKCMPTFQFYKKGQKVGEFSGANKEKLEASITEYA
A30006 A30006 31-Mar-1989 26-May-1994 11-Jun-1999
thioredoxin chicken chicken Gallus gallus Jones, S.W. Luk, K.C. J. Biol. Chem. 26319889607-9611 Isolation of a chicken thioredoxin cDNA clone: thioredoxin mRNA is differentially expressed in normal and Rous sarcoma virus-transformed chicken embryo fibroblasts. MUID88257080 A30006 mRNA 1-105 GBJ03882 NIDg212765 PIDNAAA49092.1 PIDg212766 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-92 disulfide-bonds redox-active 32-35 predicted 105 complete MVKSVGNLADFEAELKAAGEKLVVVDFSATWCGPCKMIKPFFHSLCDKFGDVVFIEIDVD DAQDVATHCDVKCMPTFQFYKNGKKVQEFSGANKEKLEETIKSLV
S34812 S34812 20-Apr-2000 20-Apr-2000 20-Apr-2000
thioredoxin h2 common tobacco common tobacco Nicotiana tabacum Brugidou, C. Marty, I. Chartier, Y. Meyer, Y. Mol. Gen. Genet. 2381993285-293 The Nicotiana tabacum genome encodes two cytoplasmic thioredoxin genes which are differently expressed. MUID93241165 S34812 DNA 1-118 EMBLZ11803 NIDg297518 PIDNCAA77847.1 PIDg297519 29/3; 70/3 thioredoxin thioredoxin homology domain thioredoxin homology 17-99 118 complete MAEEGQVIGVHTVDAWNEHLQKGIDDKKLIVVDFTASWCGPCKFIASFYAELAKKMPTVT FLKVDVDELKSVATDWAVEAMPTFMFLKEGKIVDKVVGAKKDELQQTIAKHISSTSTA
S16590 S16590 20-Apr-2000 20-Apr-2000 20-Apr-2000
thioredoxin h1 common tobacco common tobacco Nicotiana tabacum Marty, I. Meyer, Y. Plant Mol. Biol. 171991143-147 Nucleotide sequence of a cDNA encoding a tobacco thioredoxin. MUID91329721 S16590 mRNA 1-126 EMBLX58527 NIDg20046 PIDNCAA41415.1 PIDg20047 the authors translated the codon CCA for residue 54 as Arg thioredoxin thioredoxin homology domain thioredoxin homology 24-106 126 complete MAANDATSSEEGQVFGCHKVEEWNEYFKKGVETKKLVVVDFTASWCGPCRFIAPILADIA KKMPHVIFLKVDVDELKTVSAEWSVEAMPTFVFIKDGKEVDRVVGAKKEELQQTIVKHAA PATVTA
JQ2242 JQ2242 T45734 S29905 19-May-1994 26-May-1994 18-Feb-2000
thioredoxin h protein F24M12.70 Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana Rivera-Madrid, R. Marinho, P. Brugidou, C. Chartier, Y. Meyer, Y. Plant Physiol. 1021993327-328 Nucleotide sequence of a cDNA clone encoding an Arabidopsis thaliana thioredoxin h. MUID94151431 JQ2242 mRNA 1-114 EMBLZ14084 NIDg16551 PIDNCAA78462.1 PIDg16552 Vitale, D. Liguori, R. Flores, M. Argiriou, A. De Simone, V. Mewes, H.W. Lemcke, K. Mayer, K.F.X. Quetier, F. Salanoubat, M. submitted to the Protein Sequence Database December1999 T45734 preliminary DNA 1-114 EMBLAL132980 cultivar Columbia; BAC clone F24M12 F24M12.70 3 30/3; 71/3 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 18-100 disulfide-bonds redox-active 40-43 predicted 114 complete MASEEGQVIACHTVETWNEQLQKANESKTLVVVDFTASWCGPCRFIAPFFADLAKKLPNV LFLKVDTDELKSVASDWAIQAMPTFMFLKEGKILDKVVGAKKDELQSTIAKHLA
TXBY1 S15049 B39847 S05793 S53932 S61947 S64531 S63858 A38669 31-Dec-1991 31-Dec-1991 16-Jun-2000
thioredoxin I protein G7746 protein YGR209c thioredoxin 2 yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Gan, Z.R. J. Biol. Chem. 26619911692-1696 Yeast thioredoxin genes. MUID91107668 S15049 DNA 1-104 GBM59168 NIDg173025 PIDNAAA35170.1 PIDg173026 Muller, E.G.D. J. Biol. Chem. 26619919194-9202 Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. MUID91225027 B39847 DNA 1-104 GBM62648 NIDg173049 PIDNAAA35178.1 PIDg173050 Hall, D.E. Baldesten, A. Holmgren, A. Reichard, P. Eur. J. Biochem. 231971328-335 Yeast thioredoxin. Amino-acid sequence around the active-center disulfide of thioredoxin I and II. MUID72100583 S05793 protein 2;27-43;98-104 the sequence from the summary and from Fig. 5 is inconsistent with that from page 332 in having 98-Glu Guerreiro, P. Barreiros, T. Soares, H. Cyrne, L. Maia e Silva, A. Rodrigues-Pousada, C. submitted to the EMBL Data Library April1995 Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 open reading frames, including CCT, ADE3 and TR-I genes, homologous to the yeast YAL023 and EF1G genes, of the human. S53932 DNA 1-104 EMBLZ49133 NIDg790489 PIDNCAA89002.1 PIDg790500 strain S288C Song, J.M. Cheung, E. Rabinowitz, J.C. submitted to the EMBL Data Library November1995 Analysis of the 15.6-kb fragment encompassing the ADE3 gene. S61947 DNA 1-104 EMBLU40843 NIDg1165213 PIDNAAA85584.1 PIDg1165214 strain GRF88 Guerreiro, P. Barreiros, T. Cyrne, L. Soares, H. Maia e Silva, A. Rodrigues-Pousada, C. submitted to the Protein Sequence Database May1996 S64531 DNA 1-104 EMBLZ72994 NIDg1323374 PIDNCAA97236.1 PIDg1323375 GSPDBGN00007 MIPSYGR209c strain S288C Guerreiro, P. Barreiros, T. Soares, H. Cyrne, L. Maia e Silva, A. Rodrigues-Pousada, C. Yeast 121996273-280 Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs. MUID97060019 S63858 nucleic acid sequence not shown translation not shown DNA 1-104 EMBLZ49133 NIDg790489 PIDNCAA89002.1 PIDg790500 the nucleotide sequence was submitted to the EMBL Data Library, April 1995 SGDTRX2 SGDTR-I MIPSYGR209c SGDS0003441 MIPSYGR209c 7R thioredoxin thioredoxin homology redox-active disulfide product thioredoxin I 2-104 experimental domain thioredoxin homology 9-91 disulfide-bonds redox-active 31-34 experimental 104 complete MVTQLKSASEYDSALASGDKLVVVDFFATWCGPCKMIAPMIEKFAEQYSDAAFYKLDVDE VSDVAQKAEVSSMPTLIFYKGGKEVTRVVGANPAAIKQAIASNV
TXBY2 S15048 A39847 S15360 S64870 B38669 31-Dec-1991 31-Dec-1991 16-Jun-2000
thioredoxin II protein L1933 protein YLR043c yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Gan, Z.R. J. Biol. Chem. 26619911692-1696 Yeast thioredoxin genes. MUID91107668 S15048 DNA 1-103 EMBLM59169 NIDg173027 PIDNAAA35171.1 PIDg173028 Muller, E.G.D. J. Biol. Chem. 26619919194-9202 Thioredoxin deficiency in yeast prolongs S phase and shortens the G1 interval of the cell cycle. MUID91225027 A39847 DNA 1-103 GBM62647 NIDg173047 PIDNAAA35177.1 PIDg173048 Hall, D.E. Baldesten, A. Holmgren, A. Reichard, P. Eur. J. Biochem. 231971328-335 Yeast thioredoxin. Amino-acid sequence around the active-center disulfide of thioredoxin I and II. MUID72100583 S15360 protein 26-34 Koetter, P. Rose, M. Entian, K.D. submitted to the Protein Sequence Database May1996 S64870 DNA 1-103 EMBLZ73215 NIDg1360372 PIDNCAA97572.1 PIDg1360373 GSPDBGN00012 MIPSYLR043c experimental_source strain S288C SGDTRX1 SGDTR-II MIPSYLR043c SGDS0004033 MIPSYLR043c 12R thioredoxin thioredoxin homology redox-active disulfide product thioredoxin II 2-103 predicted domain thioredoxin homology 9-90 disulfide-bonds redox-active 30-33 experimental 103 complete MVTQFKTASEFDSAIAQDKLVVVDFYATWCGPCKMIAPMIEKFSEQYPQADFYKLDVDEL GDVAQKNEVSAMPTLLLFKNGKEVAKVVGANPAAIKQAIAANA
G64213 G64213 17-Nov-1995 16-Aug-1996 07-Dec-1999
thioredoxin Mycoplasma genitalium Mycoplasma genitalium Fraser, C.M. Gocayne, J.D. White, O. Adams, M.D. Clayton, R.A. Fleischmann, R.D. Bult, C.J. Kerlavage, A.R. Sutton, G. Kelley, J.M. Fritchman, J.L. Weidman, J.F. Small, K.V. Sandusky, M. Fuhrmann, J. Nguyen, D. Utterback, T.R. Saudek, D.M. Phillips, C.A. Merrick, J.M. Tomb, J.F. Dougherty, B.A. Bott, K.F. Hu, P.C. Lucier, T.S. Peterson, S.N. Smith, H.O. Hutchison III, C.A. Venter, J.C. Science 2701995397-403 The minimal gene complement of Mycoplasma genitalium. MUID96026346 G64213 nucleic acid sequence not shown translation not shown DNA 1-102 GBU39691 GBL43967 NIDg1045794 PIDg1045804 TIGRMG124 strain G-37 SGC3 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-90 disulfide-bonds redox-active 30-33 predicted 102 complete MVTEIRSLKQLEEIFSAKKNVIVDFWAAWCGPCKLTSPEFQKAADEFSDAQFVKVNVDDH TDIAAAYNITSLPTIVVFENGVEKKRAIGFMPKTKIIDLFNN
TXEC A91519 H65181 S30676 I54863 A91802 I52550 A91236 A00280 A22425 A24435 S45671 24-Apr-1984 01-Sep-1995 15-Sep-2000
thioredoxin [validated] Escherichia coli Escherichia coli Wallace, B.J. Kushner, S.R. Gene 321984399-408 Genetic and physical analysis of the thioredoxin (trxA) gene of Escherichia coli K-12. MUID85155506 A91519 DNA 'MLHQQRNQHARLIPVELY',1-109 GBK02845 NIDg147610 PIDNAAA24534.1 PIDg147611 the sequence represents translation from an upstream ATG triplet that seems not to lie in an appropriate context for translation initiation Blattner, F.R. Plunkett III, G. Bloch, C.A. Perna, N.T. Burland, V. Riley, M. Collado-Vides, J. Glasner, J.D. Rode, C.K. Mayhew, G.F. Gregor, J. Davis, N.W. Kirkpatrick, H.A. Goeden, M.A. Rose, D.J. Mau, B. Shao, Y. Science 27719971453-1462 The complete genome sequence of Escherichia coli K-12. MUID97426617 H65181 nucleic acid sequence not shown translation not shown DNA 'MLHQQRNQHARLIPVELY',1-109 GBAE000454 GBU00096 NIDg2367278 PIDNAAC76786.1 PIDg1790215 UWGPb3781 strain K-12, substrain MG1655 the sequence represents translation from an upstream ATG triplet that seems not to lie in an appropriate context for translation initiation Daniels, D.L. Plunkett III, G. Burland, V. Blattner, F.R. Science 2571992771-778 Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. MUID92358234 S30676 DNA 'MLHQQRNQHARLIPVELY',1-109 EMBLM87049 NIDg836656 PIDNAAA67582.1 PIDg148185 the sequence represents translation from an upstream ATG triplet that seems not to lie in an appropriate context for translation initiation Matsumoto, Y. Shigesada, K. Hirano, M. Imai, M. J. Bacteriol. 1661986945-958 Autogenous regulation of the gene for transcription termination factor rho in Escherichia coli: Localization and function of its attenuators. MUID86223816 I54863 translation not shown translated from GB/EMBL/DDBJ DNA 1-109 GBM12779 NIDg148067 PIDNAAA24694.1 PIDg148068 Lim, C.J. Geraghty, D. Fuchs, J.A. J. Bacteriol. 1631985311-316 Cloning and nucleotide sequence of the trxA gene of Escherichia coli K-12. MUID85234377 A91802 DNA 1-109 GBM10424 NIDg147608 PIDNAAA24533.1 PIDg147609 strain K12 Hoeoeg, J. Biosci. Rep. 41984917-923 Nucleotide sequence of the thioredoxin gene from Escherichia coli. MUID85123150 I52550 preliminary translated from GB/EMBL/DDBJ DNA 1-109 GBM26133 NIDg148065 PIDNAAA24693.1 PIDg148066 Holmgren, A. Eur. J. Biochem. 61968475-484 Thioredoxin. 6. The amino acid sequence of the protein from Escherichia coli B. MUID69079993 A91236 protein 2-16,'LV',19-71,'IG',74-109 strain B Haeberlein, I. Eur. J. Biochem. 2231994473-479 Structure requirements for disulfide bridge sulfitolysis of oxidized Escherichia coli thioredoxin studied by fluorescence spectroscopy. MUID94333336 annotation chemical activity of wild type and engineered sequence Katti, S.K. LeMaster, D.M. Eklund, H. submitted to the Brookhaven Protein Data Bank March1990 PDB2TRX annotation X-ray crystallography, 1.68 angstroms, residues 2-109 Katti, S.K. LeMaster, D.M. Eklund, H. J. Mol. Biol. 2121990167-184 Crystal structure of thioredoxin from Escherichia coli at 1.68 Angstroms resolution. MUID90204538 annotation X-ray crystallography, 1.68 angstroms Holmgren, A. Soderberg, B.O. Eklund, H. Branden, C.I. Proc. Natl. Acad. Sci. U.S.A. 7219752305-2309 Three-dimensional structure of Escherichia coli thioredoxin-S-2 to 2.8 angstrom resolution. MUID75176930 annotation X-ray crystallography, 2.8 angstroms Dyson, H.J. Gippert, G.P. Case, D.A. Holmgren, A. Wright, P.E. submitted to the Brookhaven Protein Data Bank January1990 PDB1TRX annotation conformation by (1)H-NMR, reduced form, residues 2-109 Dyson, H.J. Gippert, G.P. Case, D.A. Holmgren, A. Wright, P.E. Biochemistry 2919904129-4136 Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. MUID90298180 annotation conformation by (1)H-NMR Jeng, M.F. Campbell, A.P. Begley, T. Holmgren, A. Case, D.A. Wright, P.E. Dyson, H.J. submitted to the Brookhaven Protein Data Bank November1995 PDB1XOA annotation conformation by (1)H-, (15)N-NMR, oxidized form, residues 2-109 Jeng, M.F. Campbell, A.P. Begley, T. Holmgren, A. Case, D.A. Wright, P.E. Dyson, H.J. submitted to the Brookhaven Protein Data Bank November1995 PDB1XOB annotation conformation by (1)H-, (15)N-NMR, reduced form, residues 2-109 trxA 85 min is reduced with NADPH by thioredoxin reductase (EC 1.6.4.5); the reduced form acts as a two hydrogen atom donor in a variety of intracellular reduction reactions; participates in dithiol-disulfide exchange reactions thioredoxin thioredoxin homology redox-active disulfide product thioredoxin 2-109 experimental domain thioredoxin homology 11-94 disulfide-bonds redox-active 33-36 experimental 109 complete MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLN IDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
S35497 S35497 A49917 S31928 09-Dec-1993 26-May-1994 08-Dec-2000
thioredoxin Salmonella typhimurium Salmonella typhimurium Kotani, H. Nakajima, K. Nucleic Acids Res. 2019921424 Cloning and sequence of thioredoxin gene of Salmonella typhimurium LT2. MUID92220625 S35497 nucleic acid sequence not shown translation not shown DNA 1-109 EMBLD10015 NIDg217084 PIDNBAA00903.1 PIDg217085 strain LT2 the nucleotide sequence was submitted to the EMBL Data Library, March 1992 Miloso, M. Limauro, D. Alifano, P. Rivellini, F. Lavitola, A. Gulletta, E. Bruni, C.B. J. Bacteriol. 17519938030-8037 Characterization of the rho genes of Neisseria gonorrhoeae and Salmonella typhimurium. MUID94075245 A49917 DNA 1-109 GBZ21789 NIDg49361 PIDNCAA79851.1 PIDg49362 submitted to the EMBL Data Library, February 1993 trxA thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 11-94 disulfide-bonds redox-active 33-36 predicted 109 complete MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLN IDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDANLA
TXAI I39624 A23910 31-Dec-1988 11-Apr-1997 11-Jun-1999
thioredoxin 1 Anabaena sp. Anabaena sp. Lim, C. J. Bacteriol. 16819861258-1264 Cloning, expression, and characterization of the Anabaena thioredoxin gene in Escherichia coli. MUID87057030 I39624 preliminary translated from GB/EMBL/DDBJ DNA 1-107 GBM14736 NIDg142117 PIDNAAA22049.1 PIDg142118 Gleason, F.K. Whittaker, M.M. Holmgren, A. Joernvall, H. J. Biol. Chem. 26019859567-9573 The primary structure of thioredoxin from the filamentous cyanobacterium Anabaena sp. 7119. MUID85261357 A23910 protein 2-107 PCC 7119, ATCC 29151 thioredoxin thioredoxin homology heat-stable protein redox-active disulfide product thioredoxin 2-107 experimental domain thioredoxin homology 10-93 disulfide-bonds redox-active 32-35 predicted 107 complete MSAAAQVTDSTFKQEVLDSDVPVLVDFWAPWCGPCRMVAPVVDEIAQQYEGKIKVVKVNT DENPQVASQYGIRSIPTLMIFKGGQKVDMVVGAVPKTTLSQTLEKHL
A26622 A26622 31-Mar-1988 26-May-1994 11-Apr-1995
thioredoxin Chromatium vinosum Chromatium vinosum Johnson, R.S. Biemann, K. Biochemistry 2619871209-1214 The primary structure of thioredoxin from Chromatium vinosum determined by high-performance tandem mass spectrometry. MUID87185419 A26622 protein 1-107 unidentified residues are Ile or Leu thioredoxin thioredoxin homology heat-stable protein redox-active disulfide domain thioredoxin homology 10-93 disulfide-bonds redox-active 32-35 predicted 107 complete SDSIVHVTDDSFEEEVXKSPDPVLVDYWADWCGPCKMXAPVXDEIADEYAGRVKXAKXNX DENPNTPPRYGXRGIPTLMLFRGGEVEATKVGAVSKSQLTAFLDSNX
A35135 A35135 A30508 27-Jul-1990 26-May-1994 11-Jun-1999
thioredoxin Rhodobacter sphaeroides Rhodobacter sphaeroides Pille, S. Chuat, J.C. Breton, A.M. Clement-Metral, J.D. Galibert, F. J. Bacteriol. 17219901556-1561 Cloning, nucleotide sequence, and expression of the Rhodobacter sphaeroides Y thioredoxin gene. MUID90170874 A35135 DNA 1-106 GBM33806 NIDg152044 PIDNAAA26182.1 PIDg152045 strain Y Clement-Metral, J.D. Holmgren, A. Cambillau, C. Joernvall, H. Eklund, H. Thomas, D. Lederer, F. Eur. J. Biochem. 1721988413-419 Amino acid sequence determination and three-dimensional modelling of thioredoxin from the photosynthetic bacterium Rhodobacter sphaeroides Y. MUID88166714 A30508 protein 2-63,'Z',65-106 strain Y thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-92 disulfide-bonds redox-active 31-34 predicted 106 complete MSTVPVTDATFDTEVRKSDVPVVVDFWAEWCGPCRQIGPALEELSKEYAGKVKIVKVNVD ENPESPAMLGVRGIPALFLFKNGQVVSNKVGAAPKAALATWIASAL
A28215 A28215 28-Aug-1989 26-May-1994 11-Apr-1995
thioredoxin Rhodospirillum rubrum Rhodospirillum rubrum Johnson, T.C. Yee, B.C. Carlson, D.E. Buchanan, B.B. Johnson, R.S. Mathews, W.R. Biemann, K. J. Bacteriol. 17019882406-2408 Thioredoxin from Rhodospirillum rubrum: primary structure and relation to thioredoxins from other photosynthetic bacteria. MUID88198045 A28215 protein 1-104 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 7-90 disulfide-bonds redox-active 29-32 predicted 104 complete MKQVSDASFEEDVLKADGPVXVDFWAEWCGPCRQXAPALEELATALGDKVTVAKINIDEN PQTPSKYGVRGIPTLMIFKDGQVAATKIGALPKTKLFEWVEASV
A32956 A32956 A30842 17-Jul-1992 26-May-1994 11-Jun-1999
thioredoxin m Synechococcus sp. Synechococcus sp. Muller, E.G.D. Buchanan, B.B. J. Biol. Chem. 26419894008-4014 Thioredoxin is essential for photosynthetic growth. The thioredoxin m gene of Anacystis nidulans. MUID89139466 A32956 DNA 1-107 GBJ04475 NIDg142153 PIDNAAA22057.1 PIDg142154 the source is designated as Anacystis nidulans R2, which is also called Synechococcus R2 trxM thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 10-93 disulfide-bonds redox-active 32-35 predicted 107 complete MSVAAAVTDATFKQEVLESSIPVLVDFWAPWCGPCRMVAPVVDEIAQQYSDQVKVVKVNT DENPSVASQYGIRSIPTLMIFKDGQRVDTVVGAVPKTTLANTLDKHL
S31915 S31915 S45488 03-Mar-1994 26-May-1994 11-Jun-1999
thioredoxin red alga (Cyanidium caldarium) Cyanidium caldarium Langsdorf, A. Emich, A. Zetsche, K. submitted to the EMBL Data Library February1993 A thioredoxin gene is located upstream of rbcLS in the unicellular red alga Cyanidium caldarium, strain RK-1. S31915 DNA 1-107 EMBLZ21723 NIDg14402 PIDNCAA79820.1 PIDg14403 Ohta, N. Kawano, S. Kuroiwa, T. Curr. Genet. 261994136-138 Physical map of the plastid genome of the unicellular red alga Cyanidium caldarium strain RK-1. MUID95094309 S45488 preliminary DNA 'M',6,'IDEL',11-12,'DT',15-16,'LQ',19,'HQ',22-38,'A',40,'IL',43-44,'I',46-48,'LDI',54,'V',56-57,'L',59-64,'NLAT',69-82,'K',84,'Q',86,'L',88-99,'M',101,'TIE',105-107 trx thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 10-93 disulfide-bonds redox-active 32-35 predicted 107 complete MPSPIQVTDFSFEKEVVNSEKLVLVDFWAPWCGPCRMISPVIDELAQEYVEQVKIVKINT DENPSISAEYGIRSIPTLMLFKDGKRVDTVIGAVPKSTLTNALKKYL
TXFK A00281 02-Apr-1982 02-Apr-1982 11-Apr-1995
thioredoxin coryneform bacterium ATCC11425 coryneform bacterium ATCC11425 Meng, M. Hogenkamp, H.P.C. J. Biol. Chem. 25619819174-9182 Purification, characterization, and amino acid sequence of thioredoxin from Corynebacterium nephridii. MUID81264365 A00281 protein 1-105 the source was designated as Corynebacterium nephridii Thioredoxins are ubiquitous small hydrogen carrier proteins that participate in a wide variety of biochemical reactions. thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 8-91 disulfide-bonds redox-active 30-33 experimental 105 complete ATVKVDNSNFQSDVLQSSEPVVVDFWAEWCGPCKMIAPALDEIATEMAGQVKIAKVNIDE NPELAAQFGVRSIPTLLMFKDGELAANMVGAAPKSRLADWIKASA
TXSPM S20496 JT0023 B20273 30-Sep-1988 13-Mar-1998 11-Jun-1999
thioredoxin m precursor spinach spinach Spinacia oleracea Wedel, N. Clausmeyer, S. Herrmann, R.G. Gardet-Salvi, L. Schuermann, P. Plant Mol. Biol. 181992527-533 Nucleotide sequence of cDNAs encoding the entire precursor polypeptide for thioredoxin m from spinach chloroplasts. MUID92163017 S20496 not compared with conceptual translation mRNA 1-181 GBX51462 GBS84848 NIDg21347 PIDNCAA35826.1 PIDg21348 Maeda, K. Tsugita, A. Dalzoppo, D. Vilbois, F. Schurmann, P. Eur. J. Biochem. 1541986197-203 Further characterization and amino acid sequence of m-type thioredoxins from spinach chloroplasts. MUID86108311 JT0023 protein 68-82,'G',84-89,'Q',91,'SE',94,'S',96-127,'T',129-164,'D',166,'S',168,'YQ',171 This enzyme has amino-terminal heterogeneity. Thioredoxin m activates malate dehydrogenase. Arg-145 and Gly-164 are both essential for thioredoxin to interact with thioredoxin reductase and ribonucleotide reductase. thioredoxin thioredoxin homology chloroplast redox-active disulfide domain transit peptide (chloroplast) 1-67 predicted product thioredoxin mb 68-171 experimental product thioredoxin mc 69-171 experimental product thioredoxin md 70-171 experimental domain thioredoxin homology 82-165 disulfide-bonds redox-active 104-107 experimental 181 complete MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQF RYSSVVCKASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKE YSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLS P
