ID A0A0G2YJE8_9MUSC Unreviewed; 479 AA. AC A0A0G2YJE8; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 11-DEC-2019, entry version 18. 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:AKI84574.1}; OS Liriomyza cicerina. OG Mitochondrion {ECO:0000313|EMBL:AKI84574.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Opomyzoidea; OC Agromyzidae; Phytomyzinae; Liriomyza. OX NCBI_TaxID=1659330 {ECO:0000313|EMBL:AKI84574.1}; RN [1] {ECO:0000313|EMBL:AKI84574.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lc118 {ECO:0000313|EMBL:AKI84574.1}; RX PubMed=25991411; RA Blacket M.J., Rice A.D., Semeraro L., Malipatil M.B.; RT "DNA-based identifications reveal multiple introductions of the vegetable RT leafminer Liriomyza sativae (Diptera: Agromyzidae) into the Torres Strait RT Islands and Papua New Guinea."; RL Bull. Entomol. Res. 105:533-544(2015). 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; KR476571; AKI84574.1; -; 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: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 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; 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. 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|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AKI84574.1}; 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|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..25 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 37..59 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 133..155 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 214..234 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 255..275 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 287..311 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 323..343 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 363..384 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 396..414 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 434..457 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..479 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AKI84574.1" FT NON_TER 479 FT /evidence="ECO:0000313|EMBL:AKI84574.1" SQ SEQUENCE 479 AA; 52763 MW; CD17FB0C2B46A09D CRC64; TLYFMFGAWA GMVGTSLSIL IRAELGHPGA LIGDDQIYNV IVTAHAFIMI FFMVMPIMIG GFGNWLVPIM LGAPDMAFPR MNNMSFWLLP PALTLLLMSS MVENGAGTGW TVYPPLSSTI AHGGASVDLA IFSLHLAGIS SILGAVNFIT TIINMRSTGI SFDRMPLFVW SVLITAVLLL LSLPVLAGAI TMLLTDRNFN TSFFDPAGGG DPILYQHLFX XXXXXXXXXX XXXXXXXXXX XXXXXXXKKE TFGSLGMIYA MLAIGLLGFI VWAHHMFTVG LDVDTRAYFT SATMIIAVPT GIKIISWLAT FHGTQLSFTP TTLWALGFVF LFTVGGLTGV VLANSSIDVI LHDTYYVVAH FHYVLSMGAV FAIMAGFIHW YPLFTGLSMN TKLLKSQFII MFIGVNLTFF PQHFLGLAGM PRRYSDYPDA YTTWNVISTI GSSISLLGII LFLYIIWESM MTQRQVIFPI QLNSSIEWY //