ID F7XDJ0_SINMM Unreviewed; 264 AA.
AC F7XDJ0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 Name=wrbA3 {ECO:0000313|EMBL:AEH81616.1};
GN OrderedLocusNames=SM11_pC0542 {ECO:0000313|EMBL:AEH81616.1};
OS Sinorhizobium meliloti (strain SM11).
OG Plasmid pSmeSM11c {ECO:0000313|EMBL:AEH81616.1,
OG ECO:0000313|Proteomes:UP000009045}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH81616.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH81616.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH81616.1,
RC ECO:0000313|Proteomes:UP000009045};
RC PLASMID=pSmeSM11c {ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
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; CP001831; AEH81616.1; -; Genomic_DNA.
DR AlphaFoldDB; F7XDJ0; -.
DR KEGG; smx:SM11_pC0542; -.
DR PATRIC; fig|707241.3.peg.4514; -.
DR HOGENOM; CLU_051402_0_2_5; -.
DR Proteomes; UP000009045; Plasmid pSmeSM11c.
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};
KW Plasmid {ECO:0000313|EMBL:AEH81616.1}.
FT DOMAIN 56..244
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62..67
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 130..132
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
FT BINDING 186
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01017"
SQ SEQUENCE 264 AA; 28490 MW; 030477F1CFF29A26 CRC64;
MIYSIDRLGR FFHNYPDHSP MSSIGWQKAT GADRHGGNLV RVRSPATRQD EEMTKMLVLY
YSSYGHIEAM AKAVASGAKQ AGATVALKRV PELVPEAVAR SSGYRLGQEA PIATVAELAD
YDAIVIGTPT RFGNMASQMK NFLDQTGGLW AENKLVGKVG SVFTSTGSQH GGQESTILST
HVVMLHLGMV IVGLPYSFKG QMRMDEITGG SPYGASTLAE DENHRDRSPS ANELDGARFQ
GRHVAEVAAA MALGRSHLQP ELVR
//
