ID A0A059SQK8_LIBQU Unreviewed; 382 AA. AC A0A059SQK8; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 02-DEC-2020, entry version 24. 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: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; Pterygota; OC Palaeoptera; Odonata; Epiprocta; 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 from RT COI, 16S rRNA, 28S rRNA, and EF1-a sequences."; RL Entomol. Res. 44:65-79(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|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000256|ARBA:ARBA00011164}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|ARBA:ARBA00009578, 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:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro. 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 CDD; cd01663; Cyt_c_Oxidase_I; 1. 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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AHA51587.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..31 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 96..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 131..158 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 178..206 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 218..239 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 251..274 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 286..307 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 327..348 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 360..379 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..382 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AHA51587.1" FT NON_TER 382 FT /evidence="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 //