ID COX1_CANAL Reviewed; 531 AA. AC P0C8K9; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 03-MAY-2023, entry version 70. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=COX1; GN OrderedLocusNames=CM_00210W {ECO:0000312|CGD:CAL0000187344}; GN ORFNames=CaalfMp08; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OG Mitochondrion. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=11208783; DOI=10.1128/jb.183.3.865-872.2001; RA Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T., RA Kohn L.M.; RT "Infrequent genetic exchange and recombination in the mitochondrial genome RT of Candida albicans."; RL J. Bacteriol. 183:865-872(2001). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00401}. 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 Evidence={ECO:0000250|UniProtKB:P00401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC Note=Binds 2 heme A groups non-covalently per subunit. CC {ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000250|UniProtKB:P00401}. CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00401}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00401}. 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; AF285261; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; P0C8K9; -. DR SMR; P0C8K9; -. DR STRING; 237561.P0C8K9; -. DR EnsemblFungi; CM_00210W-T; CM_00210W-T-p1; CM_00210W. DR CGD; CAL0000187344; COX1. DR VEuPathDB; FungiDB:CM_00210W; -. DR InParanoid; P0C8K9; -. DR UniPathway; UPA00705; -. DR Proteomes; UP000000559; Mitochondrion. DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISS:CGD. DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISS:CGD. 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; IBA:GO_Central. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISS:CGD. 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 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 Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..531 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000356866" FT TRANSMEM 18..38 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 59..79 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 103..123 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 149..169 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 185..205 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 237..257 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 269..289 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 312..332 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 340..360 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 385..405 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 414..434 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 458..478 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 41 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 46 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 64 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 243 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 247 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 292 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 293 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 370 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 2" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 371 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 2" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 378 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_note="high-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 380 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 443 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT CROSSLNK 243..247 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00401" SQ SEQUENCE 531 AA; 58744 MW; EDB63911A328C6AA CRC64; MSYVTRWLFS TSHKDIGILY LIYGMVSAMV ATGMSVIIRL ELSGPGPMFL HGNNQVFNVL VTGHAIAMIF LFVMPILIGS FGNYFLPIMI GAVDMAFARL NNISFWCLPP ALVCVIASVL IETGAGTGWT VYPPLSSISA HSGPSVDLAI FAIHLTSISS LLGAINFIVT TLNMRSIGIH MIDMPLFVWA IFFTAILLLL SLPVLTAGVT LLLMDRNFNT GFYEVAAGGD PILYEHLFYF FGHPEVYIII IPGFGIISHV ISTYTKKPIF GQIGMIYAIG SIGLLGFLVW SHHMYVVGLD IDSRAYFTSA TMVIAIPTGI KIFSWLATLY GGELRLAVPM LFALGFLFLF TIGGLTGVML SNASIDVAFH DTYYVVGHFH YVLSMGALFS LIAGYYYWGP AMFGLKYNKV LAEVHYWLLF VSVNIIFLPM HFLGLNGMPR RIPQYPDAFV GWNVVSSWGS IMSVISVLIG LYSVLVQLTN GENEREEIQV TPDYLESNNT RDVRDSDLEL ITSRPAQYHT FSELPILIQQ I //