ID A0A075QV66_9TELE Unreviewed; 218 AA. AC A0A075QV66; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 13-SEP-2023, entry version 35. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, 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: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|ARBA:ARBA00009578, 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 AlphaFoldDB; A0A075QV66; -. DR UniPathway; UPA00705; -. 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008, 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|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; 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="Cytochrome oxidase subunit I profile" 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 //