B37192 B37192 H69726 31-Jan-1992 26-May-1994 16-Jun-2000
thioredoxin Bacillus subtilis Bacillus subtilis Chen, N.Y. Zhang, J.J. Paulus, H. J. Gen. Microbiol. 13519892931-2940 Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli. MUID90132525 B37192 DNA 1-104 GBJ03294 GBM26384 NIDg142519 PIDNAAA87315.1 PIDg142520 Kunst, F. Ogasawara, N. Moszer, I. Albertini, A.M. Alloni, G. Azevedo, V. Bertero, M.G. Bessieres, P. Bolotin, A. Borchert, S. Boriss, R. Boursier, L. Brans, A. Braun, M. Brignell, S.C. Bron, S. Brouillet, S. Bruschi, C.V. Caldwell, B. Capuano, V. Carter, N.M. Choi, S.K. Codani, J.J. Connerton, I.F. Cummings, N.J. Daniel, R.A. Denizot, F. Devine, K.M. Duesterhoeft, A. Ehrlich, S.D. Emmerson, P.T. Entian, K.D. Errington, J. Fabret, C. Ferrari, E. Foulger, D. Fritz, C. Fujita, M. Fujita, Y. Fuma, S. Galizzi, A. Galleron, N. Ghim, S.Y. Glaser, P. Goffeau, A. Golightly, E.J. Grandi, G. Guiseppi, G. Guy, B.J. Haga, K. Haiech, J. Harwood, C.R. Henaut, A. Hilbert, H. Holsappel, S. Hosono, S. Hullo, M.F. Itaya, M. Jones, L. Joris, B. Karamata, D. Kasahara, Y. Klaerr-Blanchard, M. Klein, C. Kobayashi, Y. Koetter, P. Koningstein, G. Krogh, S. Kumano, M. Kurita, K. Lapidus, A. Lardinois, S. Lauber, J. Lazarevic, V. Lee, S.M. Levine, A. Liu, H. Masuda, S. Maueel, C. Medigue, C. Medina, N. Mellado, R.P. Mizuno, M. Moestl, D. Nakai, S. Noback, M. Noone, D. O'Reilly, M. Ogawa, K. Ogiwara, A. Oudega, B. Park, S.H. Parro, V. Pohl, T.M. Portetelle, D. Porwolik, S. Prescott, A.M. Presecan, E. Pujic, P. Purnelle, B. Rapoport, G. Rey, M. Reynolds, S. Rieger, M. Rivolta, C. Rocha, E. Roche, B. Rose, M. Sadaie, Y. Sato, T. Scanlon, E. Schleich, S. Schroeter, R. Scoffone, F. Sekiguchi, J. Sekowska, A. Seror, S.J. Serror, P. Shin, B.S. Soldo, B. Sorokin, A. Tacconi, E. Takagi, T. Takahashi, H. Takemaru, K. Takeuchi, M. Tamakoshi, A. Tanaka, T. Terpstra, P. Tognoni, A. Tosato, V. Uchiyama, S. Vandenbol, M. Vannier, F. Vassarotti, A. Viari, A. Wambutt, R. Wedler, E. Wedler, H. Weitzenegger, T. Winters, P. Wipat, A. Yamamoto, H. Yamane, K. Yasumoto, K. Yata, K. Yoshida, K. Yoshikawa, H.F. Zumstein, E. Yoshikawa, H. Danchin, A. Nature 3901997249-256 The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. MUID98044033 H69726 nucleic acid sequence not shown translation not shown DNA 1-104 GBZ99118 GBAL009126 NIDg2635200 PIDNCAB14810.1 PIDg2635315 strain 168 trxA 70 min thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-90 disulfide-bonds redox-active 29-32 experimental 104 complete MAIVKATDQSFSAETSEGVVLADFWAPWCGPCKMIAPVLEELDQEMGDKLKIVKIDVDEN QETAGKYGVMSIPTLLVLKDGEVVETSVGFKPKEALQELVNKHL
S02802 S02802 A29797 28-Feb-1990 26-May-1994 28-May-1999
thioredoxin C-2 coryneform bacterium coryneform bacterium McFarlan, S.C. Hogenkamp, H.P.C. Eccleston, E.D. Howard, J.B. Fuchs, J.A. Eur. J. Biochem. 1791989389-398 Purification, characterization and revised amino acid sequence of a second thioredoxin from Corynebacterium nephridii. MUID89137116 S02802 protein 1-108 the source is designated as Corynebacterium nephridii Lim, C.J. Fuchs, J.A. McFarlan, S.C. Hogenkamp, H.P.C. J. Biol. Chem. 262198712114-12119 Cloning, expression, and nucleotide sequence of a gene encoding a second thioredoxin from Corynebacterium nephridii. MUID87308211 A29797 not compared with conceptual translation DNA 'MMFKFALYFLNLEQPY',2-108 GBJ02801 NIDg144988 PIDNAAA23305.1 PIDg144989 the source is designated as Corynebacterium nephridii this sequence has been revised in reference S02802 thioredoxin thioredoxin homology redox-active disulfide product thioredoxin C-2 2-108 experimental domain thioredoxin homology 11-94 disulfide-bonds redox-active 33-36 predicted 108 complete MSATIVNTTDENFQADVLDAETPVLVDFWAGWCAPCKAIAPVLEELSNEYAGKVKIVKVD VTSCEDTAVKYNIRNIPALLMFKDGEVVAQQVGAAPRSKLAAFIDQNI
S38909 S38909 22-Jan-1994 26-May-1994 11-Jun-1999
thioredoxin m precursor garden pea garden pea Pisum sativum Lopez Jaramillo, J. Chueca, A. Sahrawy, M. Prado, F. Lazaro, J.J. Hermoso, R. Lopez Gorge, J. submitted to the EMBL Data Library November1993 S38909 mRNA 1-172 EMBLX76269 NIDg431956 PIDNCAA53900.1 PIDg431957 thioredoxin thioredoxin homology chloroplast redox-active disulfide domain transit peptide (chloroplast) 1-57 predicted product thioredoxin m 58-172 predicted domain thioredoxin homology 75-158 disulfide-bonds redox-active 97-100 predicted 172 complete MALESLFKSIHTKTSLSSSIVFIFKGKACLLTSKSRIQESFAELNSFTSLVLLIENHVLL HAREAVNEVQVVNDSSWDELVIGSETPVLVDFWAPWCGPCRMIAPIIDELAKEYAGKIKC YKLNTDESPNTATKYGIRSIPTVLFFKNGERKDSVIGAVPKATLSEKVEKYI
A32233 A32233 08-Sep-1989 26-May-1994 15-Sep-2000
thioredoxin 2 [validated] Anabaena sp. (strain PCC 7120) Anabaena sp. strain PCC 7120 Alam, J. Curtis, S. Gleason, F.K. Gerami-Nejad, M. Fuchs, J.A. J. Bacteriol. 1711989162-171 Isolation, sequence, and expression in Escherichia coli of an unusual thioredoxin gene from the cyanobacterium Anabaena sp. strain PCC 7120. MUID89123014 A32233 DNA 1-111 GBM22997 NIDg340784 PIDNAAA22048.1 PIDg517044 PCC 7120 Gleason, F.K. J. Bacteriol. 17419922592-2598 Activities of two dissimilar thioredoxins from the cyanobacterium Anabaena sp. strain PCC 7120. MUID92210503 annotation expression and possible metabolic role Saarinen, M. Gleason, F.K. Eklund, H. submitted to the Brookhaven Protein Data Bank July1995 PDB1THX annotation X-ray crystallography, 1.7 angstroms, residues 2-109 strain PCC 7120, ATCC:27893, expressed in Escherichia coli is reduced with NADPH by thioredoxin reductase (EC 1.6.4.5); the reduced form acts as a two hydrogen atom donor in a variety of intracellular reduction reactions; participates in dithiol-disulfide exchange reactions thioredoxin 2 is expressed at very low levels and may function in glucose metabolism thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 11-94 disulfide-bonds redox-active 33-36 predicted 111 complete MSKGVITITDAEFESEVLKAEQPVLVYFWASWCGPCQLMSPLINLAANTYSDRLKVVKLE IDPNPTTVKKYKVEGVPALRLVKGEQILDSTEGVISKDKLLSFLDTHLNNN
S57775 S57775 S57799 S54868 S16090 S54870 27-Oct-1995 21-Jan-1997 15-Sep-2000
thioredoxin h, cytosolic [validated] Chlamydomonas reinhardtii Chlamydomonas reinhardtii Stein, M. Jacquot, J.P. Jeannette, E. Decottignies, P. Hodges, M. Lancelin, J.M. Mittard, V. Schmitter, J.M. Miginiac-Maslow, M. Plant Mol. Biol. 281995487-503 Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. MUID95359406 S57775 DNA 1-113 EMBLX80887 NIDg840742 PIDNCAA56850.1 PIDg840743 S57799 protein 2-15 Stein, M. Hodges, M. Jeanette, E. Lancelin, J.M. Jacquot, J.P. submitted to the EMBL Data Library April1994 Chlamydomonas reinhardtii thioredoxins I : cDNA and amino acid deduced sequences of chloroplastic m and cytosolic h isoforms. S54868 mRNA 1-113 EMBLX78822 NIDg840740 PIDNCAA55399.1 PIDg840741 Decottignies, P. Schmitter, J.M. Dutka, S. Jacquot, J.P. Miginiac-Maslow, M. Eur. J. Biochem. 1981991505-512 Characterization and primary structure of a second thioredoxin from the green alga, Chlamydomonas reinhardtii. MUID91249849 S16090 protein 2-112 Mittard, V. Blackledge, M.J. Stein, M. Jacquot, J.P. Marion, D. Lancelin, J.M. submitted to the Brookhaven Protein Data Bank May1996 PDB1TOF annotation conformation by (1)H, (13)C, (15)N-NMR, residues 2-113 Mittard, V. Morelle, N. Brutscher, B. Simorre, J.P. Marion, D. Stein, M. Jacquot, J.P. Lirsac, P.N. Lancelin, J.M. Eur. J. Biochem. 2291995473-485 (1)H, (13)C, (15)N-NMR resonance assignments of oxidized thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii using new methods based on two-dimensional triple-resonance NMR spectroscopy and computer-assisted backbone assignment. MUID95262711 annotation conformation by (1)H, (13)C, (15)N-NMR 27/3; 35/3; 69/3 thioredoxin thioredoxin homology redox-active disulfide product thioredoxin h 2-113 experimental domain thioredoxin homology 15-98 disulfide-bonds redox-active 37-40 experimental 113 complete MGGSVIVIDSKAAWDAQLAKGKEEHKPIVVDFTATWCGPCKMIAPLFETLSNDYAGKVIF LKVDVDAVAAVAEAAGITAMPTFHVYKDGVKADDLVGASQDKLKALVAKHAAA
A55124 A55124 10-Sep-1999 10-Sep-1999 10-Sep-1999
thioredoxin Chloroflexus aurantiacus Chloroflexus aurantiacus Biemann, K. Papayannopoulos, I.A. Acc. Chem. Res. 271994370-378 Amino acid sequencing of proteins. A55124 preliminary protein 1-109 41-Asn, 58-Asp, 59-Val were also found the species is identified as Chlorofleuxus aurianticus Unidentified residue is Ile or Leu. thioredoxin thioredoxin homology methylated amino acid redox-active disulfide domain thioredoxin homology 9-92 disulfide-bonds redox-active 31-34 predicted modified-site N6-methyllysine or N6,N6-dimethyllysine (Lys) (partial) 104 experimental 109 complete AKPIEVHDSDFAEKVLQSKTPVVVDFWAPWCGPCRVIAPILDKLAGEYAGRLTIAKVNTD DNVQYASQLGLKGLPTXVIFKDGREVGRLVGARPEAMYREIFDKVLAMA
S38989 S38989 10-Sep-1999 10-Sep-1999 21-Jul-2000
thioredoxin glycine reductase complex thioredoxin chain A Eubacterium acidaminophilum Eubacterium acidaminophilum Luebbers, M. Andreesen, J.R. Eur. J. Biochem. 2171993791-798 Components of glycine reductase from Eubacterium acidaminophilum. Cloning, sequencing and identification of the genes for thioredoxin reductase, thioredoxin and selenoprotein P(A). MUID94039119 S38989 preliminary DNA 1-110 GBL04500 NIDg2708733 PIDNAAB93304.1 PIDg388295 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 11-94 disulfide-bonds redox-active 33-36 predicted 110 complete MSALLVEIDKDQFQAEVLEAEGYVLVDYFSDGCVPCKALMPDVEELAAKYEGKVAFRKFN TSSARRLAISQKILGLPTITLYKGGQKVEEVTKDDATRENIDAMIAKHVG
A46264 A46264 10-Sep-1999 10-Sep-1999 10-Sep-1999
thioredoxin 1 slime mold (Dictyostelium discoideum) Dictyostelium discoideum Wetterauer, B. Jacquot, J.P. Veron, M. J. Biol. Chem. 26719929895-9904 Thioredoxins from Dictyostelium discoideum are a developmentally regulated multigene family. MUID92250653 A46264 preliminary not compared with conceptual translation mRNA 1-105 GBM91384 NIDg167928 PIDNAAA33258.1 PIDg167929 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 9-92 disulfide-bonds redox-active 32-35 predicted 105 complete MSNRVIHVSSCEELDKHLRDERVVVDFSAVWCGPCRAISPVFEKLSNEFITFTFLHVDID KLNVHPIVSKIKSVPTFHFYRNGSKVSEFSGASESILRSTLEANK
S47867 S47867 10-Sep-1999 10-Sep-1999 10-Sep-1999
thioredoxin-like protein fruit fly (Drosophila melanogaster) Drosophila melanogaster Salz, H.K. Flickinger, T.W. Mittendorf, E. Pellicena-Palle, A. Petschek, J.P. Brown Albrecht, E. Genetics 13619941075-1086 The Drosophila maternal effect locus deadhead encodes a thioredoxin homolog required for female meiosis and early embryonic development. MUID94274010 S47867 preliminary mRNA 1-107 EMBLL27072 NIDg435591 PIDNAAA28937.1 PIDg435963 FlyBasedhd FlyBaseFBgn0011761 thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 8-92 disulfide-bonds redox-active 31-34 predicted 107 complete MASVRTMNDYHKRIEAADDKLIVLDFYATWCGPCKEMESTVKSLARKYSSKAVVLKIDVD KFEELTERYKVRSMPTFVFLRQNRRLASFAGADEHKLTNMMAKLVKA
S19498 S19498 10-Sep-1999 10-Sep-1999 21-Jul-2000
thioredoxin homolog YCR083w yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Feldmann, H. Mannhaupt, G. Vetter, I. submitted to the Protein Sequence Database March1992 S19498 DNA 1-127 EMBLX59720 NIDg1907116 PIDNCAA42258.1 PIDg1907220 GSPDBGN00003 MIPSYCR083w MIPSYCR083w 3R thioredoxin thioredoxin homology redox-active disulfide domain thioredoxin homology 34-115 disulfide-bonds redox-active 55-58 predicted 127 complete MLFYKPVMRMAVRPLKSIRFQSSYTSITKLTNLTEFRNLIKQNDKLVIDFYATWCGPCKM MQPHLTKLIQAYPDVRFVKCDVDESPDIAKECEVTAMPTFVLGKDGQLIGKIIGANPTAL EKGIKDL
S57774 S57774 S57800 S54844 S22810 S10743 S18859 S54869 27-Oct-1995 21-Jan-1997 05-May-2000
thioredoxin m precursor, chloroplast Chlamydomonas reinhardtii Chlamydomonas reinhardtii Stein, M. Jacquot, J.P. Jeannette, E. Decottignies, P. Hodges, M. Lancelin, J.M. Mittard, V. Schmitter, J.M. Miginiac-Maslow, M. Plant Mol. Biol. 281995487-503 Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. MUID95359406 S57774 DNA 1-140 EMBLX80888 NIDg840746 PIDNCAA56851.1 PIDg840747 S57800 protein 35-42 Stein, M. Hodges, M. Jeanette, E. Lancelin, J.M. Jacquot, J.P. submitted to the EMBL Data Library April1994 Chlamydomonas reinhardtii thioredoxins I : cDNA and amino acid deduced sequences of chloroplastic m and cytosolic h isoforms. S54844 mRNA 13-140 EMBLX78821 NIDg840744 PIDNCAA55398.1 PIDg840745 Jacquot, J.P. Stein, M. Hodges, M. Miginiac-Maslow, M. Nucleic Acids Res. 201992617 PCR cloning of a nucleotidic sequence coding for the mature part of Chlamydomonas reinhardtii thioredoxin Ch2. MUID92158682 S22810 preliminary nucleic acid sequence not shown translation not shown mRNA 35-140 EMBLX62335 NIDg18240 PIDNCAA44209.1 PIDg18241 this sequence was submitted to the EMBL Data Library, November 1991 Decottignies, P. Schmitter, J.M. Jacquot, J.P. Dutka, S. Picaud, A. Gadal, P. Arch. Biochem. Biophys. 2801990112-121 Purification, characterization, and complete amino acid sequence of a thioredoxin from a green alga, Chlamydomonas reinhardtii. MUID90282480 S10743 protein 35-40,'EE',43-86,'E',88-118,'D',120-140 nuclear 111/3 thioredoxin thioredoxin homology chloroplast redox-active disulfide domain transit peptide (chloroplast) 1-34 predicted product thioredoxin 35-140 experimental domain thioredoxin homology 42-125 disulfide-bonds redox-active 64-67 predicted 140 complete MALVARRAAVPSARSSARPAFARAAPRRSVVVRAEAGAVNDDTFKNVVLESSVPVLVDFW APWCGPCRIIAPVVDEIAGEYKDKLKCVKLNTDESPNVASEYGIRSIPTIMVFKGGKKCE TIIGAVPKATIVQTVEKYLN
S47472 S68701 S45357 S70628 S77693 A44568 B44568 I37436 S67515 S47472 S67480 13-Jan-1995 02-Jul-1998 11-Jun-1999
glutaredoxin thioltransferase human man Homo sapiens Padilla, C.A. Spyrou, G. Holmgren, A. FEBS Lett. 378199669-73 High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys(7) to Ser mutant protein. MUID96140711 S68701 mRNA 1-106 EMBLX76648 NIDg531404 PIDNCAA54094.1 PIDg531405 Fernando, M.R. Sumimoto, H. Nanri, H. Kawabata, S. Iwanaga, S. Minakami, S. Fukumaki, Y. Takeshige, K. Biochim. Biophys. Acta 12181994229-231 Cloning and sequencing of the cDNA encoding human glutaredoxin. MUID94289487 S45357 mRNA 1-95,'V',97-106 EMBLD21238 NIDg643694 PIDNBAA04769.1 PIDg643695 Park, J.B. Levine, M. Biochem. J. 3151996931-938 Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin. MUID96220709 S70628 mRNA 1-106 EMBLU40574 NIDg1172130 PIDg1172131 cell-type neutrophil S77693 protein 15-27;78-87,'X',89-94 cell-type neutrophil Papov, V.V. Gravina, S.A. Mieyal, J.J. Biemann, K. Protein Sci. 31994428-434 The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells. MUID94290317 A44568 protein 2-51,'D',53-106 B44568 protein 2-106 Padilla, C.A. Martinez-Galisteo, E. Barcena, J.A. Spyrou, G. Holmgren, A. Eur. J. Biochem. 227199527-34 Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. MUID95154298 I37436 mRNA 1-106 EMBLX76648 NIDg531404 PIDNCAA54094.1 PIDg531405 placenta S67515 protein 4-105 placenta GDBGLRX GDBGXN GDB574099 GDB377324 OMIM600443 5q14-5q14 catalyzes reduction of a variety of disulfides, including protein disulfides, in the presence of reduced glutathione glutaredoxin glutaredoxin homology acetylated amino end deoxyribonucleotide biosynthesis disulfide bond electron transfer redox-active disulfide domain glutaredoxin homology 5-99 modified-site acetylated amino end (Ala) (in mature form) 2 experimental disulfide-bonds redox-active 23-26 predicted disulfide-bonds 79-83 predicted 106 complete MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDY LQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ
GDPG JQ0117 A29322 31-Dec-1990 31-Dec-1990 11-Jun-1999
glutaredoxin thioltransferase pig domestic pig Sus scrofa domestica Yang, Y. Gan, Z.R. Wells, W.W. Gene 831989339-346 Cloning and sequencing the cDNA encoding pig liver thioltransferase. MUID90060846 JQ0117 mRNA 1-106 GBM31453 NIDg164705 PIDNAAA31132.1 PIDg164706 liver Gan, Z.R. Wells, W.W. J. Biol. Chem. 26219876699-6703 The primary structure of pig liver thioltransferase. MUID87194912 A29322 protein 3-4,'A',5-106 liver This enzyme catalyzes the reduction of a variety of disulfides, including protein disulfides, in the presence of reduced glutathione. glutaredoxin glutaredoxin homology acetylated amino end deoxyribonucleotide biosynthesis electron transfer redox-active disulfide product glutaredoxin 2-106 experimental domain glutaredoxin homology 5-99 modified-site acetylated amino end (Ala) (in mature form) 2 experimental disulfide-bonds redox-active 23-26 predicted disulfide-bonds 79-83 experimental 106 complete MAQAFVNSKIQPGKVVVFIKPTCPFCRKTQELLSQLPFKEGLLEFVDITATSDTNEIQDY LQQLTGARTVPRVFIGKECIGGCTDLESMHKRGELLTRLQQIGALK
GDBO A30164 S07229 31-Dec-1990 31-Dec-1990 05-Dec-1997
glutaredoxin thioltransferase bovine cattle Bos primigenius taurus Papayannopoulos, I.A. Gan, Z.R. Wells, W.W. Biemann, K. Biochem. Biophys. Res. Commun. 15919891448-1454 A revised sequence of calf thymus glutaredoxin. MUID89193746 A30164 protein 1-105 calf thymus Klintrot, I.M. Hoeoeg, J.O. Joernvall, H. Holmgren, A. Luthman, M. Eur. J. Biochem. 1441984417-423 The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends and with an additional half-cystine/cysteine pair. MUID85027238 S07229 protein 'QA',3-67,72-105 This enzyme catalyzes the reduction of a variety of disulfides, including protein disulfides, in the presence of reduced glutathione. glutaredoxin glutaredoxin homology acetylated amino end deoxyribonucleotide biosynthesis electron transfer redox-active disulfide domain glutaredoxin homology 4-98 modified-site acetylated amino end (Ala) 1 experimental disulfide-bonds redox-active 22-25 predicted disulfide-bonds 78-82 predicted 105 complete AQAFVNSKIQPGKVVVFIKPTCPYCRKTQELLSQLPFKQGLLEFVDITAAGNISEIQDYL QQLTGARTVPRVFIGQECIGGCTDLVNMHERGELLTRLKQMGALQ
GDRB A32682 31-Dec-1990 31-Dec-1990 05-Dec-1997
glutaredoxin thioltransferase rabbit domestic rabbit Oryctolagus cuniculus Hopper, S. Johnson, R.S. Vath, J.E. Biemann, K. J. Biol. Chem. 264198920438-20447 Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry. MUID90062176 A32682 protein 1-106 bone marrow This enzyme catalyzes the reduction of a variety of disulfides, including protein disulfides, in the presence of reduced glutathione. glutaredoxin glutaredoxin homology acetylated amino end deoxyribonucleotide biosynthesis electron transfer redox-active disulfide domain glutaredoxin homology 4-98 modified-site acetylated amino end (Ala) 1 experimental disulfide-bonds redox-active 22-25 predicted disulfide-bonds 78-82 predicted 106 complete AQEFVNSKIQPGKVVVFIKPTCPYCRKTQEILSELPFKQGLLEFVDITATSDMSEIQDYL QQLTGARTVPRVFLGKDCIGGCSDLIAMQEKGELLARLKEMGALRQ
GDBY S69570 JQ1612 A35492 31-Dec-1990 13-Mar-1997 05-Nov-1999
glutaredoxin protein YDR513w thioltransferase yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Dietrich, F.S. submitted to the EMBL Data Library August1995 The sequence of S. cerevisiae cosmids 8166, 9787, 9717, and lambda 3073. S69570 DNA 1-143 EMBLU33057 NIDg927764 PIDNAAB64953.1 PIDg927781 GSPDBGN00004 MIPSYDR513w Gan, Z.R. Biochem. Biophys. Res. Commun. 1871992949-955 Cloning and sequencing of a gene encoding yeast thioltransferase. MUID92412147 JQ1612 DNA 35-143 GBS45268 NIDg256162 PIDNAAB23389.1 PIDg256163 strain DMY6 Gan, Z.R. Polokoff, M.A. Jacobs, J.W. Sardana, M.K. Biochem. Biophys. Res. Commun. 1681990944-951 Complete amino acid sequence of yeast thioltransferase (glutaredoxin). MUID90267489 A35492 protein 36-141 SGDTTR1 SGDGRX2 MIPSYDR513w SGDS0002921 MIPSYDR513w 4R thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions glutaredoxin glutaredoxin homology acetylated amino end cytosol electron transfer redox-active disulfide product glutaredoxin 36-141 experimental domain glutaredoxin homology 43-138 modified-site acetylated amino end (Val) (in mature form) 36 experimental disulfide-bonds redox-active 61-64 predicted 143 complete METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTY CPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIG GNSDLETLKKNGKLAEILKPVFQ
