ID A0A0C4ZQV2_9TELE Unreviewed; 516 AA. AC A0A0C4ZQV2; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 02-OCT-2024, entry version 49. 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}; GN Name=COI {ECO:0000313|EMBL:AJJ48725.1}; OS Cyprinus carpio 'Furong' x Carassius auratus red var. OG Mitochondrion {ECO:0000313|EMBL:AJJ48725.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinoidei intergeneric hybrids. OX NCBI_TaxID=1610701 {ECO:0000313|EMBL:AJJ48725.1}; RN [1] {ECO:0000313|EMBL:AJJ48725.1} RP NUCLEOTIDE SEQUENCE. RA Peng H.Z., Xiao T.Y.; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AJJ48725.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25648921; RA Peng H., Liu Q., Xiao T.; RT "Inheritance of the complete mitochondrial genomes Cyprinus capio RT furong(female symbol) x Cyprinus carpio var.singguonensis(male symbol)."; RL Mitochondrial DNA 1-2:0-0(2015). 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|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; 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; KP210473; AJJ48725.1; -; Genomic_DNA. DR RefSeq; YP_009122667.1; NC_026543.1. DR AlphaFoldDB; A0A0C4ZQV2; -. DR GeneID; 23630067; -. DR CTD; 4512; -. DR UniPathway; UPA00705; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. 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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. 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. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AJJ48725.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 15..37 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..83 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 104..129 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 141..162 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 183..210 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 243..261 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 268..291 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 303..327 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 379..400 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 412..436 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 448..473 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..511 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 516 AA; 56831 MW; 77296CA834C47529 CRC64; MAITRWFFST NHKDIGTLYL VFGAWAGMVG TALSLLIRAE LSQPGSLLGD DQIYNVIVTA HAFVMIFFMV MPILIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSGVEA GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTTIK MKPPAISQYQ TPLFVWSVLV TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH PEVYILILPG FGIISHVVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGG SIKWETPMLW ALGFIFLFTV GGLTGIVLSN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AAFVHWFPLL TGYTLHSTWT KIHFGVMFIG VNLTFFPQHF LGLAGMPRRY SDYPDAYALW NTVSSIGSLI SLVAVIMFLF ILWEAFAAKR EVLSVELTAT NVEWLHGCPP PYHTYEEPAF VQIQSN //