ID A0A0E3LMX0_METBA Unreviewed; 209 AA. AC A0A0E3LMX0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 02-NOV-2016, entry version 9. DE RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000256|HAMAP-Rule:MF_01017}; DE EC=1.6.5.2 {ECO:0000256|HAMAP-Rule:MF_01017}; DE AltName: Full=NAD(P)H:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017}; GN ORFNames=MSBRM_0758 {ECO:0000313|EMBL:AKB53756.1}; OS Methanosarcina barkeri MS. OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=1434108 {ECO:0000313|EMBL:AKB53756.1, ECO:0000313|Proteomes:UP000033033}; RN [1] {ECO:0000313|EMBL:AKB53756.1, ECO:0000313|Proteomes:UP000033033} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS {ECO:0000313|EMBL:AKB53756.1, RC ECO:0000313|Proteomes:UP000033033}; RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D., RA Metcalf M.E., Whitaker R.J., Metcalf W.W.; RT "Methanogenic archaea and the global carbon cycle."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: NAD(P)H + a quinone = NAD(P)(+) + a CC hydroquinone. {ECO:0000256|HAMAP-Rule:MF_01017}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01017}; CC Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_01017}; CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000256|HAMAP- CC Rule:MF_01017}. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. {ECO:0000256|HAMAP- CC Rule:MF_01017}. 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; CP009528; AKB53756.1; -; Genomic_DNA. DR RefSeq; WP_048119642.1; NZ_CP009528.1. DR EnsemblBacteria; AKB53756; AKB53756; MSBRM_0758. DR GeneID; 24885586; -. DR KEGG; mby:MSBRM_0758; -. DR KO; K03809; -. DR Proteomes; UP000033033; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.360; -; 1. DR HAMAP; MF_01017; NQOR; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR001226; Flavodoxin_CS. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR010089; Flavoprotein_WrbA. DR InterPro; IPR005025; FMN_Rdtase-like. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR TIGRFAMs; TIGR01755; flav_wrbA; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000033033}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01017}; KW FMN {ECO:0000256|HAMAP-Rule:MF_01017}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01017}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01017}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01017}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01017}. FT DOMAIN 4 199 Flavodoxin-like. {ECO:0000259|PROSITE: FT PS50902}. FT NP_BIND 10 14 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. FT NP_BIND 119 171 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. FT BINDING 107 107 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01017}. FT BINDING 143 143 FMN. {ECO:0000256|HAMAP-Rule:MF_01017}. SQ SEQUENCE 209 AA; 22826 MW; A9C678819A152576 CRC64; MVKVNVIFHS IHGHTYKMAE AIAEGAREVE GAEVGIYQVP ETLPYEVLEK MGAIETKNLF AHIPVVTRSM YEDVFAGADA LIFGTPTRYG NMSAQMRTVF DGLGGLWSRD ALVGKVGSVF TSSGTQHGGQ ESTILTTHVT LLHLGMIIVG LPYSENRQRR MDEITGGSPY GASTIAGAEE NRQPSENELA MARYQGRHVT QIAKKLTRK //