ID A0A0A0Q1M9_9CUCU Unreviewed; 205 AA. AC A0A0A0Q1M9; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 17-JUN-2020, entry version 18. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AHZ00862.1}; OS Cymbeba annulipes. OG Mitochondrion {ECO:0000313|EMBL:AHZ00862.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Coleoptera; Polyphaga; Cucujiformia; Tenebrionidae; OC Cymbeba. OX NCBI_TaxID=1470749 {ECO:0000313|EMBL:AHZ00862.1}; RN [1] {ECO:0000313|EMBL:AHZ00862.1} RP NUCLEOTIDE SEQUENCE. RA Kergoat G.J., Soldati L., Clamens A.-L., Jourdan H., Jabbour-Zahab R., RA Genson G., Bouchard P., Condamine F.L.; RT "Higher level molecular phylogeny of darkling beetles (Coleoptera: RT Tenebrionidae)."; RL Syst. Entomol. 39:486-499(2014). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {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=7.1.1.9; 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; KJ003245; AHZ00862.1; -; 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 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}; 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:AHZ00862.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 47..73 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 94..116 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 136..161 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 173..200 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..205 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHZ00862.1" FT NON_TER 205 FT /evidence="ECO:0000313|EMBL:AHZ00862.1" SQ SEQUENCE 205 AA; 22095 MW; 45778F0DF9125FE5 CRC64; NHKDIGTLYF IFGAWSGMVG TSLSLLIRAE LGNPGSLIGD DQIYNVIVTA HAFIMIFFMV MPIMIGGFGN WLVPLMLGAP DMAFPRMNNM SFWLLPPSLT LLIMSSVVEN GAGTGWTVYP PLSSNIAHSG SSVDLAIFSL HLAGISSIXG AVNFITTVIN MRPQGMTLDR MPLFVWSVVI TAILLLLSLP VLAGAITMLL TDRNI //