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 01-APR-2015, entry version 88. DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1; DE EC=1.10.3.10; DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 1; DE Short=Cytochrome o subunit 1; DE AltName: Full=Oxidase bo(3) subunit 1; DE AltName: Full=Ubiquinol oxidase polypeptide I; DE AltName: Full=Ubiquinol oxidase subunit 1; GN Name=cyoB; OrderedLocusNames=bbp_416; OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=224915; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bp; RX 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 bo(3) ubiquinol terminal oxidase is the CC component of the aerobic respiratory chain of E.coli that CC predominates when cells are grown at high aeration. Has proton CC pump activity across the membrane in addition to electron CC transfer, pumping 2 protons/electron (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 ubiquinol + O(2) + n H(+)(Side 1) = 2 CC ubiquinone + 2 H(2)O + n H(+)(Side 2). CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250}; CC Note=Binds 1 copper B ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; CC Note=Binds 1 low-spin heme b per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=heme o; Xref=ChEBI:CHEBI:24480; Evidence={ECO:0000250}; CC Note=Binds 1 high-spin heme o per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=a quinone; Xref=ChEBI:CHEBI:36141; Evidence={ECO:0000250}; CC Note=Binds 1 high-affinity quinone that appears to function as a CC tightly bound cofactor (QH), forming a semiquinone intermediate in CC the reaction. {ECO:0000250}; CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains CC and two D chains. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in CC the electron transport chain. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000305}. 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 RefSeq; NP_778021.1; NC_004545.1. DR SMR; Q89AA4; 52-555. DR STRING; 224915.bbp416; -. DR EnsemblBacteria; AAO27126; AAO27126; bbp_416. DR GeneID; 1058363; -. DR KEGG; bab:bbp416; -. DR PATRIC; 21245649; VBIBucAph80364_0417. DR eggNOG; COG0843; -. DR KO; K02298; -. DR OMA; AALCTNV; -. DR OrthoDB; EOG6B35XR; -. DR BioCyc; BAPH224915:GJ9D-416-MONOMER; -. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. DR InterPro; IPR014207; Cyt_c_ubiqinol_oxidase_su1. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR TIGRFAMs; TIGR02843; CyoB; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Copper; Electron transport; Heme; KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding; KW Oxidoreductase; Reference proteome; Respiratory chain; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 659 Cytochrome bo(3) ubiquinol oxidase FT subunit 1. FT /FTId=PRO_0000183481. FT TOPO_DOM 1 14 Extracellular. {ECO:0000255}. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TOPO_DOM 36 56 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TOPO_DOM 78 109 Extracellular. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TOPO_DOM 131 148 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TOPO_DOM 170 192 Extracellular. {ECO:0000255}. FT TRANSMEM 193 213 Helical. {ECO:0000255}. FT TOPO_DOM 214 235 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. FT TOPO_DOM 257 280 Extracellular. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT TOPO_DOM 302 318 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 319 339 Helical. {ECO:0000255}. FT TOPO_DOM 340 350 Extracellular. {ECO:0000255}. FT TRANSMEM 351 371 Helical. {ECO:0000255}. FT TOPO_DOM 372 382 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 383 403 Helical. {ECO:0000255}. FT TOPO_DOM 404 416 Extracellular. {ECO:0000255}. FT TRANSMEM 417 437 Helical. {ECO:0000255}. FT TOPO_DOM 438 459 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 460 480 Helical. {ECO:0000255}. FT TOPO_DOM 481 499 Extracellular. {ECO:0000255}. FT TRANSMEM 500 520 Helical. {ECO:0000255}. FT TOPO_DOM 521 587 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 588 608 Helical. {ECO:0000255}. FT TOPO_DOM 609 609 Extracellular. {ECO:0000255}. FT TRANSMEM 610 630 Helical. {ECO:0000255}. FT TOPO_DOM 631 659 Cytoplasmic. {ECO:0000255}. FT METAL 109 109 Iron (heme B axial ligand). FT {ECO:0000250}. FT METAL 287 287 Copper. {ECO:0000250}. FT METAL 291 291 Copper. {ECO:0000250}. FT METAL 336 336 Copper. {ECO:0000250}. FT METAL 337 337 Copper. {ECO:0000250}. FT METAL 422 422 Iron (heme O axial ligand). FT {ECO:0000250}. FT METAL 424 424 Iron (heme B axial ligand). FT {ECO:0000250}. FT BINDING 71 71 Quinone (QH). {ECO:0000250}. FT BINDING 75 75 Quinone (QH). {ECO:0000250}. FT BINDING 101 101 Quinone (QH). {ECO:0000250}. FT BINDING 104 104 Quinone (QH). {ECO:0000250}. FT CROSSLNK 287 291 1'-histidyl-3'-tyrosine (His-Tyr). FT {ECO:0000250}. 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 //