ID A0A1Q1PQG0_9TELE Unreviewed; 516 AA. AC A0A1Q1PQG0; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 26-FEB-2020, entry version 10. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=COI {ECO:0000313|EMBL:AQM74051.1}; OS Poropuntius normani. OG Mitochondrion {ECO:0000313|EMBL:AQM74051.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Poropuntius. OX NCBI_TaxID=643356 {ECO:0000313|EMBL:AQM74051.1}; RN [1] {ECO:0000313|EMBL:AQM74051.1} RP NUCLEOTIDE SEQUENCE. RA Song H.Y., Kim K.Y., Choi S.H., Bang I.C.; RT "Phylogenetic Relationships of Poropuntius (Teleostei; Cypriniformes) RT species in the Bolaven Plateau, Laos."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. 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 ECO:0000256|SAAS:SAAS01116619}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887552}. 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; KY319984; AQM74048.1; -; Genomic_DNA. DR EMBL; KY319985; AQM74049.1; -; Genomic_DNA. DR EMBL; KY319986; AQM74050.1; -; Genomic_DNA. DR EMBL; KY319987; AQM74051.1; -; Genomic_DNA. DR EMBL; KY319988; AQM74052.1; -; Genomic_DNA. DR EMBL; KY319989; AQM74053.1; -; Genomic_DNA. DR EMBL; KY319990; AQM74054.1; -; Genomic_DNA. DR EMBL; KY319991; AQM74055.1; -; Genomic_DNA. DR EMBL; KY319992; AQM74056.1; -; Genomic_DNA. DR EMBL; KY319993; AQM74057.1; -; Genomic_DNA. DR EMBL; KY319994; AQM74058.1; -; Genomic_DNA. DR EMBL; KY319995; AQM74059.1; -; Genomic_DNA. DR EMBL; KY319996; AQM74060.1; -; Genomic_DNA. DR EMBL; KY319997; AQM74061.1; -; Genomic_DNA. DR EMBL; KY319998; AQM74062.1; -; Genomic_DNA. DR EMBL; KY319999; AQM74063.1; -; Genomic_DNA. DR EMBL; KY320000; AQM74064.1; -; Genomic_DNA. DR EMBL; KY320001; AQM74065.1; -; Genomic_DNA. DR EMBL; KY320002; AQM74066.1; -; Genomic_DNA. DR EMBL; KY320003; AQM74067.1; -; Genomic_DNA. DR EMBL; KY320004; AQM74068.1; -; Genomic_DNA. DR EMBL; KY320005; AQM74069.1; -; Genomic_DNA. DR EMBL; KY320006; AQM74070.1; -; Genomic_DNA. DR EMBL; KY320007; AQM74071.1; -; Genomic_DNA. DR EMBL; KY320008; AQM74072.1; -; Genomic_DNA. DR EMBL; KY320009; AQM74073.1; -; Genomic_DNA. DR EMBL; KY320010; AQM74074.1; -; Genomic_DNA. DR EMBL; KY320011; AQM74075.1; -; Genomic_DNA. DR EMBL; KY320012; AQM74076.1; -; Genomic_DNA. DR EMBL; KY320013; AQM74077.1; -; Genomic_DNA. DR EMBL; KY320014; AQM74078.1; -; Genomic_DNA. DR EMBL; KY320015; AQM74079.1; -; 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; 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 Copper {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887236}; KW Electron transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711094}; KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161}; KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711155}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:AQM74051.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711097}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711106}; 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}; KW Transport {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 15..37 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..83 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..128 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 148..171 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 183..210 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 243..261 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 268..291 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 303..327 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 379..400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 412..436 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 448..473 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..511 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 516 AA; 56860 MW; AD999D3B51498879 CRC64; MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGSLLGD DQIYNVIVTA HAFVMIFFMV MPILIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTTIN MKPPAISQYQ TPLFVWSVLV TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PKVYILILPG FGIISHVVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPMLW ALGFIFLFTV GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AAFVHWFPLL TGYTLHSAWT KIHFAVMFIG VNLTFFPQHF LGLAGMPRRY SDYPDAYALW NTVSSIGSLI SLVAVIMFLF ILWEAFAAKR EVLSVELTMT NVEWLHGCPP PYHTYEEPAF VQIQSN //