S19363 S19363 20-Apr-2000 20-Apr-2000 16-Jun-2000
glutaredoxin GRX1 protein YCL035c thioltransferase yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Hollenberg, C.P. Kleinhans, U. Lutzenkirchen, K. Ramezani Rad, M. Xu, G. submitted to the Protein Sequence Database March1992 S19363 DNA 1-110 EMBLX59720 NIDg1907116 PIDNCAA42381.1 PIDg5328 GSPDBGN00003 MIPSYCL035c GRX1 SGDS0000540 MIPSYCL035c 3L thioltransferase catalyzes cellular thiol-disulfide transhydrogenation reactions; required for protection during oxidative stress glutaredoxin glutaredoxin homology electron transfer redox-active disulfide domain glutaredoxin homology 9-104 disulfide-bonds redox-active 27-30 predicted 110 complete MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGA DIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN
GDEC A00283 A24397 I59418 A64823 A39568 19-Feb-1984 19-Feb-1984 11-Jun-1999
glutaredoxin 1 thioltransferase Escherichia coli Escherichia coli Hoeoeg, J.O. Joernvall, H. Holmgren, A. Carlquist, M. Persson, M. Eur. J. Biochem. 1361983223-232 The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol. MUID84004402 A00283 protein 1-85 K-12, strain C10-17 Hoeoeg, J.O. von Bahr-Lindstroem, H. Joernvall, H. Holmgren, A. Gene 43198613-21 Cloning and expression of the glutaredoxin (grx) gene of Escherichia coli. MUID87005940 A24397 DNA 1-85 GBM13449 NIDg146272 PIDNAAA23936.1 PIDg146273 Chatterjee, P.K. Sternberg, N.L. Proc. Natl. Acad. Sci. U.S.A. 9219958950-8954 A general genetic approach in Escherichia coli for determining the mechanism(s) of action of tumoricidal agents: application to DMP 840, a tumoricidal agent. MUID96004656 I59418 preliminary translated from GB/EMBL/DDBJ DNA 1-85 EMBLU18655 NIDg609323 PIDNAAC43449.1 PIDg609325 Blattner, F.R. Plunkett III, G. Bloch, C.A. Perna, N.T. Burland, V. Riley, M. Collado-Vides, J. Glasner, J.D. Rode, C.K. Mayhew, G.F. Gregor, J. Davis, N.W. Kirkpatrick, H.A. Goeden, M.A. Rose, D.J. Mau, B. Shao, Y. Science 27719971453-1462 The complete genome sequence of Escherichia coli K-12. MUID97426617 A64823 nucleic acid sequence not shown translation not shown DNA 1-85 GBAE000187 GBU00096 NIDg1787070 PIDNAAC73936.1 PIDg1787073 UWGPb0849 strain K-12, substrain MG1655 Sandberg, V.A. Kren, B. Fuchs, J.A. Woodward, C. Biochemistry 3019915475-5484 Escherichia coli glutaredoxin: cloning and overexpression, thermodynamic stability of the oxidized and reduced forms, and report of an N-terminal extended species. MUID91242463 A39568 preliminary DNA 'MRREI',1-15 grxA grx 19 min the disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides from ribonucleotides by the enzyme ribonucleotide reductase; in addition, it is also involved in reducing some disulfides in a coupled system with glutathione reductase deoxyribonucleotide biosynthesis glutaredoxin glutaredoxin homology deoxyribonucleotide biosynthesis electron transfer monomer redox-active disulfide domain glutaredoxin homology 1-85 disulfide-bonds redox-active 11-14 experimental 85 complete MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVP QIFVDQQHIGGYTDFAAWVKENLDA
I64127 I64127 10-Sep-1999 10-Sep-1999 10-Sep-1999
glutaredoxin Haemophilus influenzae (strain Rd KW20) Haemophilus influenzae Fleischmann, R.D. Adams, M.D. White, O. Clayton, R.A. Kirkness, E.F. Kerlavage, A.R. Bult, C.J. Tomb, J.F. Dougherty, B.A. Merrick, J.M. McKenney, K. Sutton, G. FitzHugh, W. Fields, C. Gocayne, J.D. Scott, J. Shirley, R. Liu, L.I. Glodek, A. Kelley, J.M. Weidman, J.F. Phillips, C.A. Spriggs, T. Hedblom, E. Cotton, M.D. Utterback, T.R. Hanna, M.C. Nguyen, D.T. Saudek, D.M. Brandon, R.C. Fine, L.D. Fritchman, J.L. Fuhrmann, J.L. Geoghagen, N.S.M. Gnehm, C.L. McDonald, L.A. Small, K.V. Fraser, C.M. Smith, H.O. Venter, J.C. Science 2691995496-512 Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. MUID95350630 I64127 nucleic acid sequence not shown translation not shown DNA 1-87 GBU32829 GBL42023 NIDg1574375 PIDNAAC23182.1 PIDg1574376 TIGRHI1532 named as homolog to a protein from Escherichia coli glutaredoxin glutaredoxin homology deoxyribonucleotide biosynthesis electron transfer redox-active disulfide disulfide-bonds redox-active 11-14 predicted 87 complete MFVVIFGRPGCPYCVRAKNLAEKLKGEVADFDYRYVDIHAEGITKEDLSKSVGKPVETVP QIFIDEKPIGGCTDFEALMKEQFGIVA
TXBPT4 A00282 G30292 07-May-1981 07-May-1981 15-Sep-2000
thioredoxin [validated] glutaredoxin phage T4 phage T4 Sjoberg, B.M. Holmgren, A. J. Biol. Chem. 24719728063-8068 Studies on the structure of T4 thioredoxin. II. Amino acid sequence of the protein and comparison with thioredoxin from Escherichia coli. MUID73061516 A00282 protein 1-87 Tomaschewski, J. Rueger, W. Nucleic Acids Res. 1519873632-3633 Nucleotide sequence and primary structures of gene products coded for by the T4 genome between map positions 48.266 kb and 39.166 kb. MUID87203398 G30292 DNA 1-87 GBAF158101 NIDg5508842 PIDNAAD42626.1 PIDg5354419 Eklund, H. Ingelman, M. Soderberg, B.O. Uhlin, T. Nordlund, P. Nikkola, M. Sonnerstam, U. Joelson, T. Petratos, K. submitted to the Brookhaven Protein Data Bank April1992 PDB1AAZ annotation X-ray crystallography, 2.0 angstroms, residues 1-87 Soderberg, B.O. Sjoberg, B.M. Sonnerstam, U. Branden, C.I. Proc. Natl. Acad. Sci. U.S.A. 7519785827-5830 Three-dimensional structure of thioredoxin induced by bacteriophage T4. MUID79096070 annotation X-ray crystallography, 2.8 angstroms The name thioredoxin, assigned to this protein before glutaredoxin was discovered, should probably be regarded as a misnomer. nrdC reduced by NADPH and thioredoxin reductase, and oxidized by ribonucleotide reductase deoxyribonucleotide biosynthesis oxidized T4 thioredoxin can be reduced by host thioredoxin reductase, but reduced T4 thioredoxin functions efficiently only with phage ribonucleotide reductase glutaredoxin glutaredoxin homology deoxyribonucleotide biosynthesis electron transfer redox-active disulfide domain glutaredoxin homology 1-87 atypical disulfide-bonds redox-active 14-17 experimental 87 complete MFKVYGYDSNIHKCVYCDNAKRLLTVKKQPFEFINIMPEKGVFDDEKIAELLTKLGRDTQ IGLTMPQVFAPDGSHIGGFDQLREYFK
E42510 E42510 PN0120 T37337 10-Sep-1999 10-Sep-1999 18-Feb-2000
glutaredoxin 1 12K protein O2L protein vaccinia virus (strains Copenhagen, Ankara and L-IVP) vaccinia virus host Homo sapiens (man) Johnson, G.P. submitted to GenBank June1990 E42510 preliminary DNA 1-108 GBM35027 NIDg335317 PIDNAAA48055.1 PIDg335403 strain Copenhagen, strain L-IVP Rjazankina, O.I. Shchelkunov, S.N. Muravlev, A.I. Netesova, N.A. Mikrjukov, N.N. Gutorov, V.V. Nikulin, A.E. Kulichkov, V.A. Malygin, E.G. Mol. Biol. (Mosk.) 241990968-976 The molecular biological study of vaccinia virus genome II; localization and fine structure of the vaccinia virus genes encoding 36K and 12K polypeptides. MUID91066899 PN0120 DNA 1-108 strain L-IVP Antoine, G. Scheiflinger, F. Falkner, F.G. Dorner, F. submitted to the EMBL Data Library March1997 The complete genomic sequence of the Modified Vaccinia Ankara (MVA) strain. T37337 preliminary translated from GB/EMBL/DDBJ DNA 1-108 EMBLU94848 PIDNAAB96432.1 strain Ankara MVA061L glutaredoxin glutaredoxin homology deoxyribonucleotide biosynthesis electron transfer redox-active disulfide domain glutaredoxin homology 5-99 disulfide-bonds redox-active 23-26 predicted 108 complete MAEEFVQQRLANNKVTIFVKYTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENELRDY FEQITGGRTVPRIFFGKTSIGGYSDLLEIDNMDALGDILSSIGVLRTC
G36842 S33069 G36842 10-Sep-1999 10-Sep-1999 10-Sep-1999
glutaredoxin Q2L protein variola virus (strain India-1967) variola virus Shchelkunov, S.N. Blinov, V.M. Totmenin, A.V. Marennikova, S.S. Kolykhalov, A.A. Frolov, I.V. Chizhikov, V.E. Gytorov, V.V. Gashikov, P.V. Belanov, E.F. Belavin, P.A. Resenchuk, S.M. Andzhaparidze, O.G. Sandakhchiev, L.S. Virus Res. 27199325-35 Nucleotide sequence analysis of variola virus HindIII M, L, I genome fragments. MUID93190624 S33069 preliminary nucleic acid sequence not shown translation not shown DNA 1-108 EMBLX67119 NIDg62330 PIDNCAA47554.1 PIDg62331 the nucleotide sequence was submitted to the EMBL Data Library, April 1992 Blinov, V.M. submitted to GenBank November1992 G36842 preliminary DNA 1-108 GBX69198 NIDg456758 PIDNCAA48995.1 PIDg297235 glutaredoxin glutaredoxin homology deoxyribonucleotide biosynthesis electron transfer redox-active disulfide domain glutaredoxin homology 5-99 disulfide-bonds redox-active 23-26 predicted 108 complete MAEEFVQQRLTNNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIVDIKEFKPENKLHDY FEQITGGRTVPRIFFGKTSIGGYSDLLEIDNMDALGDILSSIGVLRTC
S45869 S45869 10-Sep-1999 10-Sep-1999 22-Oct-1999
glutaredoxin homolog YBR014c hypothetical protein YBR0219 yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Entian, K.D. Koetter, P. Rose, M. Li, Z. Thermann, R. Brendel, M. Baur, A. Boles, E. Miosga, T. Schaaff-Gerstenschlaeger, I. Zimmermann, F.K. submitted to the Protein Sequence Database August1994 S45869 DNA 1-203 EMBLZ35883 NIDg536211 PIDNCAA84956.1 PIDg536212 GSPDBGN00002 MIPSYBR014c strain S288C MIPSYBR014c 2R probable membrane protein YDL010W glutaredoxin homology transmembrane protein domain transmembrane 8-30 predicted domain glutaredoxin homology 91-184 203 complete MAIVINKRNVRVLVITNLLLIVVFFVLRNSNASVNESITTHHPDSLVTFDNSGNAPGTHQ SVHDTVNTQDKEAEEVDKNSGDAEFDAAAEYNKIMEQSPMIVFSKTGCPYSKKLKALLTN SYTFSPSYYVVELDRHEHTKELQDQIEKVTGRRTVPNVIIGGTSRGGYTEIAELHKNDEL LDSFKKWSDGAFTVKANSQSESA
S52509 S52509 S67542 10-Sep-1999 10-Sep-1999 16-Jun-2000
probable membrane protein YDL010w hypothetical protein D2890 yeast (Saccharomyces cerevisiae) Saccharomyces cerevisiae Andre, B. Vissers, S. Urrestarazu, L. submitted to the EMBL Data Library February1995 The sequence of a 42 kb segment located on the left arm of chromosome IV from Saccharomyces cerevisiae. S52509 DNA 1-231 EMBLZ48432 NIDg683669 PIDNCAA88349.1 PIDg683687 strain S288C Urrestarazu, L.A. Andre, B. Vissers, S. submitted to the Protein Sequence Database July1996 S67542 DNA 1-231 EMBLZ74059 NIDg1430970 PIDNCAA98567.1 PIDg1430972 GSPDBGN00004 MIPSYDL010w strain S288C MIPSYDL010w 4L probable membrane protein YDL010W glutaredoxin homology transmembrane protein domain transmembrane 11-27 predicted domain glutaredoxin homology 119-212 231 complete MIPSNKRNARILSITTLLLLLVFFVAQNANFLTVEIKEETSKAFSTNMDNMAGGSSREYA AMPTSTTNKGSSEVDEEINEIKQKVGLQQPIASVDDSLSAIKNDKGSRITKAFNVQKEYS LILDLSPIIIFSKSTCSYSKGMKELLENEYQFIPNYYIIELDKHGHGEELQEYIKLVTGR GTVPNLLVNGVSRGGNEEIKKLHTQGKLLESLQVWSDGKFSVEQREKPSNN
AZBR A00284 07-May-1981 07-May-1981 20-Apr-2000
azurin Bordetella bronchiseptica Bordetella bronchiseptica Ambler, R.P. Chemotaxonomy and Serotaxonomy, Hawkes, J.G., ed., pp.57-64, Academic Press, London 1968 Species differences in the amino acid sequences of bacterial proteins. A00284 protein 1-129 strain NCTC 8344 plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 predicted binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 predicted 129 complete AECSVDIAGTDQMQFDKKAIEVSKSCKQFTVNLKHTGKLPRNVMGHNWVLTKTADMQAVE KDGIAAGLDNQYLKAGDTRVLAHTKVLGGGESDSVTFDVAKLAAGDDYTFFCSFPGHGAL MKGTLKLVD
AZALCX A00285 07-May-1981 07-May-1981 20-Apr-2000
azurin Alcaligenes sp. Alcaligenes sp. Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A00285 protein 1-129 the author assigned the amides at positions 10, 14, and 47 by homology Stanier, R.Y. unpublished results, cited by Ambler, R.P., submitted to the Atlas, December 1972 1972 annotation this organism, previously called Pseudomonas denitrificans by some workers, was characterized as a species of Alcaligenes plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 predicted binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 predicted 129 complete tentative AECSVDIAGN(D.Q)MQFDKKEITVSKSCKQFTVNLKHPGKLAKN(V.M)GHN(W.V.L) TKQADMQGAV(N.D.G)MAAGLDNNYVKKDDARVIAHTKVIGGGETDSVTFDVSKLAAGE DYAYFCSFPGHFALMKGVLKLVD
AZALCD JQ0643 A00286 24-Apr-1984 27-Jan-1995 15-Sep-2000
azurin precursor [validated] Alcaligenes denitrificans Alcaligenes denitrificans Hoitink, C.W.G. Woudt, L.P. Turenhout, J.C.M. van de Kamp, M. Canters, G.W. Gene 90199015-20 Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis. MUID90337337 JQ0643 DNA 1-149 GBM30388 NIDg141901 PIDNAAA21954.1 PIDg141902 strain NCTC8582 Ambler, R.P. submitted to the Atlas July1974 A00286 protein 21-61,'AV',64-76,'E',78-149 NCIB 8582 Baker, E.N. Shepard, W.E.B. Kingston, R.L. submitted to the Brookhaven Protein Data Bank December1992 PDB1AZC annotation X-ray crystallography, 1.8 angstroms, reduced form, residues 21-149 Baker, E.N. Norris, G.E. submitted to the Brookhaven Protein Data Bank October1986 PDB2AZA annotation X-ray crystallography, 1.8 angstroms, oxdized form, residues 21-15,'D',17-41,'S',43-76,'E',78-149 Baker, E.N. J. Mol. Biol. 20319881071-1095 Structure of azurin from Alcaligenes denitrificans refinement at 1.8 Angstroms resolution and comparison of the two crystallographically independent molecules. MUID89094855 annotation X-ray crystallography, 1.8 angstroms Norris, G.E. Anderson, B.F. Baker, E.N. J. Mol. Biol. 1651983501-521 Structure of azurin from Alcaligenes denitrificans at 2.5 Angstrom resolution. MUID83189162 annotation X-ray crystallography, 2.5 angstroms Azurin is thought to transfer electrons from cytochrome c551 to cytochrome oxidase. azu plastocyanin copper electron transfer metalloprotein domain signal sequence 1-20 predicted product azurin 21-149 experimental disulfide-bonds 23-46 experimental binding-site copper (His, Cys, His, Met) (type 1) 66,132,137,141 experimental 149 complete MLAKATLAIVLSAASLPVLAAQCEATIESNDAMQYNLKEMVVDKSCKQFTVHLKHVGKMA KVAMGHNWVLTKEADKQGVATDGMNAGLAQDYVKAGDTRVIAHTKVIGGGESDSVTFDVS KLTPGEAYAYFCSFPGHWAMMKGTLKLSN
A58648 A58648 10-Sep-1999 10-Sep-1999 15-Sep-2000
azurin II [validated] Alcaligenes denitrificans subsp. xylosoxydans Alcaligenes denitrificans subsp. xylosoxydans Dodd, F.E. Hasnain, S.S. Abraham, Z.H.L. Eady, R.R. Smith, B.E. submitted to the Brookhaven Protein Data Bank March1995 PDB1ARN sequence X-ray crystallography, 2.1 angstroms A58648 protein 1-129 NCIMB 11015 plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 experimental binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 experimental 129 complete AQCEATVESNDAMQYNVKEIVVDKSCKQFTMHLKHVGKMAKVAMGHNLVLTKDADKQAVA TDGMGAGLAQDYVKAGDTRVIAHTKVIGGGESDSVTFDVSKIAAGENYAYFCSFPGHWAM MKGTLKLGS
AZALCF A00287 13-Jul-1981 13-Jul-1981 20-Apr-2000
azurin Alcaligenes faecalis Alcaligenes faecalis Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A00287 protein 1-128 NCIB 8156 the author assigned the amide at position 13 by homology plastocyanin copper electron transfer metalloprotein disulfide-bonds 2-25 predicted binding-site copper (His, Cys, His, Met) (type 1) 45,111,116,120 predicted 128 complete tentative ACDVSIEGNDSMQFNTKSIVVDKTCKEFTINLKH(T.G)KLPKAAMG(H.N.V.V.V.S) KKSDES(A,V,A,T.D.G)MKAGLNNDYVKAGDERVIAHT(S,V.I.G.G,G)ETDSVTF DVSKLKEGEDYAFFCSFPGHWSIM(K,G.T,I.E)LGS
AZPSCA JQ0644 S02268 A29339 A94436 H83030 A00288 24-Apr-1984 31-Mar-1993 31-Dec-2000
azurin precursor [validated] Pseudomonas aeruginosa Pseudomonas aeruginosa Hoitink, C.W.G. Woudt, L.P. Turenhout, J.C.M. van de Kamp, M. Canters, G.W. Gene 90199015-20 Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis. MUID90337337 JQ0644 DNA 1-148 GBM30389 NIDg151060 PIDNAAA25730.1 PIDg151062 Arvidsson, R.H.A. Nordling, M. Lundberg, L.G. Eur. J. Biochem. 1791989195-200 The azurin gene from Pseudomonas aeruginosa. Cloning and characterization. MUID89137081 S02268 DNA 1-148 EMBLX07317 NIDg45291 PIDNCAA30279.1 PIDg45292 Canters, G.W. FEBS Lett. 2121987168-172 The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene. MUID87105995 A29339 not compared with conceptual translation DNA 1-148 Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A94436 protein 21-148 strain P6009 Nar, H. Messerschmidt, A. Huber, R. submitted to the Brookhaven Protein Data Bank June1993 PDB4AZU annotation X-ray crystallography, 1.9 angstroms, pH 5.5, residues 21-148 Nar, H. Messerschmidt, A. Huber, R. submitted to the Brookhaven Protein Data Bank June1993 PDB5AZU annotation X-ray crystallography, 1.9 angstroms, pH 9.0, residues 21-148 Nar, H. Messerschmidt, A. Huber, R. van de Kamp, M. Canters, G.W. J. Mol. Biol. 2211991765-772 Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip. MUID92046032 annotation X-ray crystallography, 1.93 angstroms Adman, E.T. Sieker, L.C. Jensen, L.H. submitted to the Brookhaven Protein Data Bank August1980 PDB1AZU annotation X-ray crystallography, 2.7 angstroms, residues 23-148 Adman, E.T. Stenkamp, R.E. Sieker, L.C. Jensen, L.H. J. Mol. Biol. 123197835-47 A crystallographic model for azurin at 3 angstrom resolution. MUID78244655 annotation X-ray crystallography, 3.0 angstroms Stover, C.K. Pham, X.Q. Erwin, A.L. Mizoguchi, S.D. Warrener, P. Hickey, M.J. Brinkman, F.S.L. Hufnagle, W.O. Kowalik, D.J. Lagrou, M. Garber, R.L. Goltry, L. Tolentino, E. Westbrook-Wadman, S. Yuan, Y. Brody, L.L. Coulter, S.N. Folger, K.R. Kas, A. Larbig, K. Lim, R.M. Smith, K.A. Spencer, D.H. Wong, G.K.S. Wu, Z. Paulsen, I.T. Reizer, J. Saier, M.H. Hancock, R.E.W. Lory, S. Olson, M.V. Nature 4062000959-964 Complete genome sequence of Pseudomonas aeruginosa PA01, an opportunistic pathogen. MUID20437337 H83030 preliminary DNA 1-148 GBAE004905 GBAE004091 NIDg9951195 PIDNAAG08307.1 GSPDBGN00131 PASPPA4922 strain PAO1 azu PA4922 plastocyanin copper electron transfer metalloprotein domain signal sequence 1-20 predicted product azurin 21-148 experimental disulfide-bonds 23-46 experimental binding-site copper (His, Cys, His, Met) (type 1) 66,132,137,141 experimental 148 complete MLRKLAAVSLLSLLSAPLLAAECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP KNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVS KLKEGEQYMFFCTFPGHSALMKGTLTLK
AZPSCD A00289 13-Jul-1981 13-Jul-1981 20-Apr-2000
azurin Pseudomonas sp. Pseudomonas sp. Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A00289 protein 1-128 ATCC 13867, NCIB 9496 the author assigned the amide and acid at positions 57 and 62 by homology plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 predicted binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 predicted 128 complete tentative AECSVDIQGNDQMQFSTNAITVDKACK(T.F)TVNLSHPGSLPK(N.V.M)GHNWVL(T. T.A.A.D.M)QGVVTD(G.M)AAGLDKNYVKDGDTRVIAHTKIIGSGEKDSVTFDVSKLK AGDAYAFFCSFPGHSAMMKGTLTLK
AZPSBF A00290 07-May-1981 07-May-1981 20-Apr-2000
azurin Pseudomonas fluorescens (biotype B) Pseudomonas fluorescens Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A00290 protein 1-128 Stanier B-93; ATCC 17467 the author assigned the amides and acid at positions 11, 12, and 57 by homology plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 predicted binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 predicted 128 complete tentative AECKTTIDSTDQMSFNTKAIEIDKACKTFTVEL(T,H.S,G.S,L.P.K=N.V.M)GHNL V(I.S.K.Q.A.D)MQPIA(T.D.G)LSAGIDKNYLKEGDTRVIAHTKVIGAGEKDSLTI D(V.S)KLNAAEKYGFFCSF(P.G.H)ISMMKGTVTLK
AZPSCF A00291 07-May-1981 07-May-1981 20-Apr-2000
azurin Pseudomonas fluorescens (biotype C) Pseudomonas fluorescens Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A00291 protein 1-128 Stanier C-18; ATCC 17400 the author assigned the amide and acids at positions 8, 11, 12, and 55 by homology plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 predicted binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 predicted 128 complete tentative AECK(V.T)VDSTDQMSFDTKAIEIDKSCKTFTVDLKH(S,G.N,L.P.K)N(V.M)GHN WVLTTQADMQPVATDGMAAGIDKNYLKEGDTRIIAHTKIIGAGETDS(V.T.F)DVSKLK ADGKYMFFCSFPG(H.I.A)MMKGTVTLK
AZPSDF A00292 07-May-1981 07-May-1981 20-Apr-2000
azurin Pseudomonas fluorescens (biotype D) Pseudomonas fluorescens Ambler, R.P. Recent Developments in the Chemical Study of Protein Structures, pp.289-305, INSERM, Paris 1971 A00292 protein 1-128 Stanier D-35; ATCC 17414 plastocyanin copper electron transfer metalloprotein disulfide-bonds 3-26 predicted binding-site copper (His, Cys, His, Met) (type 1) 46,112,117,121 predicted 128 complete tentative AECKVDVDSTDQMSFNTKEITIDKSCKTFTVNLTHS(G.S.L.P)KN(V.M)GHNWVLSK SADMAGIAT(D.G)MAAGIDKDYLKPGDSRVIAHTKIIGSGEKDSVTFDVSKLTAGESYE FFCSF(P.G.H.N)SMMKGAVVLK
