ID M1X892_PIPNO Unreviewed; 229 AA. AC M1X892; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 07-JAN-2015, entry version 14. 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:CCN27095.1}; OS Pipiza noctiluca (Hoverfly) (Musca noctiluca). OG Mitochondrion {ECO:0000313|EMBL:CCN27095.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Syrphoidea; Syrphidae; Syrphinae; Pipizini; Pipiza. OX NCBI_TaxID=1162231 {ECO:0000313|EMBL:CCN27095.1}; RN [1] {ECO:0000313|EMBL:CCN27095.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FSUNS:J003 {ECO:0000313|EMBL:CCN27095.1}; RA Vujic A., Stahls G., Acanski J., Bartsch H., Bygebjerg R., RA Stefanovic A.; RT "Systematics of Pipizini and taxonomy of European Pipiza Fall.n: RT molecular and morphological evidence (Diptera, Syrphidae)."; RL Zool. Scr. 42:288-305(2013). 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; HF542967; CCN27095.1; -; Genomic_DNA. 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 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:CCN27095.1}; 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:CCN27095.1}. FT NON_TER 229 229 {ECO:0000313|EMBL:CCN27095.1}. SQ SEQUENCE 229 AA; 25908 MW; 8A1DA0E74477B3C3 CRC64; QECGKXETFG SLGMIYAMLS IGILGFIVWA HHMFTIGMDV DTRAYFTSAT MVIAIPTGIK VFSWMATIYG TQLIYSPTMM WALGFVFLFT IGGLTGVVLA NSSIDLILHD TYYVVAHFHY VLSMGAVFAI MTGFIHWYPL FTGLTLNTKW LKTQFTVMFI GVNLTFFPQH FLGLAGMPRR YSDYPDAYTT WNIMSTIGST ISLLAIIMFM IIIWKSMIKQ RQVIYAIQL //