ID A0A023HUX4_9MUSC Unreviewed; 190 AA. AC A0A023HUX4; 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:AGR66661.1}; GN Name=COI {ECO:0000313|EMBL:AGR66661.1}; OS Bactrocera chorista. OG Mitochondrion {ECO:0000313|EMBL:AGR66661.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Tephritoidea; Tephritidae; Bactrocera; Zeugodacus. OX NCBI_TaxID=639399 {ECO:0000313|EMBL:AGR66661.1}; RN [1] {ECO:0000313|EMBL:AGR66661.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=18 {ECO:0000313|EMBL:AGR66661.1}; RA Morrow J.L., Frommer M., Shearman D.C.A., Riegler M.; RT "Latitudinally restricted incidence and sharing of Wolbachia in RT Australian tephritid fruit flies."; RL Submitted (FEB-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; KC581375; AGR66661.1; -; 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:AGR66661.1}; 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:AGR66661.1}. FT NON_TER 190 190 {ECO:0000313|EMBL:AGR66661.1}. SQ SEQUENCE 190 AA; 21494 MW; 43DB03F8ACFE171A CRC64; ATLHGTQLNY SPAMLWALGF VFLFTVGGLT GVVLANSSVD IILHDTYYVV AHFHYVLSMG AVFAIMAGFV HWYPLFTGLV LNPKWLKTQF IIMFIGVNLT FFPQHFLGLA GMPRRYSDYP DAYTTWNVVS TIGSSISLLG ILFFLFIIWE SLVTQRQVIY PMQLSSSIEW LQNTPPAEHS YSELPLLINF //