AZNHM S03752 31-Mar-1993 31-Mar-1993 20-Apr-2000
azurin precursor H.8 antigen outer membrane protein H.8 Neisseria meningitidis Neisseria meningitidis Kawula, T.H. Spinola, S.M. Klapper, D.G. Cannon, J.G. Mol. Microbiol. 11987179-185 Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria. MUID88216161 S03752 DNA 1-183 EMBLY00530 NIDg45041 PIDNCAA68589.1 PIDg45042 plastocyanin blocked amino end copper electron transfer lipoprotein metalloprotein domain signal sequence 1-17 predicted product azurin 18-183 predicted region alanine/proline-rich 22-56 modified-site fatty acylated amino end (Cys) (in mature form) 18 predicted binding-site sn-2,3-diacylglycerol (Cys) (covalent) 18 predicted disulfide-bonds 59-82 predicted binding-site copper (His, Cys, His, Met) (type 1) 102,166,171,175 predicted 183 complete MKAYLALISAAVIGLAACSQEPAAPAAEATPAAEAPASEAPAAEAAPADAAEAPAAGNCA ATVESNDNMQFNTKDIQVSKACKEFTITLKHTGTQPKASMGHNLVIAKAEDMDGVFKDGV GAADTDYVKPDDARVVAHTKLIGGGEESSLTLDPAKLADGDYKFACTFPGHGALMNGKVT LVD
AZNHG S06374 31-Mar-1993 31-Mar-1993 20-Apr-2000
azurin precursor H.8 antigen outer membrane protein H.8 Neisseria gonorrhoeae Neisseria gonorrhoeae Gotschlich, E.C. Seiff, M.E. FEMS Microbiol. Lett. 431987253-255 Identification and gene structure of an azurin-like protein with a lipoprotein signal peptide in Neisseria gonorrhoeae. S06374 DNA 1-183 EMBLX06208 NIDg44841 PIDNCAA29561.1 PIDg44842 plastocyanin blocked amino end copper electron transfer lipoprotein metalloprotein domain signal sequence 1-17 predicted product azurin 18-183 predicted region alanine/proline-rich 22-56 modified-site fatty acylated amino end (Cys) (in mature form) 18 predicted binding-site sn-2,3-diacylglycerol (Cys) (covalent) 18 predicted disulfide-bonds 59-82 predicted binding-site copper (His, Cys, His, Met) (type 1) 102,166,171,175 predicted 183 complete MKAYLALISAAVIGLAACSQEPAAPAAEATPAGEAPASEAPAAEAAPADAAEAPAAGNCA ATVESNDNMQFNTKDIQVSKACKEFTITLKHTGTQPKASMGHNLVIAKAEDMDGVFKDGV GAADTDYVKPDDARVVAHTKLIGGGEESSLTLDPAKLADGDYKFACTFPGHGALMNGKVT LVD
A23706 S19732 A23706 10-Sep-1999 10-Sep-1999 10-Sep-1999
amicyanin amine dehydrogenase amicyanin component Thiobacillus versutus Thiobacillus versutus Ubbink, M. van Kleef, M.A.G. Kleinjan, D.J. Hoitink, C.W.G. Huitema, F. Beintema, J.J. Duine, J.A. Canters, G.W. Eur. J. Biochem. 20219911003-1012 Cloning, sequencing and expression studies of the genes encoding amicyanin and the beta-subunit of methylamine dehydrogenase from Thiobacillus versutus. MUID92111471 S19732 preliminary DNA 1-132 GBM58001 NIDg154632 PIDNAAA50571.1 PIDg154635 Van Beeumen, J. Van Bun, S. Canters, G.W. Lommen, A. Chothia, C. J. Biol. Chem. 26619914869-4877 The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins. MUID91161570 A23706 preliminary protein 28-132 plastocyanin copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 80,119,122,125 predicted 132 complete MISAKTLRPAIAAIALFAIGATGAWAQDKITVTSEKPVAAADVPADAVVVGIEKMKYLTP EVTIKAGETVYWVNGEVMPHNVAFKKGIVGEDAFRGEMMTKDQAYAITFNEAGSYDYFCT PHPFMRGKVIVE
S12972 S12972 10-Sep-1999 10-Sep-1999 20-Apr-2000
amicyanin Paracoccus denitrificans Paracoccus denitrificans van Spanning, R.J.M. Wansell, C.W. Reijnders, W.N.M. Oltmann, L.F. Stouthamer, A.H. FEBS Lett. 2751990217-220 Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. MUID91085564 S12972 preliminary DNA 1-131 EMBLX55665 NIDg45458 PIDNCAA39199.1 PIDg45460 plastocyanin copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 79,118,121,124 experimental 131 complete MISATKIRSCLAACVLAAFGATGALADKATIPSESPFAAAEVADGAIVVDIAKMKYETPE LHVKVGDTVTWINREAMPHNVHFVAGVLGEAALKGPMMKKEQAYSLTFTEAGTYDYHCTP HPFMRGKVVVE
CUPSZM A00293 04-Dec-1986 04-Dec-1986 15-Sep-2000
pseudoazurin [validated] Methylobacterium extorquens Methylobacterium extorquens Ambler, R.P. Tobari, J. Biochem. J. 2321985451-457 The primary structures of Pseudomonas AM1 amicyanin and pseudoazurin. Two new sequence classes of blue copper proteins. MUID86130354 A00293 protein 1-123 AM1, NCIB 9133 Inoue, T. Kai, Y. Harada, S. Kasai, N. Ohshiro, Y. Suzuki, S. Kohzuma, T. Tobari, J. submitted to the Brookhaven Protein Data Bank January1994 PDB1PMY annotation X-ray crystallography, 1.5 angstroms, residues 1-123 This species of Pseudomonas, isolated as an airborne contaminant, uses compounds such as methanol, methylamine, and formate as the sole carbon and energy source; it is quite distinct from the true pseudomonads as well as methylotrophs. plastocyanin copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 40,78,81,86 experimental 123 complete DEVAVKMLNSGPGGMMVFDPALVRLKPGDSIKFLPTDKGHNVETIKGMAPDGADYVKTTV GQEAVVKFDKEGVYGFKCAPHYMMGMVALVVVGDKRDNLEAAKSVQHNKLTQKRLDPLFA QIQ
CUALBF A28385 A00294 17-Mar-1987 27-Jan-1995 20-Apr-2000
blue copper protein precursor cupredoxin pseudoazurin Alcaligenes faecalis Alcaligenes faecalis Yamamoto, K. Uozumi, T. Beppu, T. J. Bacteriol. 16919875648-5652 The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells. MUID88058779 A28385 DNA 1-146 GBM18267 NIDg141903 PIDNAAA21955.1 PIDg141904 strain S-6 Hormel, S. Adman, E. Walsh, K.A. Beppu, T. Titani, K. FEBS Lett. 1971986301-304 The amino acid sequence of the blue copper protein of Alcaligenes faecalis. MUID86136586 A00294 protein 24-146 Petratos, K. Banner, D.W. Beppu, T. Wilson, K.S. Tsernoglou, D. FEBS Lett. 2181987209-214 The crystal structure of pseudoazurin from Alcaligenes faecalis S-6 determined at 2.9 angstroms resolution. MUID87247273 annotation strain S-6 Adman, E.T. Turley, S. Bramson, R. Petratos, K. Banner, D. Tsernoglou, D. Beppu, T. Watanabe, H. J. Biol. Chem. 264198987-99 A 2.0-angstrom structure of the blue copper protein (cupredoxin) from Alcaligenes faecalis S-6. MUID89079731 annotation strain S-6 This soluble electron transfer copper protein, required for the inactivation of copper-containing nitrite reductase in the presence of oxygen, belongs to a class of blue proteins that includes pseudoazurin and amicyanin. plastocyanin copper electron transfer metalloprotein domain signal sequence 1-23 predicted product blue copper protein 24-146 experimental binding-site copper (His, Cys, His, Met) (type 1) 63,101,104,109 experimental 146 complete MRNIAIKFAAAGILAMLAAPALAENIEVHMLNKGAEGAMVFEPAYIKANPGDTVTFIPVD KGHNVESIKDMIPEGAEKFKSKINENYVLTVTQPGAYLVKCTPHYAMGMIALIAVGDSPA NLDQIVSAKKPKIVQERLEKVIASAK
JC4649 JC4649 A27039 10-May-1996 10-Oct-1997 15-Sep-2000
pseudoazurin precursor [validated] blue copper protein Achromobacter cycloclastes Achromobacter cycloclastes Chen, J.Y. Chang, W.C. Chang, T. Chang, W.C. Liu, M.Y. Payne, W.J. LeGall, J. Biochem. Biophys. Res. Commun. 2191996423-428 Cloning, characterization, and expression of the nitric oxide-generating nitrite reductase and of the blue copper protein genes of Achromobacter cycloclastes. MUID96193667 JC4649 DNA 1-148 EMBLZ48669 NIDg1125636 PIDg1125637 IAM1013 Petratos, K. Banner, D.W. Beppu, T. Wilson, K.S. Tsernoglou, D. FEBS Lett. 2181987209-214 The crystal structure of pseudoazurin from Alcaligenes faecalis S-6 determined at 2.9 angstroms resolution. MUID87247273 A27039 protein 25-114,'E',116-148 the source may be Vibrio alginolyticus Inoue, T. Nishio, N. Hamanaka, S. Shimomura, T. Harada, S. Suzuki, S. Kohzuma, T. Shidara, S. Iwasaki, H. Kai, Y. submitted to the Brookhaven Protein Data Bank April1996 PDB1ZIA annotation X-ray crystallography, 1.54 angstroms, oxidized form, residues 25-148 Inoue, T. Nishio, N. Hamanaka, S. Shimomura, T. Harada, S. Suzuki, S. Kohzuma, T. Shidara, S. Iwasaki, H. Kai, Y. submitted to the Brookhaven Protein Data Bank April1996 PDB1ZIB annotation X-ray crystallography, 2.0 angstroms, reduced form, residues 25-148 bcp transfers electrons to nitrite reductase plastocyanin copper electron transfer metalloprotein domain signal sequence 1-24 predicted product blue copper protein 25-148 experimental binding-site copper (His, Cys, His, Met) (type 1) 64,102,105,110 experimental 148 complete MLNAIKSGFGIAIAAMLVAAPAAAADFEVHMLNKGKDGAMVFEPASLKVAPGDTVTFIPT DKGHNVETIKGMIPDGAEAFKSKINENYKVTFTAPGVYGVKCTPHYGMGMVGVVQVGDAP ANLEAVKGAKNPKKAQERLDAALAALGN
CUPSAM A56621 A00295 04-Dec-1986 21-Jul-1995 20-Apr-2000
amicyanin precursor Methylobacterium extorquens (strain AM1) Methylobacterium extorquens Chistoserdov, A.Y. Tsygankov, Y.D. Lidstrom, M.E. DNA Seq. 2199153-55 Nucleotide sequence of the amicyanin gene from Methylobacterium extorquens AM1. MUID92199244 A56621 DNA 1-119 GBM57963 NIDg150014 PIDNAAA68895.1 PIDg150016 sequence modified after extraction from NCBI backbone the authors translated the codon CAC for residue 70 as Asn sequence extracted from NCBI backbone (NCBIN:89409, NCBIP:89412) Ambler, R.P. Tobari, J. Biochem. J. 2321985451-457 The primary structures of Pseudomonas AM1 amicyanin and pseudoazurin. Two new sequence classes of blue copper proteins. MUID86130354 A00295 protein 21-119 This species of Pseudomonas, isolated as an airborne contaminant, uses compounds such as methanol, methylamine, and formate as the sole carbon and energy source; it is quite distinct from the true pseudomonads as well as methylotrophs. plastocyanin copper electron transfer metalloprotein periplasmic space domain signal sequence 1-20 predicted product amicyanin 21-119 experimental binding-site copper (His, Cys, His, Met) (type 1) 67,106,109,112 predicted 119 complete MRALAFAAALAAFSATAALAAGALEAVQEAPAGSTEVKIAKMKFQTPEVRIKAGSAVTWT NTEALPHNVHFKSGPGVEKDVEGPMLRSNQTYSVKFNAPGTYDYICTPHPFMKGKVVVE
CUAI A00296 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin Anabaena variabilis Anabaena variabilis Aitken, A. Biochem. J. 1491975675-683 Prokaryote-eukaryote relationships and the amino acid sequence of plastocyanin from Anabaena variabilis. MUID76087796 A00296 protein 1-105 plastocyanin copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 39,89,92,97 predicted 105 complete ETYTVKLGSDKGLLVFEPAKLTIKPGDTVEFLNNKVPPHNVVFDAALNPAKSADLAKSLS HKQLLMSPGQSTSTTFPADAPAGEYTFYCEPHRGAGMVGKITVAG
CUFB A00297 S01778 07-May-1981 07-May-1981 26-May-2000
plastocyanin [validated] kidney bean kidney bean Phaseolus vulgaris Milne, P.R. Wells, J.R.E. Ambler, R.P. Biochem. J. 1431974691-701 The amino acid sequence of plastocyanin from French bean (Phaseolus vulgaris). MUID75183337 A00297 protein 1-99 the source is designated as Phaseolus vulgaris (French bean) Chazin, W.J. Wright, P.E. J. Mol. Biol. 2021988623-636 Complete assignment of the H(1) nuclear magnetic resonance spectrum of french bean plastocyanin. Sequential resonance assignments, secondary structure and global fold. MUID89011985 S01778 protein 1-99 Moore, J.M. Lepre, C.A. Gippert, G.P. Chazin, W.J. Case, D.A. Wright, P.E. submitted to the Brookhaven Protein Data Bank March1991 PDB9PCY annotation conformation by (1)H-NMR, residues 1-99 Moore, J.M. Lepre, C.A. Gippert, G.P. Chazin, W.J. Case, D.A. Wright, P.E. J. Mol. Biol. 2211991533-555 High-resolution solution structure of reduced French bean plastocyanin and comparison with the crystal structure of poplar plastocyanin. MUID92015245 annotation conformation by (1)H-NMR functions as electron carrier [validated; MUID:92015245] plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 experimental 99 complete LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEE ELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN
CUSP S00446 A00299 24-Apr-1984 12-Apr-1996 11-Jun-1999
plastocyanin precursor spinach spinach Spinacia oleracea Rother, C. Jansen, T. Tyagi, A. Tittgen, J. Herrmann, R.G. Curr. Genet. 111986171-176 Plastocyanin is encoded by an uninterrupted nuclear gene in spinach. MUID88194671 S00446 DNA 1-168 EMBLX04693 NIDg21266 PIDNCAA28398.1 PIDg21267 Scawen, M.D. Ramshaw, J.A.M. Boulter, D. Biochem. J. 1471975343-349 The amino acid sequence of plastocyanin from spinach (Spinacia oleracea L.). MUID76039448 A00299 protein 70-168 plastocyanin chloroplast copper electron transfer metalloprotein domain transit peptide (chloroplast) 1-69 predicted product plastocyanin 70-168 predicted binding-site copper (His, Cys, His, Met) (type 1) 106,153,156,161 predicted 168 complete MATVASSAAVAVPSFTGLKASGSIKPTTAKIIPTTTAVPRLSVKASLKNVGAAVVATAAA GLLAGNAMAVEVLLGGGDGSLAFLPGDFSVASGEEIVFKNNAGFPHNVVFDEDEIPSGVD AAKISMSEEDLLNAPGETYKVTLTEKGTYKFYCSPHQGAGMVGKVTVN
CULC A00300 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin garden lettuce garden lettuce Lactuca sativa Ramshaw, J.A.M. Scawen, M.D. Jones, E.A. Brown, R.H. Boulter, D. Phytochemistry 1519761199-1202 The amino acid sequence of plastocyanin from Lactuca sativa (lettuce). A00300 protein 1-99 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete AEVLLGSSDGGLVFEPSTFSVASGEKIVFKNNAGFPHNVVFDEDEIPAGVDASKISMSEE DLLNAPGETYAVTLTEKGTYSFYCAPHQGAGMVGKVTVN
CUED A00301 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin European elder European elder Sambucus nigra Scawen, M.D. Ramshaw, J.A.M. Brown, R.H. Boulter, D. Eur. J. Biochem. 441974299-303 The amino-acid sequence of plastocyanin from Sambucus nigra L. (elder). MUID74308155 A00301 protein 1-99 position 15 is Ile in 60% and Val in 40% of the chains 17-Ser and 17-Gly are found in approximately equal amounts plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete VEILLGGEDGSLAFIPSNFSVPSGEKITFKNNAGFPHNVVFDEDEVPSGVDSAKISMSED DLLNAPGETYSVTLTESGTYKFYCSPHQGAGMVGKVTVN
CUVM A00302 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin field pumpkin field pumpkin, vegetable marrow Cucurbita pepo var. pepo Scawen, M.D. Boulter, D. Biochem. J. 1431974257-264 The amino acid sequence of plastocyanin from Cucurbita pepo L. (vegetable marrow). MUID75183285 A00302 protein 1-99 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete IEVLLGGDDGSLAFIPNDFSVAAGEKIVFKNNAGFPHNVVFDEDEIPSGVDAGKISMNEE DLLNAPGEVYKVNLTEKGSYSFYCSPHQGAGMVGKVTVN
CUKV A00303 18-Apr-1984 18-Apr-1984 31-Mar-2000
plastocyanin cucumber cucumber Cucumis sativus Ramshaw, J.A.M. Felton, A.A. Phytochemistry 2119821317-1320 The amino acid sequence of plastocyanin from Cucumis sativus. A00303 protein 1-99 Plastocyanin, coded by a nuclear gene, is found loosely bound to the inner thylakoid membrane surface in chloroplasts, where it participates in electron transfer between photosystem I and the cytochrome b/f complex. plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete tentative IEILLGGDDGSLAFVPNNFTVASGEKITFKNNAGFPHNVVFDEDEIPSGVDSGK.ISM.N EEDLLBAPGZVYZVZLTZK.GSYSFYCSPHQGAGM.VGKVTVN
CUSU A00304 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin shepherd's purse shepherd's purse Capsella bursa-pastoris Scawen, M.D. Ramshaw, J.A.M. Brown, R.H. Boulter, D. unpublished results, cited by Boulter, D., Haslett, B.G., Peacock, D., Ramshaw, J.A.M., and Scawen, M.D., in Plant Biochemistry II, vol.13, Northcote, D.H., ed., pp.1-40, University Park Press, Baltimore 1977 A00304 protein 1-99 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete IEVLLGGGDGSLAFVPNDFSIAKGEKIVFKNNAGFPHNVVFDEDEIPSGVDASKISMDEN DLLNAAGETYEVALTEAGTYSFYCAPHQGAGMVGKVTVN
CUDM A00305 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin dog's mercury dog's mercury Mercurialis perennis Scawen, M.D. Ramshaw, J.A.M. Brown, R.H. Boulter, D. unpublished results, cited by Boulter, D., Haslett, B.G., Peacock, D., Ramshaw, J.A.M., and Scawen, M.D., in Plant Biochemistry II, vol.13, Northcote, D.H., ed., pp.1-40, University Park Press, Baltimore 1977 A00305 protein 1-99 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete LDVLLGSDDGELAFVPNNFSVPSGEKITFKNNAGFPHNVVFDEDEIPSGVDASKISMDEA DLLNAPGETYAVTLTEKGSYSFYCSPHQGAGMVGKVTVN
CUPO A00306 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin potato potato Solanum tuberosum Ramshaw, J.A.M. Scawen, M.D. Bailey, C.J. Boulter, D. Biochem. J. 1391974583-592 The amino acid sequence of plastocyanin from Solanum tuberosum L. (potato). MUID74308153 A00306 protein 1-99 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete LDVLLGGDDGSLAFIPGNFSVSAGEKITFKNNAGFPHNVVFDEDEIPAGVDASKISMAEE DLLNAAGETYSVTLSEKGTYTFYCAPHQGAGMVGKVTVN
CUUA A00307 03-Aug-1984 03-Aug-1984 20-Feb-1998
plastocyanin Chilean potato-tree Chilean potato-tree Solanum crispum Haslett, B.G. Evans, I.M. Boulter, D. Phytochemistry 171978735-739 Amino acid sequence of plastocyanin from Solanum crispum using automatic methods. A00307 protein 1-99 Plastocyanin, coded by a nuclear gene, is found loosely bound to the inner thylakoid membrane surface in chloroplasts, where it participates in electron transfer between photosystem I and the cytochrome b/f complex. plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete IEVLLGSDDGGLAFVPGNFSISAGEKITFKNNAGFPHNVVFDEDEIPAGVDASKISMPEE DLLNAPGETYSVTLSEKGTYSFYCSPHQGAGMVGKVTVN
CURXCO A90349 A94472 A00308 13-Jul-1981 13-Jul-1981 20-Feb-1998
plastocyanin bitter dock bitter dock Rumex obtusifolius Haslett, B. Bailey, C.J. Ramshaw, J.A.M. Scawen, M.D. Boulter, D. Biochem. Soc. Trans. 219741329-1331 Studies of the amino acid sequence of plastocyanin from Rumex obtusifolius (broad-leaved dock). A90349 protein 1-91,'L',93-99 Ramshaw, J.A.M. Boulter, D. unpublished results, cited by Freeman, H.C., J. Proc. Royal Soc. N.S. Wales 112, 45-62 1979 revision A94472 protein 92 the residue at position 92 is Met, not Leu plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete IEIKLGGDDGALAFVPGSFTVAAGEKIVFKNNAGFPHNIVFDEDEVPAGVDASKISMSEE DLLNAPGETYAVTLSEKGTYSFYCSPHQGAGMVGKVTVQ
CUMUM JA0065 30-Sep-1990 30-Sep-1990 11-Jun-1999
plastocyanin precursor Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana Vorst, O. Oosterhoff-Teertstra, R. Vankan, P. Smeekens, S. Weisbeek, P. Gene 65198859-69 Plastocyanin of Arabidopsis thaliana; isolation and characterization of the gene and chloroplast import of the precursor protein. MUID88284381 JA0065 DNA 1-171 GBM20937 NIDg166789 PIDNAAA32834.1 PIDg166790 plastocyanin chloroplast copper electron transfer metalloprotein domain transit peptide (chloroplast) 1-72 predicted product plastocyanin 73-171 predicted binding-site copper (His, Cys, His, Met) (type 1) 109,156,159,164 predicted 171 complete MAAITSATVTIPSFTGLKLAVSSKPKTLSTISRSSSATRAPPKLALKSSLKDFGVIAVAT AASIVLAGNAMAMEVLLGSDDGSLAFVPSEFTVAKGEKIVFKNNAGFPHNVVFDEDEIPS GVDASKISMDETALLNGAGETYEVTLTEPGSYGFYCAPHQGAGMVGKLTVK
CUQH A24404 30-Sep-1991 30-Sep-1991 20-Feb-1998
plastocyanin precursor white campion white campion, evening lychnis Silene pratensis, Lychnis alba Smeekens, S. de Groot, M. van Binsbergen, J. Weisbeek, P. Nature 3171985456-458 Sequence of the precursor of the chloroplast thylakoid lumen protein plastocyanin. A24404 DNA 1-165 GBX02965 plastocyanin chloroplast copper electron transfer metalloprotein domain transit peptide (chloroplast) 1-66 predicted product plastocyanin 67-165 predicted binding-site copper (His, Cys, His, Met) (type 1) 103,150,153,158 predicted 165 complete MATVTSSAAVAIPSFAGLKASSTTRAATVKVAVATPRMSIKASLKDVGVVVAATAAAGIL AGNAMAAEVLLGSSDGGLAFVPSDLSIASGEKITFKNNAGFPHNDLFDEDEVPAGVDVTK ISMPEEDLLNAPGEEYSVTLTEKGTYKFYCAPHAGAGMVGKVTVN
CUVF A00298 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin fava bean fava bean Vicia faba Ramshaw, J.A.M. Scawen, M.D. Boulter, D. Biochem. J. 1411974835-843 The amino acid sequence of plastocyanin from Vicia faba L. (broad bean). MUID75204778 A00298 protein 1-99 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 37,84,87,92 predicted 99 complete VEVLLGASDGGLAFVPNSFEVSAGDTIVFKNNAGFPHNVVFDEDEIPSGVDAAKISMPEE DLLNAPGETYSVKLDAKGTYKFYCSPHQGAGMVGQVTVN
CUPX S58209 A00309 31-May-1980 31-Oct-1997 15-Sep-2000
