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 24-JAN-2024, entry version 128. DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1; DE EC=7.1.1.3 {ECO:0000250|UniProtKB:P0ABI8}; 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; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; 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 oxidase is the terminal enzyme in CC the aerobic respiratory chain. Catalyzes the four-electron reduction of CC O2 to water, using a ubiquinol as a membrane soluble electron donor for CC molecular oxygen reduction. Has proton pump activity across the CC membrane in addition to electron transfer, pumping 2 protons/electron CC and generating a proton motive force. All the redox centers of this CC enzyme complex are located within the largest subunit, subunit I. CC Protons are probably pumped via D- and K- channels found in this CC subunit. {ECO:0000250|UniProtKB:P0ABI8}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out) CC + 2 H2O; Xref=Rhea:RHEA:30251, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.3; CC Evidence={ECO:0000250|UniProtKB:P0ABI8}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000250|UniProtKB:P0ABI8}; CC Note=Binds 1 copper B ion per subunit. {ECO:0000250|UniProtKB:P0ABI8}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000250|UniProtKB:P0ABI8}; CC Note=Binds 1 low-spin heme b per subunit. CC {ECO:0000250|UniProtKB:P0ABI8}; CC -!- COFACTOR: CC Name=Fe(II)-heme o; Xref=ChEBI:CHEBI:60530; CC Evidence={ECO:0000250|UniProtKB:P0ABI8}; CC Note=Binds 1 high-spin heme o per subunit, also named heme o(3). CC {ECO:0000250|UniProtKB:P0ABI8}; CC -!- SUBUNIT: The cytochrome bo(3) ubiquinol oxidase complex is a CC heterooctamer of two A chains, two B chains, two C chains and two D CC chains. {ECO:0000250|UniProtKB:P0ABI8}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane CC protein {ECO:0000250}. CC -!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in the CC 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; WP_011091527.1; NC_004545.1. DR AlphaFoldDB; Q89AA4; -. DR SMR; Q89AA4; -. DR STRING; 224915.bbp_416; -. DR KEGG; bab:bbp_416; -. DR eggNOG; COG0843; Bacteria. DR HOGENOM; CLU_011899_7_1_6; -. DR OMA; FWGKMSF; -. DR OrthoDB; 9803294at2; -. DR Proteomes; UP000000601; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 CDD; cd01662; Ubiquinol_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR014207; Cyt_c_ubiqinol_oxidase_su1. DR NCBIfam; TIGR02843; CyoB; 1. DR PANTHER; PTHR10422:SF35; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport; KW Ion transport; Iron; Membrane; Metal-binding; Reference proteome; KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..659 FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 1" FT /id="PRO_0000183481" FT TOPO_DOM 1..14 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 15..35 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 36..56 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 57..77 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 78..109 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 110..130 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 131..148 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 149..169 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 170..192 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 193..213 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 214..235 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 236..256 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 257..280 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 281..301 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 302..318 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 319..339 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 340..350 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 351..371 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 372..382 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 383..403 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 404..416 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 417..437 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 438..459 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 460..480 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 481..499 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 500..520 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 521..587 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 588..608 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 609 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 610..630 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 631..659 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT BINDING 71 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 75 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 101 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 109 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 173 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 287 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 291 FT /ligand="Fe(II)-heme o" FT /ligand_id="ChEBI:CHEBI:60530" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 336 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 337 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 414 FT /ligand="Fe(II)-heme o" FT /ligand_id="ChEBI:CHEBI:60530" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 422 FT /ligand="Fe(II)-heme o" FT /ligand_id="ChEBI:CHEBI:60530" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 424 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 484 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT BINDING 485 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /evidence="ECO:0000250|UniProtKB:P0ABI8" FT CROSSLNK 287..291 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="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 //