ID J7EIJ6_9NEOP Unreviewed; 339 AA. AC J7EIJ6; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 11-DEC-2019, entry version 26. 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=CO1 {ECO:0000313|EMBL:ADP01204.1}; OS Spodoptera pectinicornis. OG Mitochondrion {ECO:0000313|EMBL:ADP01204.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; Noctuoidea; OC Noctuidae; Amphipyrinae; Spodoptera. OX NCBI_TaxID=134412 {ECO:0000313|EMBL:ADP01204.1}; RN [1] {ECO:0000313|EMBL:ADP01204.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22939903; DOI=10.1016/j.ympev.2012.08.006; RA Kergoat G.J., Prowell D.P., Le Ru B.P., Mitchell A., Dumas P., RA Clamens A.L., Condamine F.L., Silvain J.F.; RT "Disentangling dispersal, vicariance and adaptive radiation patterns: A RT case study using armyworms in the pest genus Spodoptera (Lepidoptera: RT Noctuidae)."; RL Mol. Phylogenet. Evol. 65:855-870(2012). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {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=1.9.3.1; 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; HQ177401; ADP01204.1; -; 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:ADP01204.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1..28 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 29..339 FT /note="Cytochrome c oxidase subunit 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003791722" FT TRANSMEM 58..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 96..123 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 156..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..204 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 216..238 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 250..270 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 290..309 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 321..338 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..339 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ADP01204.1" FT NON_TER 339 FT /evidence="ECO:0000313|EMBL:ADP01204.1" SQ SEQUENCE 339 AA; 37293 MW; 4503868C17DE1742 CRC64; GSPDMAFPRL NNMSFWLLPP SLTLLISSSI VENGAGTGWT VYPPLSSNIA HGGSSVDLAI FSLHLAGISS ILGAINFITT IINMRLNNLS FDQMPLFVWA VGITAFLLLL SLPVLAGAIT MLLTDRNLNT SFFDPAGGGD PILYQHLFWF LDTPKFMFXF LPGFGMISHI ISQESGKKET FGCLGMIYAM LAIGLLGFIV WAHHMFTVGM DIDTRAYFTS ATMIIAVPTG IKIFSWLATF HGTQINYSPS ILWSLGFVFL FTVGGLTGVI LSNSSIDITL HDTYYVVAHF HYVLSMGAVF AILGGFIHWY PLFTGLSLNP YMLKIQFFIM FIGVNLTFF //