plastocyanin a precursor [validated] Lombardy poplar Lombardy poplar Populus nigra var. italica Reichert, J. Jenzelewski, V. Haehnel, W. submitted to the EMBL Data Library July1995 Kinetic studies of recombinant poplar plastocyanins. S58209 mRNA 1-168 EMBLZ50185 NIDg929812 PIDNCAA90564.1 PIDg929813 var. italica Ambler, R. unpublished results, cited by Freeman, H.C., J. Proc. Royal Soc. N.S. Wales 112, 45-62 1979 A00309 protein 70-127,'ZZB',131-168 Guss, J.M. Freeman, H.C. submitted to the Brookhaven Protein Data Bank March1992 PDB1PLC annotation X-ray crystallography, 1.33 angstroms, residues 70-168 Guss, J.M. Freeman, H.C. submitted to the Brookhaven Protein Data Bank September1986 PDB5PCY annotation X-ray crystallography, 1.80 angstroms, residues 70-168 Guss, J.M. Harrowell, P.R. Murata, M. Norris, V.A. Freeman, H.C. J. Mol. Biol. 1921986361-387 Crystal structure analyses of reduced (Cu(I)) poplar plastocyanin at six pH values. MUID87169729 annotation X-ray crystallography, 1.80 angstroms Guss, J.M. Freeman, H.C. J. Mol. Biol. 1691983521-563 Structure of oxidized poplar plastocyanin at 1.6 Angstroms resolution. MUID84010876 annotation X-ray crystallography, 1.60 angstroms Colman, P.M. Freeman, H.C. Guss, J.M. Murata, M. Norris, V.A. Ramshaw, J.A.M. Venkatappa, M.P. Nature 2721978319-324 X-ray crystal structure analysis of plastocyanin at 2.7 angstrom resolution. annotation X-ray crystallography, 2.7 angstroms Plastocyanin is found loosely bound to the inner thylakoid membrane surface in chloroplasts. petE nuclear accepts electrons from cytochrome f and donates electrons to photosystem I plastocyanin chloroplast copper electron transfer membrane-associated protein metalloprotein domain transit peptide (chloroplast) 1-69 predicted product plastocyanin a 70-168 experimental binding-site copper (His, Cys, His, Met) (type 1) 106,153,156,161 experimental 168 complete MATVTSAAVSIPSFTGLKAGSASNAKVSASAKVSASPLPRLSIKASMKDVGAAVVATAAS AMIASNAMAIDVLLGADDGSLAFVPSEFSISPGEKIVFKNNAGFPHNIVFDEDSIPSGVD ASKISMSEEDLLNAKGETFEVALSNKGEYSFYCSPHQGAGMVGKVTVN
CUKLCF A00310 07-May-1981 07-May-1981 20-Feb-1998
plastocyanin Chlorella fusca Chlorella fusca Kelly, J. Ambler, R.P. Biochem. J. 1431974681-690 The amino acid sequence of plastocyanin from Chlorella fusca. MUID75183336 A00310 protein 1-98 plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 38,83,86,91 predicted 98 complete DVTVKLGADSGALVFEPSSVTIKAGETVTWVNNAGFPHNIVFDEDEVPSGANAEALSHED YLNAPGESYSAKFDTAGTYGYFCEPHQGAGMKGTITVQ
CUEI A25055 30-Sep-1991 30-Sep-1991 15-Sep-2000
plastocyanin [validated] green alga (Enteromorpha prolifera) Enteromorpha prolifera Simpson, R.J. Moritz, R.L. Nice, E.C. Grego, B. Yoshizaki, F. Sugimura, Y. Freeman, H.C. Murata, M. Eur. J. Biochem. 1571986497-506 Complete amino acid sequence of plastocyanin from a green alga, Enteromorpha prolifera. MUID86247647 A25055 protein 1-98 Collyer, C.A. Guss, J.M. Freeman, H.C. submitted to the Brookhaven Protein Data Bank September1989 PDB7PCY annotation X-ray crystallography, 1.8 angstroms, residues 1-98 Collyer, C.A. Guss, J.M. Sugimura, Y. Yoshizaki, F. Freeman, H.C. J. Mol. Biol. 2111990617-632 Crystal structure of plastocyanin from a green alga, Enteromorpha prolifera. MUID90172425 annotation X-ray crystallography, 1.8 angstroms Plastocyanin, a copper-containing protein coded by a nuclear gene, is found loosely bound to the inner thylakoid membrane surface in chloroplasts, where it functions as an electron carrier between the P700 of photosystem I and the cytochrome b/f complex. plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 38,83,86,91 experimental 98 complete AAIVKLGGDDGSLAFVPNNITVGAGESIEFINNAGFPHNIVFDEDAVPAGVDADAISAED YLNSKGQTVVRKLTTPGTYGVYCDPHSGAGMKMTITVQ
CUUV JU0073 JW0010 30-Sep-1991 30-Sep-1991 28-Jul-2000
plastocyanin Arasaki's sea lettuce Arasaki's sea lettuce Ulva arasakii Yoshizaki, F. Fukazawa, T. Mishina, Y. Sugimura, Y. J. Biochem. 1061989282-288 Some properties and amino acid sequence of plastocyanin from a green alga, Ulva arasakii. MUID90036775 JU0073 protein 1-98 Plastocyanin, coded by a nuclear gene, is found loosely bound to the inner thylakoid membrane surface in chloroplasts, where it functions as an electron carrier between the P700 of photosystem I and the cytochrome b/f complex. plastocyanin chloroplast copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 38,83,86,91 predicted 98 complete AQIVKLGGDDGALAFVPSKISVAAGEAIEFVNNAGFPHNIVFDEDAVPAGVDADAISYDD YLNSKGETVVRKLSTPGVYGVYCEPHAGAGMKMTITVQ
CUBCRT A40302 31-Mar-1992 31-Mar-1992 20-Apr-2000
rusticyanin Thiobacillus ferrooxidans Thiobacillus ferrooxidans Ronk, M. Shively, J.E. Shute, E.A. Blake II, R.C. Biochemistry 3019919435-9442 Amino acid sequence of the blue copper protein rusticyanin from Thiobacillus ferrooxidans. MUID91369963 A40302 protein 1-155 plastocyanin copper electron transfer metalloprotein binding-site copper (His, Cys, His, Met) (type 1) 85,138,143,148 predicted 155 complete GTLDTTWKEATLPQVKAMLEKDTGKVSGDTVTYSGKTVHVVAAAVLPGFPFPSFEVHDKK NPTLEIPAGATVDVTFINTNKGFGHSFDITKKGPPYAVMPVIDPIVAGTGFSPVPKDGKF GYTDFTWHPTAGTYYYVCQIPGHAATGMFGKIVVK
SSUL A00311 31-May-1979 31-May-1979 08-Dec-1994
stellacyanin Japanese lacquer-tree Japanese lacquer-tree Rhus vernicifera Bergman, C. Gandvik, E.K. Nyman, P.O. Strid, L. Biochem. Biophys. Res. Commun. 7719771052-1059 The amino acid sequence of stellacyanin from the lacquer tree. MUID77266668 A00311 protein 1-107 Bergman, C. Gandvik, E.K. Nyman, P.O. Strid, L. Biochem. Biophys. Res. Commun. 7919771013 annotation erratum Engeseth, H.R. Hermodson, M.A. McMillin, D.R. FEBS Lett. 1711984257-261 A new assignment of the disulfide linkage in stellacyanin. MUID84208877 annotation disulfide bond This is a blue, type 1 copper glycoprotein. plastocyanin copper electron transfer glycoprotein binding-site carbohydrate (Asn) (covalent) 28,60,102 experimental binding-site copper (His, Cys, His, Gln) 46,87,92,97 predicted disulfide-bonds 59-93 experimental 107 complete TVYTVGDSAGWKVPFFGDVDYDWKWASNKTFHIGDVLVFKYDRRFHNVDKVTQKNYQSCN DTTPIASYNTGBBRINLKTVGQKYYICGVPKHCDLGQKVHINVTVRS
BUKV A00312 17-Dec-1982 17-Dec-1982 15-Sep-2000
basic blue protein [validated] cusacyanin phytocyanin plantacyanin cucumber cucumber Cucumis sativus Murata, M. Begg, G.S. Lambrou, F. Leslie, B. Simpson, R.J. Freeman, H.C. Morgan, F.J. Proc. Natl. Acad. Sci. U.S.A. 7919826434-6437 Amino acid sequence of a basic glue protein from cucumber seedlings. A00312 protein 1-96 seedling Guss, J.M. Freeman, H.C. submitted to the Brookhaven Protein Data Bank March1996 PDB2CBP annotation X-ray crystallography, 1.8 angstroms, residues 1-36,'S',38-96 residue 37 was not determined but modeled as Ser Guss, J.M. Merritt, E.A. Phizackerley, R.P. Freeman, H.C. J. Mol. Biol. 2621996686-705 The structure of phytocyanin, the basic blue protein from cucumber, refined at 1.8 Angstroms resolution. MUID97030706 annotation X-ray crystallography, 1.8 angstroms plastocyanin copper electron transfer extracellular protein binding-site copper (His, Cys, His, Met) (type 1) 39,79,84,89 experimental disulfide-bonds 52-85 experimental 96 complete AVYVVGGSGGWTFNTESWPKGKRFRAGDILLFNYNPXMHNVVVVNQGGFSTCNTPAGAKV YTSGRDQIKLPKGQSYFICNFPGHCQSGMKIAVNAL
ARRA3 A00313 28-Feb-1981 30-Jun-1993 25-Oct-1996
allergen Ra3 common ragweed common ragweed Ambrosia artemisiifolia var. elatior Klapper, D.G. Goodfriend, L. Capra, J.D. Biochemistry 1919805729-5734 Amino acid sequence of ragweed allergen Ra3. MUID81110503 A00313 protein 1-40,'D',42-101 the residue identified as 41-Asp is bound to carbohydrate therefore we have shown it as Asn plastocyanin blocked carboxyl end copper electron transfer glycoprotein pollen binding-site carbohydrate (Asn) (covalent) 41 experimental disulfide-bonds 61-88 predicted binding-site carbohydrate (Ser) (covalent) 84 experimental modified-site blocked carboxyl end (Arg) 101 experimental 101 complete GKVYLVGGPELGGWKLQSDPRAYALWSARQQFKTTDVLWFNFTTGEDSVAEVWREEAYHA CDIKDPIRLEPGGPDRFTLLTPGSHFICTKDQKFVACVPGR
SSKV S27034 S26511 30-Sep-1993 30-Sep-1993 15-Sep-2000
cupredoxin [validated] stellacyanin cucumber cucumber Cucumis sativus Mann, K. Schaefer, W. Thoenes, U. Messerschmidt, A. Mehrabian, Z. Nalbandyan, R. FEBS Lett. 3141992220-223 The amino acid sequence of a type I copper protein with an unusual serine- and hydroxyproline-rich C-terminal domain isolated from cucumber peelings. MUID93106154 S27034 protein 1-137 submitted to the Protein Sequence Database, September 1992 Hart, P.J. Nersissian, A.M. Herrmann, R.G. Nalbandyan, R.M. Valentine, J.S. Eisenberg, D. submitted to the Brookhaven Protein Data Bank August1996 PDB1JER annotation X-ray crystallography, 1.6 angstroms, residues 'M',2-109 Cucumis sativus (cucumber) sequence expressed in Escherichia coli Hart, P.J. Nersissian, A.M. Herrmann, R.G. Nalbandyan, R.M. Valentine, J.S. Eisenberg, D. Protein Sci. 519962175-2183 A missing link in cupredoxins: crystal structure of cucumber stellacyanin at 1.6 Angstroms resolution. MUID97084802 annotation X-ray crystallography, 1.6 angstroms plastocyanin copper electron transfer extracellular protein glycoprotein hydroxyproline pyroglutamic acid domain copper binding 1-110 domain carboxyl-terminal 111-137 modified-site pyrrolidone carboxylic acid (Gln) 1 experimental binding-site copper (His, Cys, His, Gln) 46,89,94,99 experimental disulfide-bonds 60-95 experimental binding-site carbohydrate (Asn) (covalent) 109 experimental modified-site 4-hydroxyproline (Pro) (partial) 115,127 experimental modified-site 4-hydroxyproline (Pro) 116,117,121,122,128,129,133,134,136 experimental 137 complete QSTVHIVGDNTGWSVPSSPNFYSQWAAGKTFRVGDSLQFNFPANAHNVHEMETKQSFDAC NFVNSDNDVERTSPVIERLDELGMHYFVCTVGTHCSNGQKLSINVVAANATVSMPPPSSS PPSSVMPPPVMPPPSPS
CFKKA A92297 A91464 A60844 A00314 31-May-1979 02-Apr-1982 15-Sep-2000
C-phycocyanin alpha chain [validated] red alga (Cyanidium caldarium) Cyanidium caldarium Offner, G.D. Brown-Mason, A.S. Ehrhardt, M.M. Troxler, R.F. J. Biol. Chem. 256198112167-12175 Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium. I. Complete amino acid sequence of the alpha subunit. MUID82053081 A92297 protein 1-162 Troxler, R.F. Brown, A.S. Fed. Proc. 381979325B Amino acid sequence of the phycocyanin alpha subunit from the alga, Cyanidium caldarium. A91464 protein 1-48,'Q',50-52,'D',54-60,'Q',62-94,'I',96-100,'A',102-162 Brown, A.S. Offner, G.D. Ehrhardt, M.M. Troxler, R.F. J. Biol. Chem. 25419797803-7811 Phycobilin-apoprotein linkages in the alpha and beta subunits of phycocyanin from the unicellular rhodophyte, Cyanidium caldarium. Amino acid sequences of (35)S-labeled chromopeptides. MUID79239364 A60844 protein 70-94 Stec, B. Troxler, R.F. Teeter, M.M. submitted to the Brookhaven Protein Data Bank June1995 PDB1PHN annotation X-ray crystallography, 1.65 angstroms, residues 1-162 This protein was isolated from the phycobilisomes on the chloroplasts of this unicellular, acido-thermal, eukaryote red alga. heterodimers of alpha and beta (see PIR:CFKKB) chains form larger multimers phycocyanin chloroplast chromoprotein heterodimer photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 84 experimental 162 complete MKTPITEAIAAADNQGRFLSNTELQAVNGRYQRAAASLEAARSLTSNAERLINGAAQAVY SKFPYTSQMPGPQYASSAVGKAKCARDIGYYLRMVTYCLVVGGTGPMDEYLIAGLEEINR TFDLSPSWYVEALNYIKANHGLSGQAANEANTYIDYAINALS
CFMWA A00315 30-Jun-1979 30-Jun-1979 30-Apr-1999
C-phycocyanin alpha chain Fischerella sp. Fischerella sp. Frank, G. Sidler, W. Widmer, H. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 35919781491-1507 The complete amino acid sequence of both subunits of C-phycocyanin from the cyanobacterium Mastigocladus laminosus. MUID79087164 A00315 protein 1-162 the source was designated as Mastigocladus laminosus phycocyanin chromoprotein photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 84 experimental 162 complete VKTPITDAIAAADTQGRFLSNTELQAVNGRYQRAAASLEAARALTANAQRLIDGAAQAVY QKFPYLIQTSGPNYAADARGKSKCARDIGHYLRIITYSLVAGGTGPLDEYLIAGLNEIND AFELSPSWYIEALKYIKANHGLSGQAANEANTYIDYVINALS
CFYCAA A94024 A94017 A60662 A00316 B22972 13-Aug-1986 13-Aug-1986 11-Jun-1999
C-phycocyanin alpha chain Synechococcus sp. (strain PCC 7002) Synechococcus sp. de Lorimier, R. Bryant, D.A. Porter, R.D. Liu, W.Y. Jay, E. Stevens Jr., S.E. Proc. Natl. Acad. Sci. U.S.A. 8119847946-7950 Genes of the alpha and beta subunits of phycocyanin. MUID85088525 A94024 DNA 1-162 GBK02660 NIDg142182 PIDNAAB05344.1 PIDg142184 Pilot, T.J. Fox, J.L. Proc. Natl. Acad. Sci. U.S.A. 8119846983-6987 Cloning and sequencing of the genes encoding the alpha and beta subunits of C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. MUID85063716 A94017 DNA 1-162 GBK02659 NIDg142176 PIDNAAB05342.1 PIDg142178 de Lorimier, R. Guglielmi, G. Bryant, D.A. Stevens Jr., S.E. Arch. Microbiol. 1531990541-549 Structure and mutation of a gene encoding a M-r 33000 phycocyanin-associated linker polypeptide. MUID90314661 A60662 DNA 149-162 GBX81868 NIDg732557 PIDNCAA57456.1 PIDg732558 cpcA phycocyanin chromoprotein photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 84 predicted 162 complete MKTPLTEAVALADSQGRFLSNTELQYLYGRLRQGAFALEAAQTLTAKADTLVNGAAQAVY SKFPYTTSTPGNNFAADQRGKDKCARDIGYYLRMVTYCLVAGGTGPMDEYLIAGVDEINR TFDLSPSWYVEALKHIKANHGLTGDAATETNNYIDYAINALS
CFYCA A29015 S60070 S60075 A00317 18-Dec-1981 02-Jul-1996 11-Jun-1999
C-phycocyanin alpha chain Synechococcus sp. (PCC 6301) Synechococcus sp. PCC 6301 Synechococcus sp. PCC 6301 (ATCC 27144) was named Anacystis nidulans in other culture collections, e.g., CCAP, SAUG, and UTEX Lau, R.H. Alvarado-Urbina, G. Lau, P.C.K. Gene 52198721-29 Phycocyanin alpha-subunit gene of Anacystis nidulans R2: cloning, nucleotide sequencing and expression in Escherichia coli. MUID87248092 Anacystis nidulans A29015 DNA 1-163 GBM16325 NIDg142137 PIDNAAA22051.1 PIDg142139 strain R2 Kalla, S.R. Lind, L.K. Lidholm, J. Gustafsson, P. J. Bacteriol. 17019882961-2970 Transcriptional organization of the phycocyanin subunit gene clusters of the cyanobacterium Anacystis nidulans UTEX 625. MUID88257006 S60070 preliminary nucleic acid sequence not shown translation not shown DNA 1-163 EMBLM94218 NIDg142121 PIDNAAA64527.1 PIDg142123 PCC 6301 source designated as Anacystis nidulans the nucleotide sequence was submitted to the EMBL Data Library, June 1992 S60075 nucleic acid sequence not shown translation not shown DNA 1-163 EMBLM94218 NIDg142121 PIDNAAA64527.1 PIDg142123 the source is designated as Anacystis nidulans the nucleotide sequence was submitted to the EMBL Data Library, June 1992 Walsh, R.G. Wingfield, P. Glazer, A.N. DeLange, R.J. Fed. Proc. 3919801998 A00317 protein 2-53,'D',55-120,'TK',123-157,'IL',160-163 associates with beta chain (see PIR:CFCYB) photon energy transfer from phycoerythrin to allophycocyanin photosynthesis phycocyanin chromoprotein photosynthesis phycocyanobilin product C-phycocyanin alpha chain 2-163 experimental binding-site phycocyanobilin (Cys) (covalent) 85 experimental 163 complete MSKTPLTEAVAAADSQGRFLSSTELQVAFGRFRQAASGLAAAKALANNADSLVNGAANAV YSKFPYTTSTPGNNFASTPEGKAKCARDIGYYLRIVTYALVAGGTGPIDEYLLAGLDEIN KTFDLAPSWYVEALKYIKANHGLSGDSRDEANSYIDYLINALS
CFYCA3 S17735 S31068 S31073 A26703 S27718 S31061 30-Jun-1992 30-Jun-1992 20-Apr-2000
R-phycocyanin II alpha chain Synechococcus sp. Synechococcus sp. Wilson, W.H. Newman, J. Mann, N.H. Carr, N.G. Plant Mol. Biol. 171991931-933 Cloning and sequence analysis of the phycocyanin genes of the marine cyanobacterium Synechococcus sp. WH7803. MUID92003705 S17735 DNA 1-162 EMBLX59809 NIDg48036 PIDNCAA42480.1 PIDg48038 strain WH7803 de Lorimier, R. Wilbanks, S.M. Glazer, A.N. Plant Mol. Biol. 211993225-237 Genes of the R-phycocyanin II locus of marine Synechococcus spp., and comparison of protein-chromophore interactions in phycocyanins differing in bilin composition. MUID93144698 S31068 DNA 1-9,'A',11-20,'N',22-34,'K',36-42,'G',44,'T',46-49,'S',51-52,'SS',55,'T',57-60,'T',62-71,'P',73-75,'A',77,'S',79-87,'I',89-134,'H',136,'Q',138-154,'N',156-161,'T' EMBLM95288 NIDg154551 PIDNAAA27346.1 PIDg154566 strain WH8020 S31073 DNA 1-9,'A',11-20,'N',22-34,'K',36-44,'TS',47-49,'S',51-60,'S',62-75,'A',77-134,'H',136-137,'A',139-162 EMBLM95289 NIDg154605 PIDNAAA27366.1 PIDg154607 strain WH8103 Ong, L.J. Glazer, A.N. J. Biol. Chem. 26219876323-6327 R-phycocyanin II, a new phycocyanin occurring in marine Synechococcus species. Identification of the terminal energy acceptor bilin in phycocyanins. MUID87194855 A26703 protein 2-9,'A',11-20,'N';84-86 cpcA rpcA phycocyanin chromoprotein photosynthesis phycocyanobilin product R-phycocyanin II alpha chain 2-162 predicted binding-site phycocyanobilin (Cys) (covalent) 84 predicted 162 complete MKTPLTEAVSAADSQGRFLSSTEVQAASGRFNRAAASLEAAKALSAKADALVNGAAQAVY NKFPYTTQMEGSNYSTTPEGKAKCSRDVGYYLRMITYCLVAGGTGPMDDYLIAGLDEINR TFELSPSWYVEALKYIKSNHGLSGDAATEANSYIDYAINALI
RFMWA JQ0764 A00318 03-Aug-1984 03-Aug-1984 29-Sep-1999
phycoerythrocyanin alpha chain Fischerella sp. Fischerella sp. Eberlein, M. Kufer, W. Gene 941990133-136 Genes encoding both subunits of phycoerythrocyanin, a light-harvesting biliprotein from the cyanobacterium Mastigocladus laminosus. MUID91033055 JQ0764 DNA 1-162 GBM34254 NIDg149774 PIDNAAC64654.1 PIDg149776 Fuglistaller, P. Suter, F. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 3641983691-712 The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus. MUID83289130 A00318 protein 1-162 the source is designated as Mastigocladus laminosus Duerring, M. Huber, R. Bode, W. Ruembeli, R. Zuber, H. J. Mol. Biol. 2111990633-644 Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A. MUID90172426 annotation X-ray crystallography, 2.7 angstroms pecA heterodimer of alpha and beta (see PIR:RFMWB) chains; heterodimers associate to form trimeric and larger complexes phycobilisome light harvesting photosynthesis maximum absorption at approximately 550-570 nanometers phycocyanin chromoprotein light-harvesting complex photosynthesis phycobiliviolin thylakoid binding-site phycobiliviolin (Cys) (covalent) 84 experimental 162 complete MKTPLTEAIAAADLRGSYLSNTELQAVFGRFNRARAGLEAARAFANNGKKWAEAAANHVY QKFPYTTQMQGPQYASTPEGKAKCVRDIDHYLRTISYCCVVGGTGPLDDYVVAGLKEFNS ALGLSPSWYIAALEFVRDNHGLTGDVAGEANTYINYAINALS
B41841 B41841 24-Sep-1999 24-Sep-1999 20-Apr-2001
phycoerythrocyanin alpha chain Anabaena sp. (strain PCC 7120) Anabaena sp. Swanson, R.V. de Lorimier, R. Glazer, A.N. J. Bacteriol. 17419922640-2647 Genes encoding the phycobilisome rod substructure are clustered on the Anabaena chromosome: characterization of the phycoerythrocyanin operon. MUID92210509 B41841 preliminary DNA 1-162 GBM80357 NIDg142069 PIDNAAA22017.1 PIDg142071 Bishop, J.E. Rapoport, H. Klotz, A.V. Chan, C.F. Glazer, A.N. Fueglistaller, P. Zuber, H. J. Am. Chem. Soc. 1091987875-881 Chromopeptides from phycoerythrocyanin. Structure and linkage of the three bilin groups. annotation spectrographic characterization peptide linkage heterodimer of alpha and beta (see PIR:A41841) chains; heterodimers associate to form trimeric and larger complexes phycobilisome light harvesting photosynthesis maximum absorption at approximately 550-570 nanometers phycocyanin chromoprotein light-harvesting complex photosynthesis phycobiliviolin thylakoid binding-site phycobiliviolin (Cys) (covalent) 84 experimental 162 complete MKTPLTEAISAADVRGSYLSNTEMQAVFGRFNRARAGLAAAQAFSNNGKKWAEAAANHVY QKFPYTTQMSGPQYASTPEGKSKCVRDIDHYLRTISYCCVVGGTGPLDEYVVSGLSELNS ALGLSPSWYVAALEFVRDNHGLNGDVAGEANIYLNYAINALS
A44462 A44462 S75012 10-Sep-1999 10-Sep-1999 16-Jun-2000
allophycocyanin alpha chain Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Su, X. Fraenkel, P.G. Bogorad, L. J. Biol. Chem. 267199222944-22950 Excitation energy transfer from phycocyanin to chlorophyll in an apcA-defective mutant of Synechocystis sp. PCC 6803. MUID93054612 A44462 mRNA 1-161 GBM77135 NIDg154453 PIDNAAA27276.1 PIDg154454 PCC 6803 sequence extracted from NCBI backbone (NCBIP:118109) Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S75012 nucleic acid sequence not shown translation not shown DNA 1-161 EMBLD90910 GBAB001339 NIDg1652956 PIDNBAA17874.1 PIDg1652957 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 apcA phycocyanin chromoprotein photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 81 predicted 161 complete MSIVTKSIVNADAEARYLSPGELDRIKAFVTGGAARLRIAETLTGSRETIVKQAGDRLFQ KRPDIVSPGGNAYGEEMTATCLRDMDYYLRLVTYGVVSGDVTPIEEIGLVGVREMYRSLG TPIEAVAQSVREMKEVASGLMSSDDAAEASAYFDFVIGKMS
B28539 B28539 S00712 20-Apr-2000 20-Apr-2000 20-Apr-2000
