ID A0A0E3LMX0_METBA Unreviewed; 209 AA. AC A0A0E3LMX0; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 24-JAN-2024, entry version 30. 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}; DE Short=NQO {ECO:0000256|HAMAP-Rule:MF_01017}; GN ORFNames=MSBRM_0758 {ECO:0000313|EMBL:AKB53756.1}; OS Methanosarcina barkeri MS. OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; 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: CC Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); CC Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01017}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); CC Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01017}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01017}; CC Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_01017}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; CC -!- SIMILARITY: Belongs to the SsuE family. Isf subfamily. CC {ECO:0000256|ARBA:ARBA00038292}. CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000256|ARBA:ARBA00006961, CC ECO:0000256|HAMAP-Rule:MF_01017}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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 AlphaFoldDB; A0A0E3LMX0; -. DR STRING; 1434108.MSBRM_0758; -. DR GeneID; 24885586; -. DR KEGG; mby:MSBRM_0758; -. DR PATRIC; fig|1434108.4.peg.915; -. DR HOGENOM; CLU_051402_0_2_2; -. DR Proteomes; UP000033033; Chromosome. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA. 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_sf. DR InterPro; IPR010089; Flavoprotein_WrbA-like. DR InterPro; IPR005025; FMN_Rdtase-like. DR InterPro; IPR037513; NQO. DR NCBIfam; TIGR01755; flav_wrbA; 1. DR PANTHER; PTHR30546; FLAVODOXIN-RELATED PROTEIN WRBA-RELATED; 1. DR PANTHER; PTHR30546:SF23; FLAVOPROTEIN-LIKE PROTEIN YCP4-RELATED; 1. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; 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 FT /note="Flavodoxin-like" FT /evidence="ECO:0000259|PROSITE:PS50902" FT BINDING 10..15 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017" FT BINDING 87..89 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017" FT BINDING 107 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017" FT BINDING 143 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="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 //