ID A0A896SSY8_9ASCO Unreviewed; 522 AA. AC A0A896SSY8; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 27-NOV-2024, entry version 9. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; GN Name=cox1 {ECO:0000313|EMBL:QSD56444.1}; OS Metschnikowia bicuspidata. OG Mitochondrion {ECO:0000313|EMBL:QSD56444.1}. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Metschnikowiaceae; Metschnikowia. OX NCBI_TaxID=27322 {ECO:0000313|EMBL:QSD56444.1}; RN [1] {ECO:0000313|EMBL:QSD56444.1} RP NUCLEOTIDE SEQUENCE. RA Ye G.S., Liu N.J.; RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases. 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:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)- CC [cytochrome c] + 2 H2O + 4 H(+)(out); 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:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. 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; MW147605; QSD56444.1; -; Genomic_DNA. DR AlphaFoldDB; A0A896SSY8; -. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter. 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 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. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QSD56444.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 20..40 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 60..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 107..129 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 149..174 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 186..214 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 276..299 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 305..324 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 336..360 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 372..391 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 403..421 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 441..461 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..518 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 522 AA; 58193 MW; 7391EA75DE5234EE CRC64; MSYMTRWLYS TSHKDMAMLY LGYGLMSSMV ATGMSVMMRM ELSGANPQYL NGNNQVYNVM VTGHAMGMMF LFVMPVTIGA FGNYFLPIMM GAVDMAFARL NNMSFWCLPP ALVCVMASLL VENGAGTGWT VYPPLSSMNA HSGPSVDLAI FATHLTSMSS LLGAINFMVT FMNMRTMGLH MMNAPLFVWA MFFTAMLLLL SLPVLTAGVT LLLMDRNFNT GFYEVAAGGD PVLYVRVHKY GYSMKSYIMI MPGFGMMSHM VSTYSKKPIF GEMGMLYAMG SIGTLGFLVW SHHMFVVGLD IDSRAYFTSA TMVMAVPTGI KMWATVPTVY GGEVRLAVPM LFALGFLFTF TIGGVTGVML SNASMDVAFH HFHYVLSMGA LFSTVGGYYY WGPSMFGLNY NKVWAEMHFW LLFMSVNVIF LPMHFFGMPR RMPQYPDAFM GWNYMSSMGS AMSMMSVMVG LKSVQMQLDN GLNEDSEMQV TPDFLESNKM RDVRDSDIEL ILARPAEYHT FSELPVLVTP KV //