C-phycocyanin 2 alpha chain inducible phycocyanin alpha chain Calothrix sp. Calothrix sp. Capuano, V. Mazel, D. Tandeau de Marsac, N. Houmard, J. Nucleic Acids Res. 1619881626 Complete nucleotide sequence of the red-light specific set of phycocyanin genes from the cyanobacterium Calothrix PCC 7601. MUID88157728 B28539 DNA 1-162 GBM36276 NIDg144937 PIDNAAA23290.1 PIDg144939 PCC 7601 Conley, P.B. Lemaux, P.G. Grossman, A. J. Mol. Biol. 1991988447-465 Molecular characterization and evolution of sequences encoding light-harvesting components in the chromatically adapting cyanobacterium Fremyella diplosiphon. MUID88172492 S00712 DNA 1-7,'G',9-54,'TA',57-149,'V',151-162 EMBLX07012 NIDg43381 PIDNCAA30062.1 PIDg43383 source designated as Fremyella diplosiphon cpcA2 phycocyanin chromoprotein photosynthesis phycocyanobilin product C-phycocyanin 2 alpha chain 1-162 experimental binding-site phycocyanobilin (Cys) (covalent) 84 predicted 162 complete MKTPLTEAVATADSQGRFLSSTELQVAFGRFRQASASLDAAKALSSKANSLAQGAVNAVY QKFPYTTQMQGKNFASDQRGKDKCARDIGYYIRIVTYCLVAGGTGPLDDYLIGGLAEINR TFDLSPSWYVEALKYIKANHGLSGDPAVEANSYIDYAINALS
A28539 A28539 S00711 20-Apr-2000 20-Apr-2000 20-Apr-2000
C-phycocyanin 2 beta chain inducible phycocyanin beta chain Calothrix sp. Calothrix sp. Capuano, V. Mazel, D. Tandeau de Marsac, N. Houmard, J. Nucleic Acids Res. 1619881626 Complete nucleotide sequence of the red-light specific set of phycocyanin genes from the cyanobacterium Calothrix PCC 7601. MUID88157728 A28539 DNA 1-172 GBM36276 NIDg144937 PIDNAAA23289.1 PIDg144938 PCC 7601 Conley, P.B. Lemaux, P.G. Grossman, A. J. Mol. Biol. 1991988447-465 Molecular characterization and evolution of sequences encoding light-harvesting components in the chromatically adapting cyanobacterium Fremyella diplosiphon. MUID88172492 S00711 DNA 1-28,'D',30-172 EMBLX07012 source designated as Fremyella diplosiphon cpcB2 phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin product C-phycocyanin 2 beta chain 1-172 experimental modified-site N4-methylasparagine (Asn) 72 predicted binding-site phycocyanobilin (Cys) (covalent) 82 predicted binding-site phycocyanobilin (Cys) (covalent) 153 predicted 172 complete MLDAFTKVVSQADTRGAYISDAEIDALKTMVAAGSKRMDVVNRITGNASTIVANAARALF EEQPQLIAPGGNAYTNRRMAACLRDMEIILRYVTYAVFAGDASVLDDRCLNGLRETYQAL GVPGASVSTGVQKMKEAAIAIANDPSGVTRGDCSSLMSELGSYFDRAAAAVG
CFXCA A25527 A24307 S00287 31-Mar-1992 31-Mar-1992 16-Jun-2000
C-phycoerythrin alpha chain Calothrix sp. (strain PCC 7601) Calothrix sp. Mazel, D. Guglielmi, G. Houmard, J. Sidler, W. Bryant, D.A. Tandeau de Marsac, N. Nucleic Acids Res. 1419868279-8290 Green light induces transcription of the phycoerythrin operon in the cyanobacterium Calothrix 7601. MUID87066711 A25527 DNA 1-164 EMBLX04592 NIDg1546895 PIDNCAA28261.1 PIDg43390 Sidler, W. Kumpf, B. Rudiger, W. Zuber, H. Biol. Chem. Hoppe-Seyler 3671986627-642 The complete amino-acid sequence of C-phycoerythrin from the cyanobacterium Fremyella diplosiphon. MUID87000169 Fremyella diplosiphon A24307 protein 1-164 cpeA phycocyanin chromoprotein heterodimer phytochromobilin thylakoid product C-phycoerythrin alpha chain 1-164 experimental binding-site phycoerythrobilin (Cys) (covalent) 82 experimental binding-site phycoerythrobilin (Cys) (covalent) 139 experimental 164 complete MKSVVTTVIAAADAAGRFPSTSDLESVQGSIQRAAARLEAAEKLANNIDAVATEAYNACI KKYPYLNNSGEANSTDTFKAKCARDIKHYLRLIQYSLVVGGTGPLDEWGIAGQREVYRAL GLPTAPYVEALSFARNRGCAPRDMSAQALTEYNALLDYAINSLS
CFMWB S02500 A00319 S02611 31-Jan-1980 31-Dec-1990 30-Apr-1999
C-phycocyanin beta chain Fischerella sp. Fischerella sp. Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. Biol. Chem. Hoppe-Seyler 36819871401-1406 Isolation and localization of N(4)-methylasparagine in phycobiliproteins from the cyanobacterium Mastigocladus laminosus. MUID88107006 S02500 protein 37-92 source designated as Mastigocladus laminosus Frank, G. Sidler, W. Widmer, H. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 35919781491-1507 The complete amino acid sequence of both subunits of C-phycocyanin from the cyanobacterium Mastigocladus laminosus. MUID79087164 A00319 protein 1-71,'S',73,'TR',76,'GT',79-172 source designated as Mastigocladus laminosus sequence revised in reference S02496 Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. FEBS Lett. 22119871-2 Gamma-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix. S02611 protein 55-83 source designated as Mastigocladus laminosus associates with alpha chain (see PIR:CFMWA) photon energy transfer from phycoerythrin to allophycocyanin photosynthesis phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 72 experimental binding-site phycocyanobilin (Cys) (covalent) 82 experimental binding-site phycocyanobilin (Cys) (covalent) 153 experimental 172 complete AYDVFTKVVSQADSRGEFLSNEQLDALANVVKEGNKRLDVVNRITSNASTIVTNAARALF EEQPQLIAPGGNAYTNRRMAACLRDMEIILRYITYAILAGDASILDDRCLNGLRETYQAL GTPGSSVAVGIQKMKEAAINIANDPNGITKGDCSALISEVASYFDRAAAAVA
CFKKB A00320 B60844 02-Apr-1982 30-Apr-1999 15-Sep-2000
C-phycocyanin beta chain [validated] red alga (Cyanidium caldarium) Cyanidium caldarium Troxler, R.F. Ehrhardt, M.M. Brown-Mason, A.S. Offner, G.D. J. Biol. Chem. 256198112176-12184 Primary structure of phycocyanin from the unicellular rhodophyte Cyanidium caldarium. II. Complete amino acid sequence of the beta subunit. MUID82053082 A00320 protein 1-71,'T',73-172 Brown, A.S. Offner, G.D. Ehrhardt, M.M. Troxler, R.F. J. Biol. Chem. 25419797803-7811 Phycobilin-apoprotein linkages in the alpha and beta subunits of phycocyanin from the unicellular rhodophyte, Cyanidium caldarium. Amino acid sequences of (35)S-labeled chromopeptides. MUID79239364 B60844 protein 80-86;136-166 Stec, B. Troxler, R.F. Teeter, M.M. submitted to the Brookhaven Protein Data Bank June1995 PDB1PHN annotation X-ray crystallography, 1.65 angstroms, residues 1-172 residue 72 is identified as N4-methylasparagine This protein was isolated from the phycobilisomes on the chloroplasts of this unicellular, acido-thermal, eukaryote red alga. heterodimers of alpha (see PIR:CFKKA) and beta chains form larger multimers phycocyanin chloroplast chromoprotein heterodimer methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 72 experimental binding-site phycocyanobilin (Cys) (covalent) 82 experimental binding-site phycocyanobilin (Cys) (covalent) 153 experimental 172 complete MLDAFAKVVAQADARGEFLSNTQLDALSKMVSEGNKRLDVVNRITSNASAIVTNAARALF SEQPQLIQPGGNAYTNRRMAACLRDMEIILRYVSYAIIAGDSSILDDRCLNGLRETYQAL GVPGASVAVGIEKMKDSAIAIANDPSGITTGDCSALMAEVGTYFDRAATAVQ
CFYCBB B94024 B94017 A00321 A22972 13-Aug-1986 13-Aug-1986 11-Jun-1999
C-phycocyanin beta chain Synechococcus sp. Synechococcus sp. de Lorimier, R. Bryant, D.A. Porter, R.D. Liu, W.Y. Jay, E. Stevens Jr., S.E. Proc. Natl. Acad. Sci. U.S.A. 8119847946-7950 Genes of the alpha and beta subunits of phycocyanin. MUID85088525 Agmenellum quadruplicatum B94024 DNA 1-172 GBK02660 NIDg142182 PIDNAAB05343.1 PIDg142183 strain PR-6 Pilot, T.J. Fox, J.L. Proc. Natl. Acad. Sci. U.S.A. 8119846983-6987 Cloning and sequencing of the genes encoding the alpha and beta subunits of C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. MUID85063716 Agmenellum quadruplicatum B94017 DNA 1-172 GBK02659 NIDg142176 PIDNAAB05341.1 PIDg142177 strain PR-6 phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 72 predicted binding-site phycocyanobilin (Cys) (covalent) 82 predicted binding-site phycocyanobilin (Cys) (covalent) 153 predicted 172 complete MFDIFTRVVSQADARGEFISSDKLEALKKVVAEGTKRSDAVSRMTNNASSIVTNAARQLF ADQPQLIAPGGNAYTNRRMAACLRDMEIILRYVTYATFTGDASVLNDRCLNGLRETYVAL GVPGASVAAGVRAMGKAAVAIVMDPAGVTSGDCSSLQQEIELYFETAAKAVE
CFYCB A26577 S60069 S60074 A23999 A92224 A00322 30-Apr-1979 02-Jul-1996 11-Jun-1999
C-phycocyanin beta chain Synechococcus sp. (PCC 6301) Synechococcus sp. PCC 6301 Synechococcus sp. PCC 6301 (ATCC 27144) was named Anacystis nidulans in other culture collections, e.g., CCAP, SAUG, and UTEX Lau, P.C.K. Condie, J.A. Alvarado-Urbina, G. Lau, R.H. Nucleic Acids Res. 1519872394 Nucleotide sequence of phycocyanin beta-subunit gene of cyanobacterium Anacystis nidulans strain R2. MUID87174767 A26577 preliminary not compared with conceptual translation DNA 1-173 GBX04916 NIDg38899 PIDNCAA28585.1 PIDg38900 strain R2 Kalla, S.R. Lind, L.K. Lidholm, J. Gustafsson, P. J. Bacteriol. 17019882961-2970 Transcriptional organization of the phycocyanin subunit gene clusters of the cyanobacterium Anacystis nidulans UTEX 625. MUID88257006 S60069 preliminary nucleic acid sequence not shown translation not shown DNA 1-173 EMBLM94218 NIDg142121 PIDNAAA64526.1 PIDg142122 strain PCC 6301 source designated as Anacystis nidulans the nucleotide sequence was submitted to the EMBL Data Library, June j1992 S60074 nucleic acid sequence not shown translation not shown DNA 1-173 EMBLM94218 NIDg142121 PIDNAAA64531.1 PIDg142127 the source is designated as Anacystis nidulans the nucleotide sequence was submitted to the EMBL Data Library, June 1992 Lind, L.K. Kalla, S.R. Lonneborg, A. Oquist, G. Gustafsson, P. FEBS Lett. 188198527-32 Cloning of the beta-phycocyanin gene from Anacystis nidulans. A23999 DNA 52-78 source designated as Anacystis nidulans Freidenreich, P. Apell, G.S. Glazer, A.N. J. Biol. Chem. 2531978212-219 Structural studies on phycobiliproteins. II. C-phycocyanin: amino acid sequence of the beta subunit. Specific cleavage of the alpha subunit. MUID78066839 A92224 protein 2-27,'SL',30-78,80-111,'D',113-120,'S',122-126,'L',128-157,159-173 Williams, V.P. Glazer, A.N. J. Biol. Chem. 2531978202-211 Structural studies on phycobiliproteins. I. Bilin-containing peptides of C-phycocyanin. MUID78066837 annotation attachment sites of chromophores associates with alpha chain (see PIR:CFYCA) photon energy transfer from phycoerythrin to allophycocyanin photosynthesis phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin product C-phycocyanin beta chain 2-173 experimental modified-site N4-methylasparagine (Asn) 73 predicted binding-site phycocyanobilin (Cys) (covalent) 83 experimental binding-site phycocyanobilin (Cys) (covalent) 154 experimental 173 complete MTFDAFTKVVAQADARGEFLSDAQLDALSRLVAEGNKRIDTVNRITGNASSIVANAARAL FAEQPSLIAPGGNAYTNRRMAACLRDMEIILRYVTYAVFTGDASILDDRCLNGLRETYLA LGVPGASVAEGVRKMKDAAVAIVSDRNGITQGDCSAIISELGSYFDKAAAAVA
CFYCB3 S17734 S31067 S31072 B26703 S27717 S31060 30-Jun-1992 30-Jun-1992 20-Apr-2000
R-phycocyanin II beta chain Synechococcus sp. Synechococcus sp. Wilson, W.H. Newman, J. Mann, N.H. Carr, N.G. Plant Mol. Biol. 171991931-933 Cloning and sequence analysis of the phycocyanin genes of the marine cyanobacterium Synechococcus sp. WH7803. MUID92003705 S17734 DNA 1-172 EMBLX59809 NIDg48036 PIDNCAA42479.1 PIDg48037 strain WH7803 de Lorimier, R. Wilbanks, S.M. Glazer, A.N. Plant Mol. Biol. 211993225-237 Genes of the R-phycocyanin II locus of marine Synechococcus spp., and comparison of protein-chromophore interactions in phycocyanins differing in bilin composition. MUID93144698 S31067 DNA 1-20,'T',22-32,'GR',35-41,'S',43-45,'N',47-57,'E',59-64,'A',66-67,'S',69-95,'SA',98,'T',100-124,'T',126-135,'DA',138-139,'S',141-149,'N',151-169,'S',171-172 EMBLM95288 NIDg154551 PIDNAAA27345.1 PIDg154565 strain WH8020 the authors translated the codon AGG for residue 34 as Ser and TCC for residue 149 as Thr S31072 DNA 1-20,'T',22-64,'A',66-95,'SA',98,'T',100-104,'M',106-135,'DA',138-141,'I',143-144,'K',146-169,'S',171-172 EMBLM95289 NIDg154605 PIDNAAA27365.1 PIDg154606 strain WH8103 Ong, L.J. Glazer, A.N. J. Biol. Chem. 26219876323-6327 R-phycocyanin II, a new phycocyanin occurring in marine Synechococcus species. Identification of the terminal energy acceptor bilin in phycocyanins. MUID87194855 B26703 protein 2-20,'T';79-84;147-149,'X',151-158,'D',160-166 cpcB rpcB phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin product R-phycocyanin II beta chain 2-172 predicted modified-site N4-methylasparagine (Asn) 72 predicted binding-site phycocyanobilin (Cys) (covalent) 82 predicted binding-site phycocyanobilin (Cys) (covalent) 153 predicted 172 complete MFDAFTKVVAQADARGQFISASEIDALAAMVSDSNKRLDAVNRISSNASTIVASAARQLF AQQPSLIAPGGNAYTSRRMAACLRDMEIILRYVTYASFAGDASVLEDRCLNGLRETYLAL GTPGASVAAGVNLMKESALAIVNDRAGISAGDCASLSSEIGTYFDRAAAAVA
RFMWB JQ0763 A00323 03-Aug-1984 12-Apr-1996 29-Sep-1999
phycoerythrocyanin beta chain Fischerella sp. Fischerella sp. Fischerella is a genus of nitrogen-fixing, thermophilic, branching, filamentous blue-green algae Eberlein, M. Kufer, W. Gene 941990133-136 Genes encoding both subunits of phycoerythrocyanin, a light-harvesting biliprotein from the cyanobacterium Mastigocladus laminosus. MUID91033055 JQ0763 preliminary DNA 1-172 GBM34254 NIDg149774 PIDNAAC64653.1 PIDg149775 Fuglistaller, P. Suter, F. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 3641983691-712 The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus. MUID83289130 A00323 protein 1-171 the source is designated as Mastigocladus laminosus Duerring, M. Huber, R. Bode, W. Ruembeli, R. Zuber, H. J. Mol. Biol. 2111990633-644 Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A. MUID90172426 annotation X-ray crystallography, 2.7 angstroms pecB heterodimer of alpha (see PIR:RFMWA) and beta chains; heterodimers associate to form trimeric and larger complexes phycobilisome light harvesting photosynthesis maximum absorption at approximately 550-570 nanometers phycocyanin chromoprotein light-harvesting complex photosynthesis phycocyanobilin thylakoid binding-site phycocyanobilin (Cys) (covalent) 82 predicted binding-site phycocyanobilin (Cys) (covalent) 153 predicted 172 complete MLDAFSRVVEQADKKGAYLSNDEINALQAIVADSNKRLDVVNRLTSNASSIVANAYRALV AERPQVFNPGGPCFHHRNQAACIRDLGFILRYVTYSVLAGDTSVMDDRCLNGLRETYQAL GTPGDAVASGIKKMKEAALKIANDPNGITKGDCSQLMSELASYFDRAAAAVA
A41841 A41841 24-Sep-1999 24-Sep-1999 20-Apr-2001
phycoerythrocyanin beta chain Anabaena sp. (strain PCC 7120) Anabaena sp. Swanson, R.V. de Lorimier, R. Glazer, A.N. J. Bacteriol. 17419922640-2647 Genes encoding the phycobilisome rod substructure are clustered on the Anabaena chromosome: characterization of the phycoerythrocyanin operon. MUID92210509 A41841 preliminary DNA 1-172 GBM80357 NIDg142069 PIDNAAA22016.1 PIDg142070 Bishop, J.E. Rapoport, H. Klotz, A.V. Chan, C.F. Glazer, A.N. Fueglistaller, P. Zuber, H. J. Am. Chem. Soc. 1091987875-881 Chromopeptides from phycoerythrocyanin. Structure and linkage of the three bilin groups. annotation spectrographic characterization peptide linkage heterodimer of alpha (see PIR:B41841) and beta chains; heterodimers associate to form trimeric and larger complexes phycobilisome light harvesting photosynthesis maximum absorption at approximately 550-570 nanometers phycocyanin chromoprotein light-harvesting complex photosynthesis phycocyanobilin thylakoid binding-site phycocyanobilin (Cys) (covalent) 82 experimental binding-site phycocyanobilin (Cys) (covalent) 153 experimental 172 complete MLDAFSKVVEQADRKGNYLSGDEINALSALVADSNKRLDIVNRLTSNASSIVANAYRALV AERPQIFNAGGACFHNRNQAACIRDLGFILRYVTYSVLAGDGSVMDDRCLNGLRETYQAL GTPGDAVASGIQKMKDAAIAIANDSKGITKGDCSQLIAELASYFDRAASAVV
AFMDB S14676 S10457 31-Dec-1991 31-Dec-1991 30-Apr-1999
phycoerythrin beta chain Cryptomonas sp. chloroplast chloroplast Cryptomonas sp. Reith, M. Douglas, S. Plant Mol. Biol. 151990585-592 Localization of beta-phycoerythrin to the thylakoid lumen of Cryptomonas Phi does not involve a signal peptide. MUID91338697 S14676 DNA 1-177 EMBLX52158 NIDg11383 PIDg11384 cpeB chloroplast phycocyanin chloroplast chromoprotein heterotetramer methylated amino acid phycocyanobilin thylakoid binding-site phycocyanobilin (Cys) (covalent) 50,61 predicted modified-site N4-methylasparagine (Asn) 72 predicted binding-site phycocyanobilin (Cys) (covalent) 82 predicted disulfide-bonds 137-165 predicted binding-site phycocyanobilin (Cys) (covalent) 158 predicted 177 complete MLDAFSRVVTNADAKAAYVGGADLQALKKFISEGNKRLDAVNSVVSNASCIVSDAVSGMI CENPSLISPSGNCYTNRRMAACLRDGEIILRYVSYALLSGDSSVLEDRCLNGLKETYSSL GVPANSNARAVSIMKACAVAFINNTASQRKLSTPQGDCSGLASECASYFDKVTAAIS
E22102 S10604 E22102 10-Sep-1999 10-Sep-1999 10-Sep-1999
phycocyanin-645 beta chain cryptomonad (Chroomonas sp.) Chroomonas sp. Sidler, W. Nutt, H. Kumpf, B. Frank, G. Suter, F. Brenzel, A. Wehrmeyer, W. Zuber, H. Biol. Chem. Hoppe-Seyler 3711990537-547 The complete amino-acid sequence and the phylogenetic origin of phycocyanin-645 from the cryptophytan alga Chroomonas sp.. MUID91025621 S10604 preliminary protein 1-177 Sidler, W. Kumpf, B. Suter, F. Morisset, W. Wehrmeyer, W. Zuber, H. Biol. Chem. Hoppe-Seyler 3661985233-244 Structural studies on cryptomonad biliprotein subunits. Two different alpha-subunits in Chroomonas phycocyanin-645 and Cryptomonas phycoerythrin-545. MUID85225953 E22102 protein 1-31,'R',33-43 heterotetramer of two alpha chains (see PIR:S10602 and PIR:S10603) and two beta chains phycocyanin chromoprotein heterotetramer photosynthesis phycocyanobilin binding-site cryptoviolin (Cys) (covalent) 50,61 experimental binding-site phycocyanobilin (Cys) (covalent) 82 experimental binding-site phycocyanobilin (Cys) (covalent) 158 experimental 177 complete MLDAFSRVVTGADSKAAYVGGADLQALKKFVSEGNKRLDAVNAIVSNASCIVSDAVSGMI CENPSLISPSGECYTNRRMAACLRDAEIILRYVSYSLLSGDSSVLEDRCLSGLKETYASL GVPAAGNARAVGIMKATVVAFINNTSNQKKLLTPSGDCSALASEAAGYFDKVTSALA
CFXCB B25527 B24307 S02614 S00286 31-Mar-1992 31-Mar-1992 16-Jun-2000
C-phycoerythrin beta chain Calothrix sp. (strain PCC 7601) Calothrix sp. Mazel, D. Guglielmi, G. Houmard, J. Sidler, W. Bryant, D.A. Tandeau de Marsac, N. Nucleic Acids Res. 1419868279-8290 Green light induces transcription of the phycoerythrin operon in the cyanobacterium Calothrix 7601. MUID87066711 B25527 DNA 1-184 EMBLX04592 NIDg1546895 PIDNCAA28260.1 PIDg43389 Sidler, W. Kumpf, B. Rudiger, W. Zuber, H. Biol. Chem. Hoppe-Seyler 3671986627-642 The complete amino-acid sequence of C-phycoerythrin from the cyanobacterium Fremyella diplosiphon. MUID87000169 Fremyella diplosiphon B24307 protein 1-69,'S',71-184 this sequence has been revised in reference S02611 Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. FEBS Lett. 22119871-2 Gamma-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix. S02614 protein 53-81 cpeB phycocyanin chromoprotein heterodimer methylated amino acid phytochromobilin thylakoid product C-phycoerythrin beta chain 1-184 experimental binding-site phycoerythrobilin (Cys) (covalent) 48,59 experimental modified-site N4-methylasparagine (Asn) 70 experimental binding-site phycoerythrobilin (Cys) (covalent) 80 experimental binding-site phycoerythrobilin (Cys) (covalent) 165 experimental 184 complete MLDAFSRAVVSADASTSTVSDIAALRAFVASGNRRLDAVNAIASNASCMVSDAVAGMICE NQGLIQAGGNCYPNRRMAACLRDAEIVLRYVTYALLAGDASVLDDRCLNGLKETYAALGV PTTSTVRAVQIMKAQAAAHIQDTPSEARAGAKLRKMGTPVVEDRCASLVAEASSYFDRVI SALS
AFKKA S37089 A00324 25-Feb-1985 12-Jul-1996 15-Oct-1999
allophycocyanin alpha chain red alga (Cyanidium caldarium) Cyanidium caldarium Kostrzewa, M. Zetsche, K. submitted to the EMBL Data Library August1993 S37089 DNA 1-161 EMBLX74548 NIDg398386 PIDNCAA52641.1 PIDg398388 the source is designated as Galdieria sulphuraria Offner, G.D. Troxler, R.F. J. Biol. Chem. 25819839931-9940 Primary structure of allophycocyanin from the unicellular rhodophyte, Cyanidium caldarium. The complete amino acid sequences of the alpha and beta subunits. MUID83290919 A00324 protein 1,3-130,'D',132-145,'R',147-155,'KLP',159,'SS' apcA associates with beta chain (see PIR:AFKKB) photon energy transfer from phycocyanin to allophycocyanin-B photosynthesis phycocyanin chloroplast chromoprotein photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 81 predicted 161 complete MSIVTKSIVNADAEARYLSPGELDRIKSFVLSGQRRLRIAQILTDNRERIVKQAGQQLFQ QRPDIVSPGGNAYGEEMTATCLRDLDYYLRLVTYGVVAGDIAPIEEIGLVGVKEMYNSLG TPISAVAEGIKAMKNVACSLLSGDDSAEAGFYFDYTIGAMQ
AFMWA A00325 14-Nov-1983 14-Nov-1983 30-Apr-1999
