ID COX1_MYCBO Reviewed; 573 AA. AC P63853; A0A1R3Y2Z5; O53290; X2BMH9; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Probable cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome aa3 subunit 1; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=ctaD; OrderedLocusNames=BQ2027_MB3069C; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 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; LT708304; SIU01694.1; -; Genomic_DNA. DR RefSeq; NP_856714.1; NC_002945.3. DR RefSeq; WP_003415946.1; NC_002945.4. DR AlphaFoldDB; P63853; -. DR SMR; P63853; -. DR GeneID; 45427036; -. DR PATRIC; fig|233413.5.peg.3371; -. DR UniPathway; UPA00705; -. DR Proteomes; UP000001419; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. 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; IPR014241; Cyt_c_oxidase_su1_bac. DR NCBIfam; TIGR02891; CtaD_CoxA; 1. DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; 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; Iron; Membrane; KW Metal-binding; Reference proteome; Respiratory chain; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..573 FT /note="Probable cytochrome c oxidase subunit 1" FT /id="PRO_0000183444" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 89..109 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 121..141 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 170..190 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 258..278 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 315..335 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 359..379 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 398..418 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 433..453 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 476..496 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 86 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT BINDING 264 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 268 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 313 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 314 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000305" FT BINDING 397 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT BINDING 399 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000305" FT CROSSLNK 264..268 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250" SQ SEQUENCE 573 AA; 63673 MW; 9B0F91666F482BEE CRC64; MTAEAPPLGE LEAIRPYPAR TGPKGSLVYK LITTTDHKMI GIMYCVACIS FFFIGGLLAL LMRTELAAPG LQFLSNEQFN QLFTMHGTIM LLFYATPIVF GFANLVLPLQ IGAPDVAFPR LNAFSFWLFV FGATIGAAGF ITPGGAADFG WTAYTPLTDA IHSPGAGGDL WIMGLIVAGL GTILGAVNMI TTVVCMRAPG MTMFRMPIFT WNIMVTSILI LIAFPLLTAA LFGLAADRHL GAHIYDAANG GVLLWQHLFW FFGHPEVYII ALPFFGIVSE IFPVFSRKPI FGYTTLVYAT LSIAALSVAV WAHHMFATGA VLLPFFSFMT YLIAVPTGIK FFNWIGTMWK GQLTFETPML FSVGFMVTFL LGGLTGVLLA SPPLDFHVTD SYFVVAHFHY VLFGTIVFAT FAGIYFWFPK MTGRLLDERL GKLHFWLTFI GFHTTFLVQH WLGDEGMPRR YADYLPTDGF QGLNVVSTIG AFILGASMFP FVWNVFKSWR YGEVVTVDDP WGYGNSLEWA TSCPPPRHNF TELPRIRSER PAFELHYPHM VERLRAEAHV GRHHDEPAMV TSS //