ID A0A075QV66_9TELE Unreviewed; 218 AA. AC A0A075QV66; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 11-DEC-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:AIG24285.1}; OS Stegastes nigricans (dusky farmerfish). OG Mitochondrion {ECO:0000313|EMBL:AIG24285.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Pomacentridae; Stegastes. OX NCBI_TaxID=351694 {ECO:0000313|EMBL:AIG24285.1}; RN [1] {ECO:0000313|EMBL:AIG24285.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24935524; RA Hubert N., Espiau B., Meyer C., Planes S.; RT "Identifying the ichthyoplankton of a coral reef using DNA barcodes."; RL Mol. Ecol. Resour. 0:0-0(2014). RN [2] {ECO:0000313|EMBL:QDB65845.1} RP NUCLEOTIDE SEQUENCE. RA Delrieu-trotter E., Williams J., Pitassy D., Driskell A.C., Hubert N., RA Viviani J., Cribb T., Espiau B., Galzin R., Kulbicki M., Lison de loma T., RA Meyer C., Mourier J., Mou-tham G., Parravicini V., Plantard P., Sasal P., RA Siu G., Tolou N., Veuille M., Weigt L., Planes S.; RT "A DNA barcode reference library of the French Polynesian shore fishes."; RL Submitted (MAR-2019) 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 -!- 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; KJ968274; AIG24276.1; -; Genomic_DNA. DR EMBL; KJ968275; AIG24277.1; -; Genomic_DNA. DR EMBL; KJ968276; AIG24278.1; -; Genomic_DNA. DR EMBL; KJ968277; AIG24279.1; -; Genomic_DNA. DR EMBL; KJ968278; AIG24280.1; -; Genomic_DNA. DR EMBL; KJ968279; AIG24281.1; -; Genomic_DNA. DR EMBL; KJ968280; AIG24282.1; -; Genomic_DNA. DR EMBL; KJ968281; AIG24283.1; -; Genomic_DNA. DR EMBL; KJ968282; AIG24284.1; -; Genomic_DNA. DR EMBL; KJ968283; AIG24285.1; -; Genomic_DNA. DR EMBL; KJ968284; AIG24286.1; -; Genomic_DNA. DR EMBL; KJ968285; AIG24287.1; -; Genomic_DNA. DR EMBL; KJ968286; AIG24288.1; -; Genomic_DNA. DR EMBL; KJ968287; AIG24289.1; -; Genomic_DNA. DR EMBL; KJ968288; AIG24290.1; -; Genomic_DNA. DR EMBL; KJ968289; AIG24291.1; -; Genomic_DNA. DR EMBL; KJ968290; AIG24292.1; -; Genomic_DNA. DR EMBL; KJ968291; AIG24293.1; -; Genomic_DNA. DR EMBL; MK657243; QDB65845.1; -; Genomic_DNA. DR EMBL; MK657359; QDB65961.1; -; Genomic_DNA. DR EMBL; MK657569; QDB66171.1; -; 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:respirasome; 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}; 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, ECO:0000313|EMBL:AIG24285.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 6..24 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 36..58 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 92..112 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 132..154 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 166..193 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..218 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIG24285.1" FT NON_TER 218 FT /evidence="ECO:0000313|EMBL:AIG24285.1" SQ SEQUENCE 218 AA; 23281 MW; 0FC1AB61C8124E7A CRC64; LYLVFGAWAG MVGTALSLLI RAELSQPGAL LGDDQIYNVI VTAHAFVMIF FMVMPIMIGG FGNWLIPLMI GAPDMAFPRM NNMSFWLLPP SFLLLLASSG VEAGAGTGWT VYPPLSGNLA HAGASVDLTI FSLHLAGISS ILGAINFITT IINMKPPAIS QYQTPLFVWA VLITAVLLLL SLPVLAAGIT MLLTDRNLNT TFFDPAGGGD PILYQHLF //