allophycocyanin alpha chain Fischerella sp. Fischerella sp. Sidler, W. Gysi, J. Isker, E. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 3621981611-628 The complete amino acid sequence of both subunits of allophycocyanin, a light harvesting protein-pigment complex from the cyanobacterium Mastigocladus laminosus. MUID82005802 A00325 protein 1-160 the source was designated as Mastigocladus laminosus Allophycocyanin is a photosynthetic pigment--protein complex (with maximum absorption at approximately 650 nanometers) composed of two dissimilar chains. Both the alpha chain and the beta chain contain a covalently linked phycocyanobilin chromophore. phycocyanin chromoprotein photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 80 experimental 160 complete SIVTKSIVNADAEARYLSPGELDRIKSFVSSGEKRLRIAQILTDNRERIVKQAGDQLFQK RPDVVSPGGNAYGQEMTATCLRDLDYYLRLITYGIVAGDVTPIEEIGIVGVREMYKSLGT PIDAVAAGVSAMKNVASSILSAEDAAEAGAYFDYVAGALA
AFKTA A00326 C24650 T06847 28-May-1986 28-May-1986 11-Jun-1999
allophycocyanin alpha chain Cyanophora paradoxa cyanelle cyanelle Cyanophora paradoxa Bryant, D.A. De Lorimier, R. Lambert, D.H. Dubbs, J.M. Stirewalt, V.L. Stevens Jr., S.E. Porter, R.D. Tam, J. Jay, E. Proc. Natl. Acad. Sci. U.S.A. 8219853242-3246 Molecular cloning and nucleotide sequence of the alpha and beta subunits of allophycocyanin from the cyanelle genome of Cyanophora paradoxa. MUID85216477 A00326 DNA 1-161 GBM11159 NIDg336622 PIDNAAA31693.1 PIDg336623 Lemaux, P.G. Grossman, A.R. EMBO J. 419851911-1919 Major light-harvesting polypeptides encoded in polycistronic transcripts in a eukaryotic alga. MUID86055745 C24650 DNA 1-15 GBX02791 NIDg11377 PIDNCAA26558.1 PIDg951229 Stirewalt, V.L. Michalowski, C.B. Luffelhardt, W. Bohnert, H.J. Bryant, D.A. submitted to the EMBL Data Library July1995 Nucleotide sequence of the cyanelle genome from Cyanophora paradoxa. T06847 preliminary translated from GB/EMBL/DDBJ DNA 1-161 EMBLU30821 NIDg1016083 PIDNAAA81190.1 PIDg1016103 strain Pringsheim LB555 apcA cyanelle heterotetramer of two alpha and two beta chains (see PIR:AFKTB) phycocyanin chromoprotein cyanelle heterotetramer photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 81 predicted 161 complete MSIVTKSIVNADAEARYLSPGELDRIKSFAASGERRLRIAQILTDNRERIVREAGQQLFQ KRPDIVSPGGNAYGEEMTATCLRDLDYYLRLVTYGVVAGDATPIEEIGLVGVKEMYNSLG TPVAAVAEGVRSAKSVATGLLSGDDAAEAGSYFDYVIAALQ
AFAIAC A24224 28-Dec-1987 28-Dec-1987 30-Apr-1999
allophycocyanin alpha chain Anabaena cylindrica Anabaena cylindrica Minami, Y. Yamada, F. Hase, T. Matsubara, H. Murakami, A. Fujita, Y. Takao, T. Shimonishi, Y. FEBS Lett. 1911985216-220 Amino acid sequences of allophycocyanin alpha- and beta-subunits isolated from Anabaena cylindrica. A24224 protein 1-160 This protein is a common component of light-gathering protein complexes called phycobilisomes, which are involved in the energy transfer process to chlorophyll a. phycocyanin chromoprotein photosynthesis phycocyanobilin binding-site phycocyanobilin (Cys) (covalent) 80 experimental 160 complete SIVTKAIVNADAEARYLSPGELDRIKSFVAGGASRLRIAQVLTENRERIVKQAGDQLFQK RPDVVSPGGNAYGQEMTATCLRDLDYYLRLVTYGIVSGDVTPIEEIGIVGVREMYKSLGT PIDAVAGGVAAMKNVAATLLSAEDSSEAGSYFDYVVGAMQ
AFKTB A00327 D24650 T06846 28-May-1986 28-May-1986 11-Jun-1999
allophycocyanin beta chain Cyanophora paradoxa cyanelle cyanelle Cyanophora paradoxa Bryant, D.A. De Lorimier, R. Lambert, D.H. Dubbs, J.M. Stirewalt, V.L. Stevens Jr., S.E. Porter, R.D. Tam, J. Jay, E. Proc. Natl. Acad. Sci. U.S.A. 8219853242-3246 Molecular cloning and nucleotide sequence of the alpha and beta subunits of allophycocyanin from the cyanelle genome of Cyanophora paradoxa. MUID85216477 A00327 DNA 1-161 GBM11159 NIDg336622 PIDNAAA31694.1 PIDg336624 Lemaux, P.G. Grossman, A.R. EMBO J. 419851911-1919 Major light-harvesting polypeptides encoded in polycistronic transcripts in a eukaryotic alga. MUID86055745 D24650 DNA 1-15 GBX02792 NIDg11379 PIDNCAA26559.1 PIDg11380 Stirewalt, V.L. Michalowski, C.B. Luffelhardt, W. Bohnert, H.J. Bryant, D.A. submitted to the EMBL Data Library July1995 Nucleotide sequence of the cyanelle genome from Cyanophora paradoxa. T06846 preliminary translated from GB/EMBL/DDBJ DNA 1-161 EMBLU30821 NIDg1016083 PIDNAAA81189.1 PIDg1016102 strain Pringsheim LB555 apcB cyanelle phycocyanin chromoprotein cyanelle methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 71 predicted binding-site phycocyanobilin (Cys) (covalent) 81 predicted 161 complete MQDAITAVINAADVQGKYLDTASVEKLKSYFQTGELRVRAAATIAANSSAIIKEAVAKSL LYSDITRPGGNMYTTRRYAACIRDLDYYVRYATYAMLAGDTSILDERVLNGLKETYNSLG VPVGATIQAIQAAKEVTAGLVGPDAGREMGIYYDYISSGLG
AFAIB A00328 A61422 18-Dec-1981 18-Dec-1981 30-Apr-1999
allophycocyanin beta chain Anabaena variabilis Anabaena variabilis DeLange, R.J. Williams, L.C. Glazer, A.N. J. Biol. Chem. 25619819558-9566 The amino acid sequence of the beta subunit of allophycocyanin. MUID82030740 A00328 protein 1-161 Klotz, A.V. Leary, J.A. Glazer, A.N. J. Biol. Chem. 261198615891-15894 Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin. MUID87057240 A61422 protein 63-71 phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 71 experimental binding-site phycocyanobilin (Cys) (covalent) 81 experimental 161 complete AQDAITAVINSADVQGKYLDTAALEKLKAYFSTGELRVRAATTISANAAAIVKEAVAKSL LYSDITRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDPSILDERVLNGLKETYNSLG VPVGATVQAIQAIKEVTASLVGAKAGKEMGIYLDYISSGLS
AFAIBC B24224 28-Dec-1987 08-Nov-1996 30-Apr-1999
allophycocyanin beta chain Anabaena cylindrica Anabaena cylindrica Minami, Y. Yamada, F. Hase, T. Matsubara, H. Murakami, A. Fujita, Y. Takao, T. Shimonishi, Y. FEBS Lett. 1911985216-220 Amino acid sequences of allophycocyanin alpha- and beta-subunits isolated from Anabaena cylindrica. B24224 protein 1-70,'D',72-161 residue 71 presented as Asp was identified as N4-hydroxymethylasparagine therefore, we have shown it as Asn This protein is a common component of light-gathering protein complexes called phycobilisomes, which are involved in the energy transfer process to chlorophyll a. phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site asparagine derivative (Asn) (probably N4-hydroxymethylasparagine) 71 experimental binding-site phycocyanobilin (Cys) (covalent) 81 predicted 161 complete MQDAITSVINSSDVQGKYLDTAALEKLKGYFATGELRVRAATTISANAAAIVKEAVAKSL LYSDITRPGGNMYTTRRYAACIRDLDYYLRYSTYAMLAGDPSILDERVLNGLKETYNSLG VPVGATVQAIQAMKEVTASLVGPDAGKEMGVYFDYISSGLS
AFMWB S02501 A00329 S02612 14-Nov-1983 31-Dec-1990 30-Apr-1999
allophycocyanin beta chain Fischerella sp. Fischerella sp. Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. Biol. Chem. Hoppe-Seyler 36819871401-1406 Isolation and localization of N(4)-methylasparagine in phycobiliproteins from the cyanobacterium Mastigocladus laminosus. MUID88107006 S02501 protein 59-82 source designated as Mastigocladus laminosus Sidler, W. Gysi, J. Isker, E. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 3621981611-628 The complete amino acid sequence of both subunits of allophycocyanin, a light harvesting protein-pigment complex from the cyanobacterium Mastigocladus laminosus. MUID82005802 A00329 protein 1-58,'LT',61-66,'L',68-70,'D',72-161 source designated as Mastigocladus laminosus sequence revised in reference S02496 Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. FEBS Lett. 22119871-2 Gamma-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix. S02612 protein 55-82 source designated as Mastigocladus laminosus This phycocyanin beta chain contains only one covalently attached chromophore. associates with alpha chain (see PIR:AFMWA) photon energy transfer from phycocyanin to allophycocyanin-B photosynthesis phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 71 experimental binding-site phycocyanobilin (Cys) (covalent) 81 experimental 161 complete MQDAITAVINSSDVQGKYLDTAALEKLKSYFSTGELRVRAATTIAANAAAIVKEAVAKSL LYSDITRPGGNMYTTRRYAACIRDLDYYLRYATYAMLAGDPSILDERVLNGLKETYNSLG VPISATVQAIQAMKEVTASLVGPDAGKEMGVYFDYICSGLS
AFKKB S37090 S70823 A00330 S36414 25-Feb-1985 12-Jul-1996 01-Dec-2000
allophycocyanin beta chain red alga (Cyanidium caldarium) chloroplast chloroplast Cyanidium caldarium Kostrzewa, M. Zetsche, K. submitted to the EMBL Data Library August1993 S37090 DNA 1-161 EMBLX74548 NIDg398386 PIDNCAA52642.1 PIDg398389 the source is designated as Galdieria sulphuraria Kostrzewa, M. Zetsche, K. Plant Mol. Biol. 23199367-76 Organization of plastid-encoded ATPase genes and flanking regions including homologues of infB and tsf in the thermophilic red alga Galdieria sulphuraria. MUID94033298 S70823 preliminary nucleic acid sequence not shown translation not shown DNA 51-161 EMBLX66698 NIDg396522 PIDNCAA47243.1 PIDg396527 the source is designated as Galdieria sulphuraria the nucleotide sequence was submitted to the EMBL Data Library, June 1992 Offner, G.D. Troxler, R.F. J. Biol. Chem. 25819839931-9940 Primary structure of allophycocyanin from the unicellular rhodophyte, Cyanidium caldarium. The complete amino acid sequences of the alpha and beta subunits. MUID83290919 A00330 protein 1-22,'I',24-69,'LD',72-93,'L',95-142,'P',144-161 apcB chloroplast associates with alpha chain (see PIR:AFKKA) photon energy transfer from phycocyanin to allophycocyanin-B photosynthesis phycocyanin chloroplast chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 71 predicted binding-site phycocyanobilin (Cys) (covalent) 81 predicted 161 complete MQDAITAVINTADVQGKYLDSSSIEKLKGYFQTGELRVRAAATIAANAAGIIKDAVAKSL LYSDITRPGGNMYTTRRYAACIRDLDYYLRYATYSMLAGDPSILDERVLNGLKETYNSLG VPIGATIQSIQAMKEVTSSLVGSEAGKEMGIYFDYICSGLS
AFMWB6 A26428 S02502 S02613 28-Dec-1987 31-Dec-1990 30-Apr-1999
phycobiliprotein 16.2 beta chain Fischerella sp. Fischerella sp. Ruembeli, R. Wirth, M. Suter, F. Zuber, H. Biol. Chem. Hoppe-Seyler 36819871-9 The phycobiliprotein beta-16.2 of the allophycocyanin core from the cyanobacterium Mastigocladus laminosus. MUID87157096 A26428 protein 1-71,'S',73-169 the source is designated as Mastigocladus laminosus this sequence has been revised in reference S02496 Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. Biol. Chem. Hoppe-Seyler 36819871401-1406 Isolation and localization of N(4)-methylasparagine in phycobiliproteins from the cyanobacterium Mastigocladus laminosus. MUID88107006 S02502 protein 58-100 the source is designated as Mastigocladus laminosus Ruembeli, R. Suter, F. Wirth, M. Sidler, W. Zuber, H. FEBS Lett. 22119871-2 Gamma-N-methylasparagine in phycobiliproteins from the cyanobacteria Mastigocladus laminosus and Calothrix. S02613 protein 55-83 the source is designated as Mastigocladus laminosus this is one of the components of phycobilisomes, which are high-molecular mass complexes of phycobiliproteins attached to the photosynthetic membranes of cyanobacteria and red algae; it is a protein functionally equivalent to, but with weaker absorbance than, allophycocyanin beta chain phycocyanin chromoprotein methylated amino acid photosynthesis phycocyanobilin modified-site N4-methylasparagine (Asn) 72 experimental binding-site phycocyanobilin (Cys) (covalent) 82 experimental 169 complete MRDAVTSLIKNYDVAGRYFDRNAIESLKSYFESGTQRVQAAKAINANAAAIVKQTGSKLF DEQPELIRPGGNAYTTRRYAACLRDLDYYLRYATYAIVAGSMDVLDERVLQGLRETYNSL GVPIGPTVRGIQIMKEIVKEQLGAAGIPNTSFVDEPFDYMTRELGEKDI
S74962 S74962 10-Sep-1999 10-Sep-1999 16-Jun-2000
probable allophycocyanin linker protein protein sll1509 Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S74962 nucleic acid sequence not shown translation not shown DNA 1-109 EMBLD90902 GBAB001339 NIDg1652027 PIDNBAA17002.1 PIDg1652077 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 probable allophycocyanin linker protein 109 complete MQRTRLNTIVEVRGQQLSQFFRNPWRRISLSLLSFLFGFFVGTAVATTAGQNSQWDVVCA AFILLFCELVNRWFYRRGVKMGDLQAEVLNIFKMGVSYSLFLEAFKLGS
S25307 S25307 10-Sep-1999 10-Sep-1999 10-Sep-1999
probable allophycocyanin linker protein red alga (Cyanidium caldarium) chloroplast chloroplast Cyanidium caldarium Valentin, K. Maid, U. Emich, A. Zetsche, K. Plant Mol. Biol. 201992267-276 Organization and expression of a phycobiliprotein gene cluster from the unicellular red alga Cyanidium caldarium. MUID93004479 S25307 DNA 1-83 EMBLX57251 NIDg17969 PIDNCAA40532.1 PIDg17971 apcL chloroplast probable allophycocyanin linker protein chloroplast 83 complete MQLIIINTLLGIFSSNLLCTIYTQTGDWSLYLTSCIIALYEIISYISYNQFIKKTHKNII NCFNGFKIGLIYGLYLDAFKLGS
S73135 S73135 10-Sep-1999 10-Sep-1999 10-Sep-1999
probable allophycocyanin linker protein red alga (Porphyra purpurea) chloroplast chloroplast Porphyra purpurea Reith, M. Munholland, J. Plant Mol. Biol. Rep. 131995333-335 Complete nucleotide sequence of the Porphyra purpurea chloroplast genome. S73135 preliminary nucleic acid sequence not shown translation not shown DNA 1-108 EMBLU38804 NIDg1276652 PIDNAAC08100.1 PIDg1276680 the nucleotide sequence was submitted to the EMBL Data Library, October 1995 ycf20 chloroplast probable allophycocyanin linker protein chloroplast 108 complete MIRTKLSIFFSYFVQNLSSRLYYSLNELTAGLISLLLGFFISTGLSTIPGQTGDWGIIAA SLIVAAIELVSKIVYSNKKKYGVRINLLNNLKIGITYGLFVDAFKLGS
S59989 S59989 S75014 C44462 10-Sep-1999 10-Sep-1999 16-Jun-2000
allophycocyanin core-associated linker subunit L8c hypothetical protein ssr3383 phycobilisome LC linker protein small core linker protein Synechocystis sp. Synechocystis sp. PCC 6714 DiMagno, L. Haselkorn, R. Plant Mol. Biol. 211993835-845 Isolation and characterization of the genes encoding allophycocyanin subunits and two linker proteins from Synechocystis 6714. MUID93222481 S59989 nucleic acid sequence not shown translation not shown DNA 1-67 EMBLL02308 NIDg154449 PIDNAAA69684.1 PIDg154452 PCC 6714 the nucleotide sequence was submitted to the EMBL Data Library, September 1992 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S75014 DNA 1-67 EMBLD90910 GBAB001339 NIDg1652956 PIDNBAA17876.1 PIDg1652959 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 Su, X. Fraenkel, P.G. Bogorad, L. J. Biol. Chem. 267199222944-22950 Excitation energy transfer from phycocyanin to chlorophyll in an apcA-defective mutant of Synechocystis sp. PCC 6803. MUID93054612 C44462 not compared with conceptual translation DNA 1-35,'S',37-67 GBM77135 NIDg154453 PIDNAAA27278.1 PIDg154456 PCC 6803 sequence extracted from NCBI backbone (NCBIP:118111) apcC allophycocyanin linker protein 67 complete MRMFRITACVPSQTRIRTQRELQNTYFTKLVPYDNWFREQQRIMKMGGKIVKVELATGRP GTNAGLA
C27873 C27873 10-Sep-1999 10-Sep-1999 10-Sep-1999
allophycocyanin linker protein Synechococcus sp. (PCC 6301) Synechococcus sp. Houmard, J. Mazel, D. Moguet, C. Bryant, D.A. Tandeau de Marsac, N. Mol. Gen. Genet. 2051986404-410 Organization and nucleotide sequence of genes encoding core components of the phycobilisomes from Synechococcus 6301. MUID87172294 C27873 DNA 1-67 GBX04716 NIDg46819 PIDNCAA28423.1 PIDg46822 PCC 6301 allophycocyanin linker protein 67 complete MRMFRITACLPSPSKIRTQRELQNTFFTKLVPYDAWFREQQRIQKLGGKIIKVELATGRP NTNTGLL
D31385 D31385 C30764 10-Sep-1999 10-Sep-1999 10-Sep-1999
allophycocyanin linker protein L (C-7.8) Calothrix sp. Calothrix sp. Houmard, J. Capuano, V. Coursin, T. Tandeau de Marsac, N. J. Bacteriol. 17019885512-5521 Genes encoding core components of the phycobilisome in the cyanobacterium Calothrix sp. strain PCC 7601: occurrence of a multigene family. MUID89053869 D31385 DNA 1-68 GBM20806 GBM31224 NIDg148538 PIDNAAA24876.1 PIDg148542 PCC 7601 allophycocyanin linker protein 68 complete MARLFKVTACVPSQTRIRTQRELQNTYFTKLVPFENWFREQQRIMKMGGKIVKVELATGK QGTNTGLL
S00284 S00284 10-Sep-1999 10-Sep-1999 10-Sep-1999
allophycocyanin linker protein, 8.9K Fischerella sp. Fischerella sp. Fueglistaller, P. Ruembeli, R. Suter, F. Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 36519841085-1096 Minor polypeptides from the phycobilisome of the cyanobacterium Mastigocladus laminosus. Isolation, characterization and amino-acid sequences of a colourless 8.9-kDa polypeptide and of a 16.2-kDa phycobiliprotein. S00284 protein 1-67 9-Ser was also found the source is designated as Mastigocladus laminosus allophycocyanin linker protein 67 complete GRLFKITACVPSQTRIRTQRELQNTYFTKLVPYENWFREQQRIQKMGGKIVKVELATGKQ GINTGLA
FKPUZ S00099 30-Sep-1991 30-Sep-1991 11-Jun-1999
phytochrome zucchini zucchini Cucurbita pepo var. melopepo Sharrock, R.A. Lissemore, J.L. Quail, P.H. Gene 471986287-295 Nucleotide and amino acid sequence of a Cucurbita phytochrome cDNA clone: identification of conserved features by comparison with Avena phytochrome. MUID87163500 S00099 mRNA 1-1124 EMBLM15265 NIDg167500 PIDNAAA33115.1 PIDg167501 phytochrome phytochrome homology chromoprotein homodimer photoreceptor phytochromobilin transcription regulation domain phytochrome homology 67-581 domain signal transduction 867-1124 binding-site phytochromobilin (Cys) (covalent) 323 predicted 1124 complete MSTSRPSQSSSNSGRSRHSTRIIAQTSVDANVQADFEESGNSFDYSSSVRVTSDVSGDQQ PRSDKVTTAYLHHIQKGKLIQPFGCLLALDDKTFKVIAYSENAPEMLTMVSHAVPSMGDY PVLGIGTDVRTIFTAPSASALLKALGFGEVTLLNPILVHCKTSGKPFYAIVHRVTGSLII DFEPVKPYEGPVTAAGALQSYKLAAKAITRLQSLPSGSMARLCDTMVQEVFELTGYDRVM AYKFHDDDHGEVISEVAKPGLQPYLGLHYPATDIPQAARFLFMKNKVRMIVDCRAKHLKV LQDEKLQFDLTLCGSTLRAPHSCHLQYMENMNSIASLVMAVVVNEGDEENEGPALQQQKR KRLWGLVVCHNSSPRFVPFPLRYACEFLAQVFAIHVNKELELENQIIEKNILRTQTLLCD MLMRDAPLGIVSRSPNIMDLVKSDGAALLYKKKIWRLGLTPNDFQLLDIASWLSEYHMDS TGLSTDSLYDAGYPGAIALGDEVCGMAAVRITNNDMIFWFRSHTASEIRWGGAKHEHGQK DDARKMHPRSSFKAFLEVVKTRSLPWKDYEMDAIHSLQLILRNTFKDTDATEINRKSIQT TLGDLKIEGRQELESVTSEMVRLIETATVPILAVDLDGLINGWNTKIAELTGLPVDKAIG KHLLTLVEDSSVEVVRKMLFLALQGQEEQNVQFEIKTHGSHIEVGSISLVVNACASRDLR ENVVGVFFVAQDITGQKMVMDKFTRLEGDYKAIVQNPNPLIPPIFGSDEFGWCSEWNPAM AKLTGWSREEVIDKMLLGEVFGVHKSCCRLKNQEAFVNLGIVLNNAMCGQDPEKASFGFL ARNGMYVECLLCVNKILDKDGAVTGFFCFLQLPSHELQQALNIQRLCEQTALKRLRALGY IKRQIQNPLSGIIFSRRLLERTELGVEQKELLRTSGLCQKQISKVLDESDIDKIIDGFID LEMDEFTLHEVLMVSISQVMLKIKGKGIQIVNETPEEAMSETLYGDSLRLQQVLADFLLI SVSYAPSGGQLTISTDVTKNQLGKSVHLVHLEFRITYAGGGIPESLLNEMFGSEEDASEE GFSLLISRKLVKLMNGDVRYMREAGKSSFIITVELAAAHKSRTT
FKMUA A33473 S07719 30-Sep-1991 30-Sep-1991 11-Jun-1999
phytochrome A Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana Sharrock, R.A. Quail, P.H. Genes Dev. 319891745-1757 Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family. MUID90108670 A33473 mRNA 1-1122 EMBLX17341 NIDg16420 PIDNCAA35221.1 PIDg16421 phyA phytochrome phytochrome homology chromoprotein dimer photoreceptor phytochromobilin transcription regulation domain phytochrome homology 67-583 domain signal transduction 869-1122 binding-site phytochromobilin (Cys) (covalent) 323 predicted 1122 complete MSGSRPTQSSEGSRRSRHSARIIAQTTVDAKLHADFEESGSSFDYSTSVRVTGPVVENQP PRSDKVTTTYLHHIQKGKLIQPFGCLLALDEKTFKVIAYSENASELLTMASHAVPSVGEH PVLGIGTDIRSLFTAPSASALQKALGFGDVSLLNPILVHCRTSAKPFYAIIHRVTGSIII DFEPVKPYEVPMTAAGALQSYKLAAKAITRLQSLPSGSMERLCDTMVQEVFELTGYDRVM AYKFHEDDHGEVVSEVTKPGLEPYLGLHYPATDIPQAARFLFMKNKVRMIVDCNAKHARV LQDEKLSFDLTLCGSTLRAPHSCHLQYMANMDSIASLVMAVVVNEEDGEGDAPDATTQPQ KRKRLWGLVVCHNTTPRFVPFPLRYACEFLAQVFAIHVNKEVELDNQMVEKNILRTQTLL CDMLMRDAPLGIVSQSPNIMDLVKCDGAALLYKDKIWKLGTTPSEFHLQEIASWLCEYHM DSTGLSTDSLHDAGFPRALSLGDSVCGMAAVRISSKDMIFWFRSHTAGEVRWGGAKHDPD DRDDARRMHPRSSFKAFLEVVKTRSLPWKDYEMDAIHSLQLILRNAFKDSETTDVNTKVI YSKLNDLKIDGIQELEAVTSEMVRLIETATVPILAVDSDGLVNGWNTKIAELTGLSVDEA IGKHFLTLVEDSSVEIVKRMLENALEGTEEQNVQFEIKTHLSRADAGPISLVVNACASRD LHENVVGVCFVAHDLTGQKTVMDKFTRIEGDYKAIIQNPNPLIPPIFGTDEFGWCTEWNP AMSKLTGLKREEVIDKMLLGEVFGTQKSCCRLKNQEAFVNLGIVLNNAVTSQDPDKVSFA FFTRGGKYVECLLCVSKKLDRKGVVTGVFCFLQLASHELQQALHVQRLAERTAVKRLKAL AYIKRQIRNPLSGIMFTRKMIEGTELGPEQRRILQTSALCQKQLSKILDDSDLESIIEGC LDLEMKEFTLNEVLTASTSQVMMKSNGKSVRITNETGEEVMSDTLYGDSIRLQQVLADFM LMAVNFTPSGGQLTVSASLRKDQLGRSVHLANLEIRLTHTGAGIPEFLLNQMFGTEEDVS EEGLSLMVSRKLVKLMNGDVQYLRQAGKSSFIITAELAAANK
FKMUB B33473 JQ2141 F84568 S07718 30-Sep-1991 30-Sep-1991 24-May-2001
