ID CYDA_AZOVI STANDARD; PRT; 537 AA. AC Q09049; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-MAR-2006, entry version 32. DE Cytochrome d ubiquinol oxidase subunit 1 (EC 1.10.3.-) (Cytochrome d DE ubiquinol oxidase subunit I). GN Name=cydA; OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 [GENOMIC DNA]. 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: Binds 1 protoheme IX. CC -!- SUBUNIT: Heterodimer of subunits I and II. CC -!- SUBCELLULAR LOCATION: Bacterial cell inner membrane; multi-pass CC membrane protein. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77787; AAA22123.1; -; Genomic_DNA. DR EMBL; S57066; AAB19986.1; -; Genomic_DNA. DR PIR; A38170; A38170. DR InterPro; IPR002585; Bac_Ubq_Cox. DR Pfam; PF01654; Bac_Ubq_Cox; 1. KW Electron transport; Heme; Inner membrane; Iron; Membrane; KW Metal-binding; Oxidoreductase; Transmembrane; Transport. FT CHAIN 1 537 Cytochrome d ubiquinol oxidase subunit 1. FT /FTId=PRO_0000183917. FT TOPO_DOM 1 24 Cytoplasmic (Potential). FT TRANSMEM 25 44 Potential. FT TOPO_DOM 45 96 Periplasmic (Potential). FT TRANSMEM 97 116 Potential. FT TOPO_DOM 117 131 Cytoplasmic (Potential). FT TRANSMEM 132 151 Potential. FT TOPO_DOM 152 189 Periplasmic (Potential). FT TRANSMEM 190 209 Potential. FT TOPO_DOM 210 221 Cytoplasmic (Potential). FT TRANSMEM 222 241 Potential. FT TOPO_DOM 242 394 Periplasmic (Potential). FT TRANSMEM 395 414 Potential. FT TOPO_DOM 415 472 Cytoplasmic (Potential). FT TRANSMEM 473 492 Potential. FT TOPO_DOM 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 //