ID A0A6B9SYV2_9STRA Unreviewed; 427 AA. AC A0A6B9SYV2; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 14-DEC-2022, entry version 7. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=cox1 {ECO:0000313|EMBL:QHJ86646.1}; OS Phytophthora cf. sp. sylvatica 3. OG Mitochondrion {ECO:0000313|EMBL:QHJ86646.1}. OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae; OC Phytophthora. OX NCBI_TaxID=2692154 {ECO:0000313|EMBL:QHJ86646.1}; RN [1] {ECO:0000313|EMBL:QHJ86646.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=VN222 {ECO:0000313|EMBL:QHJ86646.1}; RA Jung T., Scanu B., Brasier C., Webber J., Milenkovic I., Corcobado T., RA Tomsovsky M., Panek M., Bakonyi J., Maia C., Bacova A., Raco M., Rees H., RA Perez-Sierra A., Horta Jung M.; RT "A survey in natural forest ecosystems in Vietnam reveals high diversity of RT both new and described Phytophthora taxa including P. ramorum."; RL Forests 11:0-93(2020). 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] + 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:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane CC protein {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; MN866081; QHJ86646.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6B9SYV2; -. 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; -; 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 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 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QHJ86646.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 26..53 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 74..96 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 116..141 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 153..180 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 213..232 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 239..260 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 272..295 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 307..326 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 378..400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..427 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QHJ86646.1" FT NON_TER 427 FT /evidence="ECO:0000313|EMBL:QHJ86646.1" SQ SEQUENCE 427 AA; 46837 MW; 3816EDC77BFE69E9 CRC64; LSLLIRMELA QPGNQIFMGN HQLYNVIVTA HAFIMVFFLV MPALIGGFGN WFVPLMIGAP DMAFPRMNNI SFWLLPPALL LLVSSAIVES GAGTGWTVYP PLSSVQAHSG PSVDLAIFSL HLTGISSLLG AINFISTIYN MRAPGLSFHR LPLFVWSVLI TAFLLLLTLP VLAGAITMLL TDRNLNTSFY DPSGGGDPVL YQHLFWFFGH PEVYILILPA FGIISQVAAA FAKKNVFGYL GMVYAMLSIG LLGCIVWAHH MFTVGLDVDT RAYFSAATMI IAVPTGIKIF SWLATLWGGS LKFETPLLFV LGFILLFVMG GVTGVAMSNS GLDIAIHDTY YIVGHFHYVL SMGAVFGIFT GFYFWIGKIS GRRYPEVLGQ IHFWLFFIGV NITFFPMHFL GLAGMPRRIP DFPDAMSGWN AVSSFGS //