ID Q5IJJ0_9NEOP Unreviewed; 269 AA. AC Q5IJJ0; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 03-AUG-2022, entry version 80. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AAW56264.1}; OS Ithomia iphianassa panamensis. OG Mitochondrion {ECO:0000313|EMBL:AAW56264.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea; OC Nymphalidae; Danainae; Ithomiini; Ithomiina; Ithomia. OX NCBI_TaxID=306001 {ECO:0000313|EMBL:AAW56264.1}; RN [1] {ECO:0000313|EMBL:AAW56264.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15683934; DOI=10.1016/j.ympev.2004.10.021; RA Mallarino R., Bermingham E., Willmott K.R., Whinnett A., Jiggins C.D.; RT "Molecular systematics of the butterfly genus Ithomia (Lepidoptera: RT Ithomiinae): a composite phylogenetic hypothesis based on seven genes."; RL Mol. Phylogenet. Evol. 34:625-644(2005). 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] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; 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: 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|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; AY713064; AAW56264.1; -; Genomic_DNA. DR EMBL; AY713065; AAW56266.1; -; 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: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:AAW56264.1}; 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 23..46 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 58..81 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 93..114 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 126..151 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 163..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 202..228 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..267 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAW56264.1" SQ SEQUENCE 269 AA; 30366 MW; 7079902F78F8BB63 CRC64; LILPGFGMIS HIISQESGKK ETFGSLGMIY AMMAIGLLGF IVWAHHMFTV GMDIDTRAYF TSATMIIAVP TGIKIFSWLA TLHGTQINYS PSILWSLGFV FLFTVGGLTG VILANSSIDI TLHDTYYVVA HFHYVLSMGA VFAILGGFIH WYPLFTGLIM NPYLLKIQFF TMFLGVNITF FPQHFLGLAG MPRRYSDYPD SFMSWNIISS LGSYISLLSM MMIIIIIWES MINQRIILFS LNMPSSIEWY QNLPPAEHSY NELPILSNF //