ID A0A023HRY2_9TELE Unreviewed; 516 AA. AC A0A023HRY2; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 08-JUN-2016, 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:AGQ46019.1}; OS Phoxinus phoxinus tumensis. OG Mitochondrion {ECO:0000313|EMBL:AGQ46019.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Phoxinus. OX NCBI_TaxID=1347777 {ECO:0000313|EMBL:AGQ46019.1}; RN [1] {ECO:0000313|EMBL:AGQ46019.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23815320; DOI=10.3109/19401736.2013.803096; RA Xu W., Chen A., Xia R., Fu C.; RT "Complete mitochondrial genome of Phoxinus tumensis (Cypriniformes: RT Cyprinidae)."; RL Mitochondrial DNA 25:368-369(2014). 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: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {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; KC992395; AGQ46019.1; -; Genomic_DNA. 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:respiratory chain; 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:0005506; F:iron ion binding; IEA:InterPro. 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; IPR000883; COX1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR023616; 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}; 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, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AGQ46019.1}; 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|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 15 37 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 57 83 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 104 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 148 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 183 210 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 263 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 270 291 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 327 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 339 359 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 379 400 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 412 436 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 473 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 511 COX1. {ECO:0000259|PROSITE:PS50855}. SQ SEQUENCE 516 AA; 56784 MW; 9BDD777C027842B6 CRC64; MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGSLLGD SQIYNVIVTA HAFVMIFFMV MPILIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AVNFITTIIN MKPPAISQYQ TPLFVWAVLV TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG FGIISHVVAY YAGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPMLW ALGFIFLFTV GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AAFVHWFPLF SGYTLNDTWT KIHFGVMFIG VNLTFFPQHF LGLAGMPRRY SDYPDAYALW NTVSSIGSLI SLVAVIMFLF ILWEAFSAKR EVSSVELTMT NVEWLHGCPP PYHTFEEPAF VQVQSN //