NQOR_BRUA2
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 03-AUG-2022, entry version 88.
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; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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 EnsemblBacteria; CAJ11026; CAJ11026; BAB1_1070.
DR GeneID; 3787724; -.
DR KEGG; bmf:BAB1_1070; -.
DR PATRIC; fig|359391.11.peg.1781; -.
DR HOGENOM; CLU_051402_0_2_5; -.
DR OMA; KFADGNP; -.
DR PhylomeDB; Q2YQ23; -.
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 Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01755; flav_wrbA; 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
