ID A0A023SFC5_9BIVA Unreviewed; 201 AA. AC A0A023SFC5; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 01-OCT-2014, entry version 3. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment {ECO:0000313|EMBL:AHX73839.1}; GN Name=COI {ECO:0000313|EMBL:AHX73839.1}; OS Solenaia oleivora. OG Mitochondrion {ECO:0000313|EMBL:AHX73839.1}. OC Eukaryota; Metazoa; Lophotrochozoa; Mollusca; Bivalvia; OC Palaeoheterodonta; Unionoida; Unionoidea; Unionidae; Unioninae; OC Solenaia. OX NCBI_TaxID=165460 {ECO:0000313|EMBL:AHX73839.1}; RN [1] {ECO:0000313|EMBL:AHX73839.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=146SO4 {ECO:0000313|EMBL:AHX73841.1}, 211SO6 RC {ECO:0000313|EMBL:AHX73843.1}, 72SO2 {ECO:0000313|EMBL:AHX73839.1}, RC and 73SO3 {ECO:0000313|EMBL:AHX73840.1}; RA Uyang J., Wu X., Li S.; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {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; KJ434512; AHX73839.1; -; Genomic_DNA. DR EMBL; KJ434513; AHX73840.1; -; Genomic_DNA. DR EMBL; KJ434514; AHX73841.1; -; Genomic_DNA. DR EMBL; KJ434516; AHX73843.1; -; Genomic_DNA. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AHX73839.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT NON_TER 1 1 {ECO:0000313|EMBL:AHX73839.1}. FT NON_TER 201 201 {ECO:0000313|EMBL:AHX73839.1}. SQ SEQUENCE 201 AA; 21298 MW; 18D9AE6C1EDB9268 CRC64; LSLLIRAELG QPGSLLGDDQ LYNVIVTAHA FMMIFFLVMP MMIGGFGNWL IPLMIGAPDM AFPRLNNLSF WLLVPALFLL LSSSLVESGV GTGWTVYPPL SGNVAHSGAS VDLAIFSLHL AGASSILGAI NFISTVGNMR SPGLVAERIP LFVWAVTVTA VLLVAALPVL AGAITMLLTD RNINTSFFDP TGGGDPILYM H //