ID D0Z677_9TELE Unreviewed; 516 AA. AC D0Z677; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 30-NOV-2016, entry version 36. 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:BAI50171.1}; OS Bathytroctes breviceps. OG Mitochondrion {ECO:0000313|EMBL:BAI50171.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Alepocephali; OC Alepocephaliformes; Alepocephalidae; Bathytroctes. OX NCBI_TaxID=492029 {ECO:0000313|EMBL:BAI50171.1}; RN [1] {ECO:0000313|EMBL:BAI50171.1} RP NUCLEOTIDE SEQUENCE. RA Poulsen J.Y., Moller P.R., Lavoue S., Knudsen S.W., Nishida M., RA Miya M.; RT "Higher and lower-level relationships of the deep-sea fish order RT Alepocephaliformes (Teleostei: Otocephala) inferred from whole RT mitogenome sequences."; RL Biol. J. Linn. Soc. Lond. 98:923-936(2009). 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 ECO:0000256|SAAS:SAAS00634758}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00634716}. 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; AP009576; BAI50171.1; -; Genomic_DNA. DR RefSeq; YP_003331265.1; NC_013574.1. DR GeneID; 8656288; -. DR CTD; 4512; -. 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: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 CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. 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:SAAS00640849}; 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:0000256|SAAS:SAAS00634733, ECO:0000313|EMBL:BAI50171.1}; 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 104 126 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 146 171 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 303 326 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 338 359 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; 56837 MW; 1D7709962E9204FE CRC64; MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGALLGD DQIYNVIVTA HAFVMIFFMV MPIMIGGFGN WLLPLMLGAP DMAFPRMNNM SFWLLPPSLL LLLSSSGVEA GVGTGWTVYP PLAGNLAHAG ASVDLAIFSL HLAGVSSILG SINFITTITN MKPPAISQYQ TPLFVWSLLV TTVLLLLSLP VLAAAITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG FGIVSHVVAY YAGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPLLW ALGFIFLFTV GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFVHWFPLF SGYTLHSTWS KIHFGVMFLG VNLTFFPQHF LGLAGMPRRY SDYPDAYALW NTVSSIGSMI SMVAVIMFLF ILWEAFAAKR EVLSVELTST NVEWLHGCPP PYHTFEEPAF VQVQAN //