ID CYDA_AZOVI STANDARD; PRT; 537 AA. AC Q09049; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE Cytochrome d ubiquinol oxidase subunit I (EC 1.10.3.-). GN Name=cydA; OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CA; RX MEDLINE=92011387; PubMed=1655703; RA Moshiri F., Chawla A., Maier R.J.; RT "Cloning, characterization, and expression in Escherichia coli of the RT genes encoding the cytochrome d oxidase complex from Azotobacter RT vinelandii."; RL J. Bacteriol. 173:6230-6241(1991). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CA; RX MEDLINE=92078187; PubMed=1660468; RA Moshiri F., Smith E.G., Taormino J.P., Maier R.J.; RT "Transcriptional regulation of cytochrome d in nitrogen-fixing RT Azotobacter vinelandii. Evidence that up-regulation during N2 fixation RT is independent of nifA but dependent on ntrA."; RL J. Biol. Chem. 266:23169-23174(1991). RN [3] RP CHARACTERIZATION. RX MEDLINE=91008979; PubMed=2170336; RA Kelly M.J.S., Poole R.K., Yates M.G., Kennedy C.; RT "Cloning and mutagenesis of genes encoding the cytochrome bd terminal RT oxidase complex in Azotobacter vinelandii: mutants deficient in the RT cytochrome d complex are unable to fix nitrogen in air."; RL J. Bacteriol. 172:6010-6019(1990). CC -!- FUNCTION: May be involved in maintaining the low intracellular CC oxygen concentration required for nitrogen fixation. CC -!- CATALYTIC ACTIVITY: Ubiquinol-8 + O(2) = Ubiquinone-8 + H(2)O. CC -!- COFACTOR: Contains the protoheme IX center b558. CC -!- SUBUNIT: Heterodimer of subunits I and II. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Inner membrane. CC -------------------------------------------------------------------------- CC This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; M77787; AAA22123.1; -. DR EMBL; S57066; AAB19986.1; -. DR PIR; A38170; A38170. DR InterPro; IPR002585; Bac_Ubq_Cox. DR Pfam; PF01654; Bac_Ubq_Cox; 1. KW Electron transport; Heme; Inner membrane; Oxidoreductase; KW Transmembrane. FT DOMAIN 1 24 Cytoplasmic (Potential). FT TRANSMEM 25 44 Potential. FT DOMAIN 45 96 Periplasmic (Potential). FT TRANSMEM 97 116 Potential. FT DOMAIN 117 131 Cytoplasmic (Potential). FT TRANSMEM 132 151 Potential. FT DOMAIN 152 189 Periplasmic (Potential). FT TRANSMEM 190 209 Potential. FT DOMAIN 210 221 Cytoplasmic (Potential). FT TRANSMEM 222 241 Potential. FT DOMAIN 242 394 Periplasmic (Potential). FT TRANSMEM 395 414 Potential. FT DOMAIN 415 472 Cytoplasmic (Potential). FT TRANSMEM 473 492 Potential. FT DOMAIN 493 537 Periplasmic (Potential). FT METAL 188 188 Iron (heme b558 axial ligand) (By FT similarity). SQ SEQUENCE 537 AA; 59719 MW; 8F78A49F6AB4902E CRC64; MISESVVDLS RLQFAMTALY HFLFVPLTLG MTFLLAIMES VYVMTGKQVY KDMVKFWGKL FGINFALGVT TGITMEFQFG TNWAYYSHYV GDIFGAPLAI EGLTAFFLES TFIGMFFFGW DRLSKIQHLA VTWLVALGSN LSALWILVAN GWMQHPVGAE FNFETMRMEL VDFGALLLNP VAQVKFVHTV ASGYVTGAVF VLAISSYYLL KKRDLGFARR SFAIASAFGM ASILSVIVLG DESGYEVGEV QKAKLAAIEA EWETHPAPAS FTLIGFPNEE EQRTDFAVKI PWVLGIIATR SLDEQVIGIK DLIADHEARI RNGMVRYGLL EELRAGNKSP EKIAAFNEVK DDLGYGLLLK KYTPNVVDAS EEQIKQAAKD TIPSVASMFW SFRAMVGAGF AMLILFVCAF WASARKNEES KPWLLKFALY SLPLPWIATQ TGWFVAEHGR QPWTIGGVLP THLSASSLST GDLWGSLIAL IAFYTLLLVV EMYLMIRFAR LGPSSLHTGR YHFEQLEQHA VKHASPSQAD PQQPVNA //