ID D7H3J3_BRUAO Unreviewed; 199 AA.
AC D7H3J3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=BAYG_01320 {ECO:0000313|EMBL:EFH34886.1};
OS Brucella abortus bv. 5 str. B3196.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH34886.1, ECO:0000313|Proteomes:UP000005752};
RN [1] {ECO:0000313|EMBL:EFH34886.1, ECO:0000313|Proteomes:UP000005752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3196 {ECO:0000313|EMBL:EFH34886.1,
RC ECO:0000313|Proteomes:UP000005752};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Brucella abortus bv. 5 str. B3196.";
RL Submitted (FEB-2010) 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 -!- 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}.
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DR EMBL; GG774511; EFH34886.1; -; Genomic_DNA.
DR RefSeq; WP_002964168.1; NZ_GG774511.1.
DR AlphaFoldDB; D7H3J3; -.
DR SMR; D7H3J3; -.
DR DNASU; 3787724; -.
DR GeneID; 3787724; -.
DR HOGENOM; CLU_051402_0_2_5; -.
DR Proteomes; UP000005752; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01017};
KW FMN {ECO:0000256|HAMAP-Rule:MF_01017};
KW NAD {ECO:0000256|ARBA:ARBA00023027, 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..190
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
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:0000256|HAMAP-Rule:MF_01017"
FT BINDING 12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 78..80
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 134
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
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
//
