ID CYOB_BUCBP Reviewed; 659 AA. AC Q89AA4; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 31-OCT-2006, entry version 25. DE Ubiquinol oxidase subunit 1 (EC 1.10.3.-) (Ubiquinol oxidase DE polypeptide I) (Cytochrome o subunit 1) (Oxidase BO(3) subunit 1) DE (Cytochrome o ubiquinol oxidase subunit 1). GN Name=cyoB; OrderedLocusNames=bbp_416; OS Buchnera aphidicola subsp. Baizongia pistaciae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=135842; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22426901; PubMed=12522265; DOI=10.1073/pnas.0235981100; RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.; RT "Reductive genome evolution in Buchnera aphidicola."; RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003). CC -!- FUNCTION: Cytochrome o terminal oxidase complex is the component CC of the aerobic respiratory chain that predominates when cells are CC grown at high aeration. This ubiquinol oxidase shows proton pump CC activity across the membrane in addition to the electron transfer CC (By similarity). CC -!- CATALYTIC ACTIVITY: Ubiquinol-8 + O(2) = Ubiquinone-8 + H(2)O. CC -!- COFACTOR: Binds 1 copper ion (By similarity). CC -!- COFACTOR: Binds 2 protoheme IX (heme b55 and b562) groups. CC -!- PATHWAY: Ubiquinol oxidase catalyzes the terminal step in the CC electron transport chain. CC -!- SUBCELLULAR LOCATION: Cell membrane; multi-pass membrane protein CC (By similarity). CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016826; AAO27126.1; -; Genomic_DNA. DR HSSP; P18401; 1FFT. DR GenomeReviews; AE016826_GR; bbp_416. DR KEGG; bab:bbp416; -. DR BioCyc; BAPH224915:BBP416-MONOMER; -. DR InterPro; IPR000883; COX1. DR PANTHER; PTHR10422; COX1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. KW Complete proteome; Copper; Electron transport; Heme; KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding; KW Oxidoreductase; Respiratory chain; Transmembrane; Transport. FT CHAIN 1 659 Ubiquinol oxidase subunit 1. FT /FTId=PRO_0000183481. FT TOPO_DOM 1 14 Extracellular (Potential). FT TRANSMEM 15 35 Potential. FT TOPO_DOM 36 56 Cytoplasmic (Potential). FT TRANSMEM 57 77 Potential. FT TOPO_DOM 78 109 Extracellular (Potential). FT TRANSMEM 110 130 Potential. FT TOPO_DOM 131 148 Cytoplasmic (Potential). FT TRANSMEM 149 169 Potential. FT TOPO_DOM 170 192 Extracellular (Potential). FT TRANSMEM 193 213 Potential. FT TOPO_DOM 214 235 Cytoplasmic (Potential). FT TRANSMEM 236 256 Potential. FT TOPO_DOM 257 280 Extracellular (Potential). FT TRANSMEM 281 301 Potential. FT TOPO_DOM 302 318 Cytoplasmic (Potential). FT TRANSMEM 319 339 Potential. FT TOPO_DOM 340 350 Extracellular (Potential). FT TRANSMEM 351 371 Potential. FT TOPO_DOM 372 382 Cytoplasmic (Potential). FT TRANSMEM 383 403 Potential. FT TOPO_DOM 404 416 Extracellular (Potential). FT TRANSMEM 417 437 Potential. FT TOPO_DOM 438 459 Cytoplasmic (Potential). FT TRANSMEM 460 480 Potential. FT TOPO_DOM 481 499 Extracellular (Potential). FT TRANSMEM 500 520 Potential. FT TOPO_DOM 521 587 Cytoplasmic (Potential). FT TRANSMEM 588 608 Potential. FT TOPO_DOM 609 609 Extracellular (Potential). FT TRANSMEM 610 630 Potential. FT TOPO_DOM 631 659 Cytoplasmic (Potential). FT METAL 109 109 Iron (heme B axial ligand) (Probable). FT METAL 287 287 Copper B (Probable). FT METAL 291 291 Copper B (Probable). FT METAL 336 336 Copper B (Probable). FT METAL 337 337 Copper B (Probable). FT METAL 422 422 Iron (heme O axial ligand) (Probable). FT METAL 424 424 Iron (heme B axial ligand) (Probable). FT CROSSLNK 287 291 1'-histidyl-3'-tyrosine (His-Tyr) (By FT similarity). SQ SEQUENCE 659 AA; 75583 MW; 13DD8E19D4F5FC15 CRC64; MFGKLSLNSI PYHDPIIMIT CCVVILVFLV ISIIITIAQK WQYLWNEWCC TVDHKKIAKM YIFLAFIMLF RGFADAIMMR MQQFLVSSYH GNGTGFLPPH HYDQIFTAHG VIMIFFVAMP LVIGLMNFVV PLQIGSRDVA FPFLNNLSLW LTIFSALLMN VSLGIGEFAQ TGWLAYPPLS ELQYSPGVGV DYWIWSLQIS GIGTTLTAIN FLVTIIKMRS SGMNWFKIPV FTWTSFCTNI LIIASFPVLT VSLLLLTLDR YLGFHFFTND FGGNMMMYVN LIWIWGHPEV YILILPVFGI FSEVVATFSS KELFGYTSLI WATIVITILS FIVWLHHFFT MGASANVNAF FGITTMIISI PTGVKIFNWL FTMYRGNVRI NSIMLWTIGF LITFSIGGMA GVLLSLPVID FSLHNSLFLV AHFHNVIIGG VVFGCFAGIT YWFPKLFGFM LSEKWGKRAF WCWFFGFFCA FMPLYALGLM GMTRRLSQNI NPQFHSMLTI AALGTILIFI GIVFQIIQIF VSIRDRNLNR DCSGDPWNGR TLEWSTTSPP PFYNFAVLPI VQFRDSFWES KKSFKSNKLP ILYTSFHMPK NTKFGFLIGF FAFLLGFSAV WYIFWLFFIS FFVIIYLLVI KSLDTNCDYI ISIEEIKEIE KCINIKKMD //