ID A0A0G2YJE8_9MUSC Unreviewed; 479 AA. AC A0A0G2YJE8; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 16-JAN-2019, entry version 17. 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; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Opomyzoidea; 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 RT vegetable leafminer Liriomyza sativae (Diptera: Agromyzidae) into the RT Torres Strait 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- 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: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA- CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC 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}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW 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 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 37 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 113 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 133 155 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 167 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 234 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 255 275 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 311 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 323 343 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 363 384 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 396 414 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 434 457 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 479 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AKI84574.1}. FT NON_TER 479 479 {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 //