ID A0A166HSN9_9TELE Unreviewed; 217 AA. AC A0A166HSN9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 05-DEC-2018, 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}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:ANA09114.1}; OS Capoeta damascina saadii. OG Mitochondrion {ECO:0000313|EMBL:ANA09114.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Capoeta. OX NCBI_TaxID=1051495 {ECO:0000313|EMBL:ANA09114.1}; RN [1] {ECO:0000313|EMBL:ANA09114.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=15_Ex82B4 {ECO:0000313|EMBL:ANA09114.1}, M824_Ex90A3 RC {ECO:0000313|EMBL:ANA09118.1}, M826_Ex90A5 RC {ECO:0000313|EMBL:ANA09117.1}, M830_Ex90A11 RC {ECO:0000313|EMBL:ANA09116.1}, and M832_Ex90A6 RC {ECO:0000313|EMBL:ANA09115.1}; RX PubMed=27394223; DOI=10.11646/zootaxa.4083.1.7; RA Zareian H., Esmaeili H.R., Freyhof J.; RT "Capoeta anamisensis, a new species from the Minab and Hasan Langhi RT River drainages in Iran (Teleostei: Cyprinidae)."; RL Zootaxa 4083:126-142(2016). 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, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399; 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; KU312353; ANA09114.1; -; Genomic_DNA. DR EMBL; KU312354; ANA09115.1; -; Genomic_DNA. DR EMBL; KU312355; ANA09116.1; -; Genomic_DNA. DR EMBL; KU312356; ANA09117.1; -; Genomic_DNA. DR EMBL; KU312357; ANA09118.1; -; 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: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: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 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 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, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:ANA09114.1}; 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 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 36 58 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 92 112 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 132 154 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 166 193 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 217 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:ANA09114.1}. FT NON_TER 217 217 {ECO:0000313|EMBL:ANA09114.1}. SQ SEQUENCE 217 AA; 23093 MW; 1390F64A377BC315 CRC64; LYLVFGAWAG MVGTALSLLI RAELSQPGSL LGDDQIYNVI VTAHAFVMIF FMVMPILIGG FGNWLVPLMI GAPDMAFPRM NNMSFWLLPP SFLLLLASSG VEAGAGTGWT VYPPLSGNLA HAGASVDLTI FSLHLAGVSS ILGAINFITT TINMKPPAIS QYQTPLFVWS VLVTAVLLLL SLPVLAAGIT MLLTDRNLNT TFFDPAGGGD PILYQHL //