ID A0A059SQK8_LIBQU Unreviewed; 382 AA. AC A0A059SQK8; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 14-OCT-2015, entry version 7. 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:AHA51587.1}; OS Libellula quadrimaculata (Four-spotted chaser dragonfly) (Libellula OS quadripunctata). OG Mitochondrion {ECO:0000313|EMBL:AHA51587.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Palaeoptera; Odonata; Anisoptera; Libellulidae; Libellula. OX NCBI_TaxID=70395 {ECO:0000313|EMBL:AHA51587.1}; RN [1] {ECO:0000313|EMBL:AHA51587.1} RP NUCLEOTIDE SEQUENCE. RA Kim M.J., Jung K.S., Park N.S., Wan X., Kim K.-G., Jun J., Yoon T.J., RA Bae Y.J., Lee S.M., Kim I.; RT "Molecular phylogeny of the higher taxa of Odonata (Insecta) inferred RT from COI, 16S rRNA, 28S rRNA, and EF1-a sequences."; RL Entomol. Res. 44:65-79(2014). 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; KF257060; AHA51587.1; -; 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: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; IPR023615; Cyt_c_Oxase_su1_BS. 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. DR PROSITE; PS00077; COX1_CUB; 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, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AHA51587.1}; 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 ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 131 158 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 206 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 239 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 251 274 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 286 307 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 327 348 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 360 379 Helical. {ECO:0000256|SAM:Phobius}. FT NON_TER 1 1 {ECO:0000313|EMBL:AHA51587.1}. FT NON_TER 382 382 {ECO:0000313|EMBL:AHA51587.1}. SQ SEQUENCE 382 AA; 41625 MW; 1B1352FD50F63105 CRC64; IYNVIVTAHA FVMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRLNNMSF WLLPPSFTLL LASSMVESGA GTGWTVYPPL AGAIAHAGAS VDLTIFSLHL AGVSSILGAI NFITTVINMK SPGMKMDQMP LFVWAVVITA VLLLLSLPVL AGAITMLLTD RNINTSFFDP AGGGDPILYQ HLFWFFGHPE VYILILPGFG MISHIIAQES GKKETFGVLG MIYAMVAIGI LGFVVWAHHM FTVGMDVDTR AYFTSATMVI AVPTGIKIFS WLATLHGTQF SYSPSLLWAL GFVFLFTIGG LTGVVLANSS IDITLHDTYY VVAHFHYVLS MGAVFAIMGG LVQWFSLFTG VTLNNHLLKI QFLIMFIGVN LTFFPQHFLG LS //