ID NQOR_BRUA2 Reviewed; 199 AA. AC Q2YQ23; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=NAD(P)H dehydrogenase (quinone) {ECO:0000255|HAMAP-Rule:MF_01017}; DE EC=1.6.5.2 {ECO:0000255|HAMAP-Rule:MF_01017}; DE AltName: Full=Flavoprotein WrbA; DE AltName: Full=NAD(P)H:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01017}; DE Short=NQO {ECO:0000255|HAMAP-Rule:MF_01017}; GN OrderedLocusNames=BAB1_1070; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). 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:0000255|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:0000255|HAMAP-Rule:MF_01017}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01017}; CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_01017}; CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000255|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; AM040264; CAJ11026.1; -; Genomic_DNA. DR RefSeq; WP_002964168.1; NZ_KN046823.1. DR PDB; 5F4B; X-ray; 2.50 A; A/B=1-199. DR PDB; 5F51; X-ray; 2.53 A; A=1-199. DR PDBsum; 5F4B; -. DR PDBsum; 5F51; -. DR AlphaFoldDB; Q2YQ23; -. DR SMR; Q2YQ23; -. DR STRING; 359391.BAB1_1070; -. DR DNASU; 3787724; -. DR GeneID; 3787724; -. DR KEGG; bmf:BAB1_1070; -. DR PATRIC; fig|359391.11.peg.1781; -. DR HOGENOM; CLU_051402_0_2_5; -. DR PhylomeDB; Q2YQ23; -. DR PHI-base; PHI:9134; -. DR Proteomes; UP000002719; Chromosome I. 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; 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; PROTEIN RFS1-RELATED; 1. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; Flavoproteins; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Flavoprotein; FMN; NAD; NADP; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..199 FT /note="NAD(P)H dehydrogenase (quinone)" FT /id="PRO_0000291007" FT DOMAIN 4..190 FT /note="Flavodoxin-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT REGION 158..181 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 10..15 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT BINDING 12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT BINDING 78..80 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT BINDING 113..119 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT BINDING 134 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017" FT STRAND 3..9 FT /evidence="ECO:0007829|PDB:5F4B" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:5F4B" FT HELIX 14..27 FT /evidence="ECO:0007829|PDB:5F4B" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:5F4B" FT STRAND 32..37 FT /evidence="ECO:0007829|PDB:5F4B" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:5F51" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:5F51" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:5F51" FT HELIX 63..68 FT /evidence="ECO:0007829|PDB:5F4B" FT STRAND 70..79 FT /evidence="ECO:0007829|PDB:5F4B" FT HELIX 85..91 FT /evidence="ECO:0007829|PDB:5F4B" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:5F51" FT HELIX 95..100 FT /evidence="ECO:0007829|PDB:5F4B" FT TURN 101..105 FT /evidence="ECO:0007829|PDB:5F4B" FT STRAND 107..113 FT /evidence="ECO:0007829|PDB:5F4B" FT HELIX 122..133 FT /evidence="ECO:0007829|PDB:5F4B" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:5F4B" FT HELIX 144..157 FT /evidence="ECO:0007829|PDB:5F4B" FT HELIX 177..198 FT /evidence="ECO:0007829|PDB:5F4B" SQ SEQUENCE 199 AA; 21442 MW; 1E70DC2A51E5A676 CRC64; MVKMLVLYYS AYGYMEQMAK AAAEGAREGG AEVTLKRVPE LVPEEVAKAS HYKIDQEVPI ATPGELADYD AIIIGTATRY GMMASQMKNF LDQTGGLWAK GALINKVGSV MVSTATQHGG AELALISTQW QMQHHGMIIV PLSYAYREQM GNDVVRGGAP YGMTTTADGD GSRQPSAQEL DGARFQGRRV AEITAKLHG //