ID A0A1Y0K3V8_9HYME Unreviewed; 196 AA. AC A0A1Y0K3V8; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 11-DEC-2019, entry version 8. 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; OS Exoneurella tridentata. OG Mitochondrion {ECO:0000313|EMBL:ARU79597.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae; OC Exoneurella. OX NCBI_TaxID=78189 {ECO:0000313|EMBL:ARU79597.1}; RN [1] {ECO:0000313|EMBL:ARU79597.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WP026SW17T {ECO:0000313|EMBL:ARU79597.1}; RA Dew R.M., Stevens M.I., Gardner M.G., Schwarz M.P.; RT "Mixed responses of arid-adapted bees to the Last Glacial Maximum: The role RT of behaviour in responses to climate change."; RL Submitted (DEC-2016) 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 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.3.1; 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; KY314605; ARU79597.1; -; 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: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; 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 PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 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|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:ARU79597.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..196 FT /note="Cytochrome c oxidase subunit 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5012891959" FT TRANSMEM 49..73 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 85..113 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 133..157 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 169..191 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..196 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ARU79597.1" FT NON_TER 196 FT /evidence="ECO:0000313|EMBL:ARU79597.1" SQ SEQUENCE 196 AA; 22000 MW; C8AC77B0DF4E5211 CRC64; NISFWLLPPS LFLLLLSNLF NPSSGTGWTV YPPLSSYIFH SSPSVDLTIF SLHMSGISSI LGAMNFMVTI MMMKNLSLNY DYITLFSWSV FITAILLLLS LPVLAGAITM LLFDRNFNTS FFDPMGGGDP VLYQHLFWFF GHPEVYILIL PGFGLISHIV MNESGKKEIF GNLGMIYAMM GIGFLGFIVW AHHMFT //