ID A0A0A7B6Z2_9MUSC Unreviewed; 202 AA. AC A0A0A7B6Z2; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 29-APR-2015, entry version 2. 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:AHM14791.1}; OS Drosophilidae sp. BOLD:ABA0755. OG Mitochondrion {ECO:0000313|EMBL:AHM14791.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae. OX NCBI_TaxID=1474152 {ECO:0000313|EMBL:AHM14791.1}; RN [1] {ECO:0000313|EMBL:AHM14791.1} RP NUCLEOTIDE SEQUENCE. RA Dewaard J.R., Dewaard S.L., Brown H., Dobbie I., Ivanova N., Naik S., RA Labbe R., Levesque-beaudin V., Pawlowski A., Ratnasingham S.R., RA Sobel C., Sones J., Young M.R., Zakharov E.V., Hebert P.D.N.; RT "Rapid Barcode-assisted Terrestrial Biomonitoring Point Pelee National RT Park."; RL Submitted (JAN-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; KJ085134; AHM14791.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. 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:AHM14791.1}; 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:AHM14791.1}. FT NON_TER 202 202 {ECO:0000313|EMBL:AHM14791.1}. SQ SEQUENCE 202 AA; 21552 MW; 1534A1C3439C7982 CRC64; TLYFIFGAWA GMVGTSLSIL IRAELGHPGA LIGDDQIYNV IVTAHAFIMI FFMVMPIMIG GFGNWLVPLM LGAPDMAFPR MNNMSFWLLP PALTLLLVSS MVENGAGTGW TVYPPLSSGI AHGGASVDLA IFSLHLAGIS SILGAVNFIT TVINMRSTGI TLDRMPLFVW SVVITALLLL LSLPVLAGAI TMLLTDRNLN TS //