phytochrome B Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana Sharrock, R.A. Quail, P.H. Genes Dev. 319891745-1757 Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family. MUID90108670 B33473 mRNA 1-1172 EMBLX17342 NIDg16422 PIDNCAA35222.1 PIDg16423 Reed, J.W. Nagpal, P. Poole, D.S. Furuya, M. Chory, J. Plant Cell 51993147-157 Mutations in the gene for the red/far-red light receptor phytochrome B alter cell elongation and physiological responses throughout Arabidopsis development. MUID93200802 JQ2141 DNA 1-1172 GBL09262 ecotype Landsberg, mutant hy3 Lin, X. Kaul, S. Rounsley, S.D. Shea, T.P. Benito, M.I. Town, C.D. Fujii, C.Y. Mason, T.M. Bowman, C.L. Barnstead, M.E. Feldblyum, T.V. Buell, C.R. Ketchum, K.A. Lee, J.J. Ronning, C.M. Koo, H. Moffat, K.S. Cronin, L.A. Shen, M. VanAken, S.E. Umayam, L. Tallon, L.J. Gill, J.E. Adams, M.D. Carrera, A.J. Creasy, T.H. Goodman, H.M. Somerville, C.R. Copenhaver, G.P. Preuss, D. Nierman, W.C. White, O. Eisen, J.A. Salzberg, S.L. Fraser, C.M. Venter, J.C. Nature 4021999761-768 Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana. MUID20083487 F84568 preliminary DNA 1-1172 GBAE002093 NIDg4185145 PIDNAAD08948.1 GSPDBGN00139 phyB At2g18790 2 722/1; 991/2; 1088/2 phytochrome phytochrome homology chromoprotein dimer photoreceptor phytochromobilin transcription regulation domain phytochrome homology 101-614 domain signal transduction 901-1172 binding-site phytochromobilin (Cys) (covalent) 357 predicted 1172 complete MVSGVGGSGGGRGGGRGGEEEPSSSHTPNNRRGGEQAQSSGTKSLRPRSNTESMSKAIQQ YTVDARLHAVFEQSGESGKSFDYSQSLKTTTYGSSVPEQQITAYLSRIQRGGYIQPFGCM IAVDESSFRIIGYSENAREMLGIMPQSVPTLEKPEILAMGTDVRSLFTSSSSILLERAFV AREITLLNPVWIHSKNTGKPFYAILHRIDVGVVIDLEPARTEDPALSIAGAVQSQKLAVR AISQLQALPGGDIKLLCDTVVESVRDLTGYDRVMVYKFHEDEHGEVVAESKRDDLEPYIG LHYPATDIPQASRFLFKQNRVRMIVDCNATPVLVVQDDRLTQSMCLVGSTLRAPHGCHSQ YMANMGSIASLAMAVIINGNEDDGSNVASGRSSMRLWGLVVCHHTSSRCIPFPLRYACEF LMQAFGLQLNMELQLALQMSEKRVLRTQTLLCDMLLRDSPAGIVTQSPSIMDLVKCDGAA FLYHGKYYPLGVAPSEVQIKDVVEWLLANHADSTGLSTDSLGDAGYPGAAALGDAVCGMA VAYITKRDFLFWFRSHTAKEIKWGGAKHHPEDKDDGQRMHPRSSFQAFLEVVKSRSQPWE TAEMDAIHSLQLILRDSFKESEAAMNSKVVDGVVQPCRDMAGEQGIDELGAVAREMVRLI ETATVPIFAVDAGGCINGWNAKIAELTGLSVEEAMGKSLVSDLIYKENEATVNKLLSRAL RGDEEKNVEVKLKTFSPELQGKAVFVVVNACSSKDYLNNIVGVCFVGQDVTSQKIVMDKF INIQGDYKAIVHSPNPLIPPIFAADENTCCLEWNMAMEKLTGWSRSEVIGKMIVGEVFGS CCMLKGPDALTKFMIVLHNAIGGQDTDKFPFPFFDRNGKFVQALLTANKRVSLEGKVIGA FCFLQIPSPELQQALAVQRRQDTECFTKAKELAYICQVIKNPLSGMRFANSLLEATDLNE DQKQLLETSVSCEKQISRIVGDMDLESIEDGSFVLKREEFFLGSVINAIVSQAMFLLRDR GLQLIRDIPEEIKSIEVFGDQIRIQQLLAEFLLSIIRYAPSQEWVEIHLSQLSKQMADGF AAIRTEFRMACPGEGLPPELVRDMFHSSRWTSPEGLGLSVCRKILKLMNGEVQYIRESER SYFLIILELPVPRKRPLSTASGSGDMMLMMPY
FKMUC C33473 S07717 30-Sep-1991 30-Sep-1991 11-Jun-1999
phytochrome C Arabidopsis thaliana mouse-ear cress Arabidopsis thaliana Sharrock, R.A. Quail, P.H. Genes Dev. 319891745-1757 Novel phytochrome sequences in Arabidopsis thaliana: structure, evolution, and differential expression of a plant regulatory photoreceptor family. MUID90108670 C33473 mRNA 1-1111 EMBLX17343 NIDg16424 PIDNCAA35223.1 PIDg16425 phyC phytochrome phytochrome homology chromoprotein dimer photoreceptor phytochromobilin transcription regulation domain phytochrome homology 62-573 domain signal transduction 856-1111 binding-site phytochromobilin (Cys) (covalent) 318 predicted 1111 complete MSSNTSRSCSTRSRQNSRVSSQVLVDAKLHGNFEESERLFDYSASINLNMPSSSCEIPSS AVSTYLQKIQRGMLIQPFGCLIVVDEKNLKVIAFSENTQEMLGLIPHTVPSMEQREALTI GTDVKSLFLSPGCSALEKAVDFGEISILNPITLHCRSSSKPFYAILHRIEEGLVIDLEPV SPDEVPVTAAGALRSYKLAAKSISRLQALPSGNMLLLCDALVKEVSELTGYDRVMVYKFH EDGHGEVIAECCREDMEPYLGLHYSATDIPQASRFLFMRNKVRMICDCSAVPVKVVQDKS LSQPISLSGSTLRAPHGCHAQYMSNMGSVASLVMSVTINGSDSDEMNRDLQTGRHLWGLV VCHHASPRFVPFPLRYACEFLTQVFGVQINKEAESAVLLKEKRILQTQSVLCDMLFRNAP IGIVTQSPNIMDLVKCDGAALYYRDNLWSLGVTPTETQIRDLIDWVLKSHGGNTGFTTES LMESGYPDASVLGESICGMAAVYISEKDFLFWFRSSTAKQIKWGGARHDPNDRDGKRMHP RSSFKAFMEIVRWKSVPWDDMEMDAINSLQLIIKGSLQEEHSKTVVDVPLVDNRVQKVDE LCVIVNEMVRLIDTAAVPIFAVDASGVINGWNSKAAEVTGLAVEQAIGKPVSDLVEDDSV ETVKNMLALALEGSEERGAEIRIRAFGPKRKSSPVELVVNTCCSRDMTNNVLGVCFIGQD VTGQKTLTENYSRVKGDYARIMWSPSTLIPPIFITNENGVCSEWNNAMQKLSGIKREEVV NKILLGEVFTTDDYGCCLKDHDTLTKLRIGFNAVISGQKNIEKLLFGFYHRDGSFIEALL SANKRTDIEGKVTGVLCFLQVPSPELQYALQVQQISEHAIACALNKLAYLRHEVKDPEKA ISFLQDLLHSSGLSEDQKRLLRTSVLCREQLAKVISDSDIEGIEEGYVELDCSEFGLQES LEAVVKQVMELSIERKVQISCDYPQEVSSMRLYGDNLRLQQILSETLLSSIRFTPALRGL CVSFKVIARIEAIGKRMKRVELEFRIIHPAPGLPEDLVREMFQPLRKGTSREGLGLHITQ KLVKLMERGTLRYLRESEMSAFVILTEFPLI
S27396 S27396 S20160 S12966 10-Sep-1999 10-Sep-1999 10-Sep-1999
phytochrome / protein kinase (EC 2.7.1.-) moss (Ceratodon purpureus) Ceratodon purpureus Thuemmler, F. Dufner, M. Kreisl, P. Dittrich, P. Plant Mol. Biol. 2019921003-1017 Molecular cloning of a novel phytochrome gene of the moss Ceratodon purpureus which encodes a putative light-regulated protein kinase. MUID93099252 S27396 DNA 1-1303 GBU87632 GBS51224 NIDg1839247 Thuemmler, F. Dufner, M. Kreisl, P. Dittrich, P. submitted to the Protein Sequence Database April1992 Molecular cloning of a novel phytochrome gene of the moss Ceratodon purpureus which encodes a putative light regulated protein kinase. S20160 DNA 1-1303 GBU87632 GBS51224 NIDg1839247 Thuemmler, F. Beetz, A. Ruediger, W. FEBS Lett. 2751990125-129 Phytochrome in lower plants. Detection and partial sequence of a phytochrome gene in the moss Ceratodon purpureus using the polymerase chain reaction. MUID91085543 S12966 DNA 49-539 GBX17084 NIDg296090 phy 679/1; 779/1 phytochrome / protein kinase phytochrome homology protein kinase homology ATP chromoprotein phosphotransferase photoreceptor phytochromobilin serine/threonine-specific protein kinase transcription regulation domain phytochrome homology 63-575 domain protein kinase homology 1002-1289 binding-site phytochromobilin (Cys) (covalent) 320 predicted 1303 complete MSATKKTYSSTTSAKSKHSVRVAQTTADAALEAVYEMSGDSGDSFDYSKSVGQSAESVPA GAVTAYLQRMQREGLIQNFGCMVAVEEPNFCVIAYSENASEFLDLIPQAVPSMGEMDVLG IGTDIRTLFTPSSSAALEKAAATQDISLLNPITVHCRRSGKPLYAIAHRIDIGIVIDFEA VKMIDVPVSAAAGALQSHKLAARAITRLQALPGGDIELLCDTIVEEVRELTGYDRVMAFK FHEDEHGEVVAEIRRMDLEPYMGLHYPATDIPQASRFLLMKNRVRLIADCYASPVKLIQD PDIRQPVSLAGSTLRAPHGCHAQYMGNMGSIASLVMAVIINDNEEYSRGAIQRGRKLWGL VVCQHTSPRTVPFPLRSVCEFLMQVFGMQLNLHVELAAQLREKHILRTQTLLCDMLLRDA PIGIVSQTPNIMDLVKCDGAALYYGKRVWLLGTTPTENQIKEIADWLLEHHNDSTGLSTD SLADANYPGAHLLGDAVCGMAAAKITAKDFLFWFRSHTATEVKWGGAKHDPDEKDDGRKM HPRSSFKAFLEVVNKRSPPWEDVEMDAIHSLQLILRGSFRDIADSDTKTMIHARLNDLKL QGVEERNALANEMSRVLETAAAPILAVDSRGMINAWNAKIAQVTGLPVEEAMHCSLTKDL VLDESVVVVERLLSLALQGEEEQNVEIKLKTFGTQTTERAVILIVNACCSRDASDFVVGV FFVGQDVTEQRMFMDRFTRIQGGEKTTVQDPHPLMRPSFDGDEFGRTFKRNSALGGLKDH ATGSVERLDLYLRRAEECMEVMETIPSPKFNNKQCQYLAGKLKAVLQSASLFLRISHHEH HELGASIDMGRHVEIFKLLLALAKEIESFIQGCCKDEWIKAAMTLTNVSEYVSSMGFNLE LCKIAFCKSCAASGSLTLDQIEVICKDEAEVVKRNASIDVDTLFAKVIYDLTEKTLSSDQ NDLAIYLLQRLKRAKPILPSFSSRPSWWNFYDDWSFSEKFFQWIQITGSLGSGSSATVEK AVWLGTPVAKKTFYGRNNEDFKREVEILAELCHPNITSMFCSPLYRRKCSIIMELMDGDL LALMQRRLDRNEDHDSPPFSILEVVDIILQTSEGMNYLHEKGIIHRDLKSMNILVKSVKV TKSEIGYVHVKVADFGLSKTKDSSTRYSNQTWNRGTNRWMAPEVINLGYESTEGEISFDG KVPKYPLKSDVYSFGMVCYEVLTGDVPFPEEKNPNNVKRMVLEGVRPDLPAHCPIELKAL ITDCWNQDPLKRPSFAVICQKLKYLKYLLMTGKLSSHSYLTSK
S74389 S74389 25-Apr-1997 25-Apr-1997 16-Jun-2000
phytochrome phy hypothetical protein slr0473 Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A. Nakazaki, N. Naruo, K. Okumura, S. Shimpo, S. Takeuchi, C. Wada, T. Watanabe, A. Yamada, M. Yasuda, M. Tabata, S. DNA Res. 31996109-136 Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. MUID97061201 S74389 nucleic acid sequence not shown translation not shown DNA 1-748 EMBLD64001 GBAB001339 NIDg1001102 PIDNBAA10307.1 PIDg1001165 the nucleotide sequence was submitted to the EMBL Data Library, June 1996 phy phytochrome phy phytochrome homology chromoprotein photoreceptor phytochromobilin domain phytochrome homology 2-504 domain sensor histidine kinase homology 507-745 binding-site phytochromobilin (Cys) (covalent) 259 predicted 748 complete MATTVQLSDQSLRQLETLAIHTAHLIQPHGLVVVLQEPDLTISQISANCTGILGRSPEDL LGRTLGEVFDSFQIDPIQSRLTAGQISSLNPSKLWARVMGDDFVIFDGVFHRNSDGLLVC ELEPAYTSDNLPFLGFYHMANAALNRLRQQANLRDFYDVIVEEVRRMTGFDRVMLYRFDE NNHGDVIAEDKRDDMEPYLGLHYPESDIPQPARRLFIHNPIRVIPDVYGVAVPLTPAVNP STNRAVDLTESILRSAYHCHLTYLKNMGVGASLTISLIKDGHLWGLIACHHQTPKVIPFE LRKACEFFGRVVFSNISAQEDTETFDYRVQLAEHEAVLLDKMTTAADFVEGLTNHPDRLL GLTGSQGAAICFGEKLILVGETPDEKAVQYLLQWLENREVQDVFFTSSLSQIYPDAVNFK SVASGLLAIPIARHNFLLWFRPEVLQTVNWGGDPNHAYEATQEDGKIELHPRQSFDLWKE IVRLQSLPWQSVEIQSALALKKAIVNLILRQAEELAQLARNLERSNADLKKFAYIASHDL QEPLNQVSNYVQLLEMRYSEALDEDAKDFIDFAVTGVSLMQTLIDDILTYAKVDTQYAQL TFTDVQEVVDKALANLKQRIEESGAEIEVGSMPAVMADQIQLMQVFQNLIANGIKFAGDK SPKIKIWGDRQEDAWVFAVQDNGIGIDPQFFERIFVIFQRLHTRDEYKGTGMGLAICKKI IEGHQGQIWLESNPGEGSTFYFSIPIGN
JC5446 B55993 A37428 JC5446 03-Dec-1999 03-Dec-1999 03-Dec-1999
photoactive yellow protein Ectothiorhodospira halophila Ectothiorhodospira halophila Baca, M. Borgstahl, G.E.O. Boissinot, M. Burke, P.M. Williams, D.R. Slater, K.A. Getzoff, E.D. Biochemistry 33199414369-14377 Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. MUID95072006 B55993 DNA 1-125 GBU17017 NIDg602427 PIDNAAA61735.1 PIDg602429 Van Beeumen, J.J. Devreese, B.V. Van Bun, S.M. Hoff, W.D. Hellingwerf, K.J. Meyer, T.E. McRee, D.E. Cusanovich, M.A. Protein Sci. 219931114-1125 Primary structure of a photoactive yellow protein from the phototrophic bacterium Ectothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore. MUID93364264 A37428 protein 1-55,'E',57-125 Mihara, K. Hisatomi, O. Imamoto, Y. Kataoka, M. Tokunaga, F. J. Biochem. 1211997876-880 Functional expression and site-directed mutagenesis of photoactive yellow protein. MUID97335933 annotation This small, soluble protein functions as a photoreceptor for the negative phototaxis of this organism. pyp Ectothiorhodospira halophila photoactive yellow protein chromoprotein photoreceptor thiolester bond binding-site 4-hydroxycinnamyl (Cys) (covalent) 69 experimental 125 complete MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKQVIGK NFFKDVAPCTDSPEFYGKFKEGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWV FVKRV
FXME A92137 A92156 A00331 13-Jul-1981 13-Jul-1981 07-May-1999
flavodoxin Megasphaera elsdenii Megasphaera elsdenii Tanaka, M. Haniu, M. Yasunobu, K.T. Mayhew, S. Massey, V. J. Biol. Chem. 24819734354-4366 MUID73197809 A92137 protein 1-77,'GKKLK',83-137 strain LC1 Tanaka, M. Haniu, M. Yasunobu, K.T. Mayhew, S.G. Massey, V. J. Biol. Chem. 24919744397 Correction of the amino acid sequence of Peptostreptococcus elsdenii flavodoxin. MUID74277393 A92156 protein 78-82 Tanaka, M. Haniu, M. Matsueda, G. Yasunobu, K.T. Mayhew, S. Massey, V. Biochemistry 1019713041-3046 Amino- and carboxyl-terminal amino acid sequences of the Peptostreptococcus elsdenii and Clostridium pasteurianum flavodoxins. MUID72062407 annotation Some anaerobic bacteria, when grown on iron-deficient media, produce flavodoxin instead of ferredoxin, which flavodoxin can replace in certain reactions. flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 4-135 137 complete MVEIVYWSGTGNTEAMANEIEAAVKAAGADVESVRFEDTNVDDVASKDVILLGCPAMGSE ELEDSVVEPFFTDLAPKLKGKKVGLFGSYGWGSGEWMDAWKQRTEDTGATVIGTAIVNEM PDNAPECKELGEAAAKA
A39414 A39414 10-Sep-1999 10-Sep-1999 10-Sep-1999
flavodoxin electron transport protein nifF Enterobacter agglomerans plasmid pEA3 Enterobacter agglomerans Kreutzer, R. Dayananda, S. Klingmueller, W. J. Bacteriol. 17319913252-3256 Cotranscription of the electron transport protein genes nifJ and nifF in Enterobacter agglomerans 333. MUID91217003 A39414 DNA 1-177 GBM38221 NIDg145132 PIDNAAA23385.1 PIDg145134 nifF plasmid flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 6-173 177 complete MATIGIFFGSDTGQTRKVAKLIHQKLDGIADAPLDVRRATREQFLSYPVLLLGTPTLGDG ELPGVEAGSQYDSWQEFTNTLSEADLTGKTVALFGLGDQLNYSKNFVSAMRILYDLVIAR GACVVGNWPREGYKFSFSAALLENNEFVGLPLDQENQYDLTEERIDSWLEKLKPAVL
S02511 S02511 10-Sep-1999 10-Sep-1999 10-Sep-1999
flavodoxin Klebsiella pneumoniae Klebsiella pneumoniae Arnold, W. Rump, A. Klipp, W. Priefer, U.B. Puehler, A. J. Mol. Biol. 2031988715-738 Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae. MUID89094839 S02511 DNA 1-176 EMBLX13303 NIDg43820 PIDNCAA31680.1 PIDg43836 nifF flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 6-172 176 complete MANIGIFFGTDTGKTRKIAKMIHKQLGELADAPVNINRTTLDDFMAYPVLLLGTPTLGDG QLPGLEAGCESESWSEFISGLDDASLKGKTVALFGLGDQRGYPDNFVSGMRPLFDALSAR GAQMIGSWPNEGYEFSASSALEGDRFVGLVLDQDNQFDQTEARLASWLEEIKRTVL
FXDV A31991 S06447 A00333 S45692 24-Apr-1984 31-Dec-1993 11-Jun-1999
flavodoxin Desulfovibrio vulgaris Desulfovibrio vulgaris Krey, G.D. Vanin, E.F. Swenson, R.P. J. Biol. Chem. 263198815436-15443 Cloning, nucleotide sequence, and expression of the flavodoxin gene from Desulfovibrio vulgaris (Hildenborough). MUID89008444 A31991 DNA 1-148 GBJ04033 NIDg145088 PIDNAAA23367.1 PIDg145089 Curley, G.P. Voordouw, G. FEMS Microbiol. Lett. 491988295-299 Cloning and sequencing of the gene encoding flavodoxin from Desulfovibrio vulgaris Hildenborough. S06447 not compared with conceptual translation DNA 1-148 Dubourdieu, M. Fox, J.L. J. Biol. Chem. 25219771453-1463 Amino acid sequence of Desulfovibrio vulgaris flavodoxin. MUID77118626 A00333 protein 1-27,'N',29-148 strain Hildenborough Watenpaugh, K.D. Sieker, L.C. Jensen, L.H. Proc. Natl. Acad. Sci. U.S.A. 7019733857-3860 The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin at 2.0 angstrom resolution. MUID74087652 annotation X-ray crystallography, 2.0 angstroms the flavin mononucleotide binding site is described Watenpaugh, K.D. Sieker, L.C. Jensen, L.H. LeGall, J. Dubourdieu, M. Proc. Natl. Acad. Sci. U.S.A. 6919723185-3188 Structure of the oxidized form of a flavodoxin at 2.5-angstrom resolution: resolution of the phase ambiguity by anomalous scattering. MUID73044810 annotation X-ray crystallography, 2.5 angstroms Pirola, M.C. Monti, F. Aliverti, A. Zanetti, G. Arch. Biochem. Biophys. 3111994480-486 A functional heterologous electron-transfer protein complex: Desulfovibrio vulgaris flavodoxin covalently linked to spinach ferredoxin-NADP(+) reductase. MUID94263229 S45692 protein 2-15 No disulfide bonds are present. flavodoxin flavodoxin homology electron transfer flavoprotein FMN product flavodoxin 1-148 experimental domain flavodoxin homology 6-145 region FMN-phosphate binding 10-15,58-62,95-102 experimental 148 complete MPKALIVYGSTTGNTEYTAETIARELADAGYEVDSRDAASVEAGGLFEGFDLVLLGCSTW GDDSIELQDDFIPLFDSLEETGAQGRKVACFGCGDSSYEYFCGAVDAIEEKLKNLGAEIV QDGLRIDGDPRAARDDIVGWAHDVRGAI
A34640 A34640 10-Sep-1999 10-Sep-1999 10-Sep-1999
flavodoxin Desulfovibrio salexigens Desulfovibrio salexigens Helms, L.R. Krey, G.D. Swenson, R.P. Biochem. Biophys. Res. Commun. 1681990809-817 Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. MUID90241257 A34640 preliminary DNA 1-146 GBM35475 NIDg145090 PIDNAAA23368.1 PIDg145091 flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 6-143 146 complete MSKSLIVYGSTTGNTETAAEYVAEAFENKEIDVELKNVTDVSVADLGNGYDIVLFGCSTW GEEEIELQDDFIPLYDSLENADLKGKKVSVFGCGDSDYTYFCGAVDAIEEKLEKMGAVVI GDSLKIDGDPERDEIVSWGSGIADKI
S24310 S24310 20-Apr-2000 20-Apr-2000 05-May-2000
flavodoxin Desulfovibrio gigas (ATCC 29494) Desulfovibrio gigas Helms, L.R. Swenson, R.P. Biochim. Biophys. Acta 11311992325-328 The primary structures of the flavodoxins from two strains of Desulfovibrio gigas. Cloning and nucleotide sequence of the structural genes. MUID92329549 S24310 DNA 1-147 EMBLX64765 NIDg40798 PIDNCAA46012.1 PIDg40799 strain ATCC 29494 flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 6-143 147 complete MGKALVVFGSTTGNTETVAEVVAKVLEESGMAVDLKNATKVKAAGLAEGYDLVVFGCSTW GDDEIELQEDFIPLYDDLGAAGLGGRKVAVFGCGDSSYTHFCGAVDAIAEKAASLGAKVI DLPLKIDGAPDTAEARDWAKEVLRSAA
S24311 S24311 20-Apr-2000 20-Apr-2000 05-May-2000
flavodoxin Desulfovibrio gigas (ATCC 19364) Desulfovibrio gigas Helms, L.R. Swenson, R.P. Biochim. Biophys. Acta 11311992325-328 The primary structures of the flavodoxins from two strains of Desulfovibrio gigas. Cloning and nucleotide sequence of the structural genes. MUID92329549 S24311 DNA 1-146 EMBLX64766 NIDg40800 PIDNCAA46013.1 PIDg40801 strain ATCC 19364 flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 6-143 146 complete MPKALIVYGSTTGNTEGVAEAIAKTLNSEGMETTVVNVADVTAPGLAEGYDVVLLGCSTW GDDEIELQEDFVPLYEDLDRAGLKDKKVGVFGCGDSSYTYFCGAVDVIEKKAEELGATLV ASSLKIDGEPDSAEVLDWAREVLARV
FXDVD S17000 31-Dec-1992 31-Dec-1992 11-Jun-1999
flavodoxin Desulfovibrio desulfuricans (ATCC 29577) Desulfovibrio desulfuricans Helms, L.R. Swenson, R.P. Biochim. Biophys. Acta 10891991417-419 Cloning and characterization of the flavodoxin gene from Desulfovibrio desulfuricans. MUID91316149 S17000 DNA 1-148 EMBLX59438 NIDg40796 PIDNCAA42064.1 PIDg40797 strain ATCC 29577 flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 6-145 148 complete MSKVLIVFGSSTGNTESIAQKLEELIAAGGHEVTLLNAADASAENLADGYDAVLFGCSAW GMEDLEMQDDFLSLFEEFNRIGLAGRKVAAFASGDQEYEHFCGAVPAIEERAKELGATII AEGLKMEGDASNDPEAVASFAEDVLKQL
FXCLEX A00332 07-May-1981 07-May-1981 05-Apr-1995
flavodoxin Clostridium sp. Clostridium sp. Tanaka, M. Haniu, M. Yasunobu, K.T. Mayhew, S.G. J. Biol. Chem. 24919744393-4396 The amino acid sequence of the Clostridium MP flavodoxin. MUID74277392 A00332 protein 1-138 strain MP Burnett, R.M. Darling, G.D. Kendall, D.S. LeQuesne, M.E. Mayhew, S.G. Smith, W.W. Ludwig, M.L. J. Biol. Chem. 24919744383-4392 The structure of the oxidized form of clostridial flavodoxin at 1.9-A resolution. Description of the flavin mononucleotide binding site. MUID74277391 annotation X-ray crystallography, 1.9 angstroms, oxidized form no disulfide bonds are present flavodoxin flavodoxin homology electron transfer flavoprotein FMN domain flavodoxin homology 3-136 138 complete MKIVYWSGTGNTEKMAELIAKGIIESGKDVNTINVSDVNIDELLNEDILILGCSAMGDEV LEESEFEPFIEEISTKISGKKVALFGSYGWGDGKWMRDFEERMNGYGCVVVETPLIVQNE PDEAEQDCIEFGKKIANI
FXAVEP A29935 A00334 24-Apr-1984 20-Aug-1994 11-Jun-1999
flavodoxin Azotobacter vinelandii Azotobacter vinelandii Bennett, L.T. Jacobson, M.R. Dean, D.R. J. Biol. Chem. 26319881364-1369 Isolation, sequencing, and mutagenesis of the nifF gene encoding flavodoxin from Azotobacter vinelandii. MUID88087273 A29935 DNA 1-180 GBJ03519 NIDg142373 PIDNAAA22154.1 PIDg142374 Tanaka, M. Haniu, M. Yasunobu, K.T. Yoch, D.C. Biochemistry 1619773525-3537 Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii. MUID77242321 A00334 protein 2-180 strain OP nifF flavodoxin flavodoxin homology electron transfer flavoprotein FMN product flavodoxin 2-180 experimental domain flavodoxin homology 6-173 180 complete MAKIGLFFGSNTGKTRKVAKSIKKRFDDETMSDALNVNRVSAEDFAQYQFLILGTPTLGE GELPGLSSDCENESWEEFLPKIEGLDFSGKTVALFGLGDQVGYPENYLDALGELYSFFKD RGAKIVGSWSTDGYEFESSEAVVDGKFVGLALDLDNQSGKTDERVAAWLAQIAPEFGLSL
A28670 A28670 A05103 19-Feb-1999 19-Feb-1999 17-Nov-2000
flavodoxin [validated] Synechococcus sp. Synechococcus sp. Laudenbach, D.E. Reith, M.E. Straus, N.A. J. Bacteriol. 1701988258-265 Isolation, sequence analysis, and transcriptional studies of the flavodoxin gene from Anacystis nidulans R2. MUID88086879 A28670 DNA 1-170 GBM19116 NIDg142132 PIDNAAA22050.1 PIDg142133 the source is designated as Anacystis nidulans Smith, W.W. Pattridge, K.A. Ludwig, M.L. Petsko, G.A. Tsernoglou, D. Tanaka, M. Yasunobu, K.T. J. Mol. Biol. 1651983737-755 MUID83216115 sequence X-ray crystallography, oxidized form, 2.5 angstroms A05103 protein 2-54,'S',56;167,'GF',170 Smith, W.W. Pattridge, K.A. Luschinsky, C.L. Ludwig, M.L. submitted to the Brookhaven Protein Data Bank June1992 PDB1OFV annotation X-ray crystallography, 1.7 angstroms, residues 2-170 oxidized form the source is designated as Anacystis nidulans flavodoxin flavodoxin homology electron transfer flavoprotein FMN product flavodoxin 2-170 experimental domain flavodoxin homology 6-165 region FMN-phosphate binding 10-15,58-62,90-100 experimental 170 complete MAKIGLFYGTQTGVTQTIAESIQQEFGGESIVDLNDIANADASDLNAYDYLIIGCPTWNV GELQSDWEGIYDDLDSVNFQGKKVAYFGAGDQVGYSDNFQDAMGILEEKISSLGSQTVGY WPIEGYDFNESKAVRNNQFVGLAIDEDNQPDLTKNRIKTWVSQLKSEFGL
S38632 S38632 S75085 B56811 10-Sep-1999 10-Sep-1999 16-Jun-2000
flavodoxin protein sll0248 Synechocystis sp. (strain PCC 6803) Synechocystis sp. PCC 6803 Poncelet, M.G. Cassier-Chauvat, C.J. Chauvat, F.R. submitted to the EMBL Data Library November1993 Sequence of the flavodoxin gene from Synechocystis PCC6803. S38632 preliminary DNA 1-170 EMBLZ27091 NIDg415403 PIDNCAA81614.1 PIDg415404 Kaneko, T. Sato, S. Kotani, H. Tanaka, A. Asamizu, E. Nakamura, Y. Miyajima, N. Hirosawa, M. Sugiura, M. Sasamoto, S. Kimura, T. Hosouchi, T. Matsuno, A. Muraki, A.