ID H9XHB4_9DIPT Unreviewed; 136 AA. AC H9XHB4; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 05-SEP-2012, entry version 3. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE Flags: Fragment; GN Name=COI; OS Culicoides clastrieri. OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; OC Ceratopogonidae; Ceratopogoninae; Culicoides; Oecacta. OX NCBI_TaxID=1168194; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KKCLA02; RA Ander M., Chirico J., Troell K.; RT "Barcoding of Swedish Culicoides fauna as a tool for rapid and RT accurate species determination for potential vectors of bluetongue RT virus."; RL Submitted (FEB-2012) 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. 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; JQ620057; AFG73732.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC. PE 3: Inferred from homology; KW Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Respiratory chain; Transmembrane; Transport. FT NON_TER 1 1 FT NON_TER 136 136 SQ SEQUENCE 136 AA; 14438 MW; 0FEC39CBB4568B9E CRC64; PPSLSLLLVS SLVENGAGTG WTVYPPLSAN VSHAGASVDL AIFSLHLAGI SSILGAVNFI TTIINMRSSG ISFDRMPLFV WSVLITAILL LLSLPVLAGA ITMLLTDRNI NTSFFDPAGG GDPILYQHLF WFFGHP //