ID A0A075CGE7_9HYME Unreviewed; 219 AA. AC A0A075CGE7; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 01-APR-2015, entry version 5. 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; GN Name=COI {ECO:0000313|EMBL:AGZ92549.1}; OS Tapinoma sessile (odorous house ant). OG Mitochondrion {ECO:0000313|EMBL:AGZ92549.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; OC Vespoidea; Formicidae; Dolichoderinae; Tapinoma. OX NCBI_TaxID=29039 {ECO:0000313|EMBL:AGZ92549.1}; RN [1] {ECO:0000313|EMBL:AGZ92549.1} RP NUCLEOTIDE SEQUENCE. RA Smith M.A., Des Brisay P.; RT "A phylogeographic assessment of the transcontinental ant Tapinoma RT sessile Say 1836 (Formicidae: Dolichoderinae): one species?"; RL Submitted (AUG-2013) 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; KF604929; AGZ92387.1; -; Genomic_DNA. DR EMBL; KF604983; AGZ92441.1; -; Genomic_DNA. DR EMBL; KF605007; AGZ92465.1; -; Genomic_DNA. DR EMBL; KF605026; AGZ92484.1; -; Genomic_DNA. DR EMBL; KF605051; AGZ92509.1; -; Genomic_DNA. DR EMBL; KF605066; AGZ92524.1; -; Genomic_DNA. DR EMBL; KF605091; AGZ92549.1; -; Genomic_DNA. DR EMBL; KF605094; AGZ92552.1; -; Genomic_DNA. DR EMBL; KF605123; AGZ92581.1; -; Genomic_DNA. DR EMBL; KF605124; AGZ92582.1; -; Genomic_DNA. DR EMBL; KF605127; AGZ92585.1; -; Genomic_DNA. DR EMBL; KF605139; AGZ92597.1; -; Genomic_DNA. DR EMBL; KF605141; AGZ92599.1; -; Genomic_DNA. DR EMBL; KF605143; AGZ92601.1; -; Genomic_DNA. DR EMBL; KF605150; AGZ92608.1; -; Genomic_DNA. DR EMBL; KF605163; AGZ92621.1; -; Genomic_DNA. DR EMBL; KF605164; AGZ92622.1; -; Genomic_DNA. DR EMBL; KF605192; AGZ92650.1; -; Genomic_DNA. DR EMBL; KF605208; AGZ92666.1; -; Genomic_DNA. DR EMBL; KF605215; AGZ92673.1; -; Genomic_DNA. DR EMBL; KF605268; AGZ92726.1; -; Genomic_DNA. DR EMBL; KF605302; AGZ92760.1; -; Genomic_DNA. DR EMBL; KF605321; AGZ92779.1; -; Genomic_DNA. DR EMBL; KF605324; AGZ92782.1; -; 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:respiratory chain; 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:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. 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}; 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:AGZ92549.1}; 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:AGZ92549.1}. FT NON_TER 219 219 {ECO:0000313|EMBL:AGZ92549.1}. SQ SEQUENCE 219 AA; 23983 MW; 626AC83DBD9386E7 CRC64; LLYFIFAIWS GMIGSSMSMI IRIELGTCGA LINNDQIYNS IVTGHAFIMI FFMVMPFMIG GFGNFLVPLM LGAPDMAYPR MNNMSFWLLP PSILLLTISN FISSGVGTGW TVYPPLASNI YHNGPSVDLA IFSLHIAGMS SILGAINFIS TIINMHHKNF STDKIPLLVW SILITAILLL LSLPVLAGAI TMLLTDRNLN TSFFDPSGGG DPILYQHLF //