ID COX1_KLULA Reviewed; 534 AA. AC P20386; Q6DN59; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 3. DT 08-NOV-2023, entry version 143. 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; OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica). OG Mitochondrion. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=284590; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 90735 / K8; RX PubMed=1657415; DOI=10.1007/bf00312772; RA Hardy C.M., Clark-Walker G.D.; RT "Nucleotide sequence of the COX1 gene in Kluyveromyces lactis mitochondrial RT DNA: evidence for recent horizontal transfer of a group II intron."; RL Curr. Genet. 20:99-114(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210; RX PubMed=15691736; DOI=10.1016/j.femsyr.2004.09.003; RA Zivanovic Y., Wincker P., Vacherie B., Bolotin-Fukuhara M., Fukuhara H.; RT "Complete nucleotide sequence of the mitochondrial DNA from Kluyveromyces RT lactis."; RL FEMS Yeast Res. 5:315-322(2005). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RC STRAIN=ATCC 90735 / K8; RX PubMed=2171241; DOI=10.1002/yea.320060505; RA Hardy C.M., Clark-Walker G.D.; RT "Nucleotide sequence of the cytochrome oxidase subunit 2 and val-tRNA genes RT and surrounding sequences from Kluyveromyces lactis K8 mitochondrial DNA."; RL Yeast 6:403-410(1990). 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; X57546; CAA40765.1; -; Genomic_DNA. DR EMBL; AY654900; AAT64956.1; -; Genomic_DNA. DR EMBL; X15999; CAA34130.1; -; Genomic_DNA. DR PIR; S17993; S17993. DR RefSeq; YP_054500.1; NC_006077.1. DR AlphaFoldDB; P20386; -. DR SMR; P20386; -. DR STRING; 284590.P20386; -. DR PaxDb; 284590-P20386; -. DR GeneID; 2914076; -. DR KEGG; kla:KllafMp05; -. DR InParanoid; P20386; -. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner 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: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 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 Respiratory chain; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..534 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183348" FT TRANSMEM 16..36 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 57..77 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 101..121 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 182..202 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 267..287 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 338..358 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 372..392 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 412..432 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 452..472 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 39 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 42 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 44 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 62 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 241 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 245 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 290 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 291 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 368 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 369 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 376 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 378 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 441 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT CROSSLNK 241..245 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00401" FT CONFLICT 66 FT /note="I -> M (in Ref. 1; CAA40765)" FT /evidence="ECO:0000305" FT CONFLICT 97..98 FT /note="RL -> KM (in Ref. 1; CAA40765)" FT /evidence="ECO:0000305" FT CONFLICT 237 FT /note="W -> G (in Ref. 1; CAA40765)" FT /evidence="ECO:0000305" SQ SEQUENCE 534 AA; 58798 MW; 9CBF85E4091BA04D CRC64; MIERWLYSTN AKDIAVLYFI FAIFCGMAGT AMSLIIRLEL AAPGNQVLSG NHQLFNVLVV GHAVLIIFFL VMPALIGGFG NYMLPLLIGA SDMSFARLNN ISFWCLPPAL VCLVTSTLVE SGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GAINFIVTTL NMRTNGMTMH RLPLFVWSIF ITAFLLLLSL PVLSAGVTML LLDRNFNTSF FEVAGGGDPV LYQHLFWFFG HPEVYILIIP GFGIISHIVS TYSKKPVFGE VSMVYAMASI GLLGFLVWSH HMYIVGLDAD TRAYFTSATM IIAIPTGIKI FSWLATIYGG SIRLAVPMLY AIAFLFLFTI GGLTGVALAN ASLDVAFHDT YYVVGHFHYV LSMGAIFSLF AGYYYWSPQI LGLYYNEKLA QIQFWLIFVG ANVIFLPMHF LGVNGMPRRI PDYPDAFAGW NYVASIGSII AVFSLFLFIY ILYDQLVNGL ENKVNNKSVI YNKGPDFVES NQIFATNKIK SSSIEFLLTS PPAVHTFNTP AVQS //