ID A0A2Z5WJA3_9ANNE Unreviewed; 219 AA. AC A0A2Z5WJA3; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 19-JAN-2022, entry version 13. 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:BBC08986.1}; OS Sternaspis sp. 4 GK-2017. OG Mitochondrion {ECO:0000313|EMBL:BBC08986.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta; OC Sedentaria; Canalipalpata; Terebellida; Cirratuliformia; Sternaspidae; OC Sternaspis. OX NCBI_TaxID=2060733 {ECO:0000313|EMBL:BBC08986.1}; RN [1] {ECO:0000313|EMBL:BBC08986.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GK49 {ECO:0000313|EMBL:BBC08986.1}; RA Kobayashi G., Mukai R., Alalykina I., Miura T., Kojima S.; RT "Phylogeography of benthic invertebrates in deep waters: A case study of RT Sternaspis cf. williamsae (Annelida: Sternaspidae) from the northwestern RT Pacific Ocean."; RL Deep Sea Res. Part II Top. Stud. Oceanogr. 0:0-0(2018). 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|ARBA:ARBA00004673, 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|ARBA:ARBA00009578, 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; LC341930; BBC08986.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. 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 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 PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 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:BBC08986.1}; 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 46..67 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 88..110 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 130..155 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..219 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BBC08986.1" FT NON_TER 219 FT /evidence="ECO:0000313|EMBL:BBC08986.1" SQ SEQUENCE 219 AA; 23647 MW; 27B3B5F5E62F40ED CRC64; TMYFIFGIWS GLLGTSMSLL VRIELSQPGA LMGNDQIYNV LVTAHAFLMI FFLVMPVLMS GFGNWLIPTL LSAPDMAFPR LNNMSFWLLP PSLILLTMSA VVEGGVGTGW TVYPPLSNNI FHSGPSVDLA IFSLHLAGVS SILGSLNFIT TALNMRPAGM TPERTPLFVW AVAITGLLLV LSIPVLAAGI TMLLTDRNLN TSFFDPTGGG DPVLFQHLF //