ID COX1_RICFE Reviewed; 532 AA. AC Q4ULU5; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 117. 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; Synonyms=coxA; OrderedLocusNames=RF_0627; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). 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; CP000053; AAY61478.1; -; Genomic_DNA. DR AlphaFoldDB; Q4ULU5; -. DR SMR; Q4ULU5; -. DR STRING; 315456.RF_0627; -. DR KEGG; rfe:RF_0627; -. DR eggNOG; COG0843; Bacteria. DR HOGENOM; CLU_011899_7_3_5; -. DR OrthoDB; 9803294at2; -. DR UniPathway; UPA00705; -. DR Proteomes; UP000008548; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro. 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; cd01663; Cyt_c_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; IPR033944; Cyt_c_oxase_su1_dom. 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; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..532 FT /note="Probable cytochrome c oxidase subunit 1" FT /id="PRO_0000280885" FT TRANSMEM 33..53 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 95..115 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 163..183 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 200..220 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 252..272 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 284..304 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 318..338 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 355..375 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 394..414 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 431..451 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 473..493 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 79 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:0000250" FT BINDING 258 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 262 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 307 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250" FT BINDING 393 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:0000250" FT BINDING 395 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:0000250" SQ SEQUENCE 532 AA; 58834 MW; 8DB5305BDF07B274 CRC64; MDITTTEIYH DDHHTPHGWK RWLFSTNHKD IGIMYIIFAV FAGIVGGLFS LLFRLELAMP GGTFLNHDFQ LYNVLITAHA VIMVFFMIMP ALFGGFGNYF VPLLIGAPDM AFPRLNNISF WLLVTAFILL MGSAFVDGGP GTGWTLYPPL SNLSGHPGAA VDMAIFSLHL TGLSSILGSI NLIVTIFNMR APGMGLFKMP LFVWSILVTA FLIILAMPVL GGAITMLLTD RNFGTNFFKP DGGGDPVLFQ HLFWFFGHPE VYIVILPGFG IVSQVISTFS RKPIFGYQGM VGAMVIIGFV GFIVWAHHMF TVGLSYNALI YFTAGTMIIA VPTGIKIFSW IATMWGGSIT FPTPMLFSIG FIILFTIGGV TGIILSNSAL DRVLHDTYYV VAHFHYTMSL GALFTAFAGF YYWFGKISGK QYPEILGKIH FWITFIGVNL TFFPQHFLGL AGMPRRIPDY PEAFAGWNMV SSIGAGISMA AALYFVFIVF YTLKYGKDCP NNPWGDGADT LEWTLTSPPP FHTFETPPHI EG //