ID A0A679EW98_SCAAR Unreviewed; 173 AA. AC A0A679EW98; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 12-AUG-2020, entry version 2. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 6 {ECO:0000256|RuleBase:RU004430}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU004430}; GN Name=ND6 {ECO:0000313|EMBL:BBU26161.1}; OS Scatophagus argus (Spotted scat) (Chaetodon argus). OG Mitochondrion {ECO:0000313|EMBL:BBU26161.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Scatophagidae; Scatophagus. OX NCBI_TaxID=75038 {ECO:0000313|EMBL:BBU26161.1}; RN [1] {ECO:0000313|EMBL:BBU26161.1} RP NUCLEOTIDE SEQUENCE. RA Miya M.; RT "The ray-finned fish phylogeny."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|ARBA:ARBA00002539, ECO:0000256|RuleBase:RU004430}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC Evidence={ECO:0000256|RuleBase:RU004430}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC membrane {ECO:0000256|ARBA:ARBA00004225, CC ECO:0000256|RuleBase:RU004430}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004225, ECO:0000256|RuleBase:RU004430}. CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. CC {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004430}. 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; AP006826; BBU26161.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.1200; -; 1. DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6. DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ. DR Pfam; PF00499; Oxidored_q3; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU004430}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004430}; KW Mitochondrion {ECO:0000256|RuleBase:RU004430, ECO:0000313|EMBL:BBU26161.1}; KW NAD {ECO:0000256|RuleBase:RU004430}; KW Respiratory chain {ECO:0000256|RuleBase:RU004430}; KW Signal {ECO:0000256|SAM:SignalP}; KW Translocase {ECO:0000256|RuleBase:RU004430}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU004430}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU004430}; Transport {ECO:0000256|RuleBase:RU004430}; KW Ubiquinone {ECO:0000256|RuleBase:RU004430}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..173 FT /note="NADH-ubiquinone oxidoreductase chain 6" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5025571445" FT TRANSMEM 49..70 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004430" FT TRANSMEM 91..114 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004430" FT TRANSMEM 134..159 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU004430" SQ SEQUENCE 173 AA; 18337 MW; 7FF0C5DB3B72022D CRC64; MTWVFYLFLG GVVLGAMAVA SNPSPHYSAF GMVFVAGCGG VLLMSQGMIF LGMLLFLIYL GGMLIVFMFA NALASEAHPM AWGSQGAGFS AGVYTCIVAL AYVMLGEGWG GFFWHSVEEL NGFSMFRGDL GGVALMYSMG GGMLVISAWV LLLTLFVVLE LTRGLSRGAL RAV //