NQOR_SHISS
ID NQOR_SHISS Reviewed; 201 AA.
AC Q3Z3B7;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SSON_1014;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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; CP000038; AAZ87745.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z3B7; -.
DR SMR; Q3Z3B7; -.
DR CAZy; AA6; Auxiliary Activities 6.
DR PRIDE; Q3Z3B7; -.
DR EnsemblBacteria; AAZ87745; AAZ87745; SSON_1014.
DR KEGG; ssn:SSON_1014; -.
DR HOGENOM; CLU_051402_0_2_6; -.
DR OMA; KFADGNP; -.
DR Proteomes; UP000002529; Chromosome.
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 3: Inferred from homology;
KW Flavoprotein; FMN; NAD; NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..201
FT /note="NAD(P)H dehydrogenase (quinone)"
FT /id="PRO_0000291032"
FT DOMAIN 7..192
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 13..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 81..83
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 116..121
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 136
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
SQ SEQUENCE 201 AA; 21202 MW; C613D17C1BD2C9D7 CRC64;
MSVKARILVL YYSMYGHIET MARAVAEGAS KVDGAEVVVK RVPETMPPQL FEKAGGKTQT
APVATPQELA DYDAIIFGTP TRFGNMSGQM RTFLDQTGGL WASGALYGKL ASVFSSTGTG
GGQEQTITST WTTLAHHGMV IVPIGYAAQE LFDVSQVRGG TPYGATTIAG GDGSRQPSQE
ELSIARYQGE YVAGLAVKLN G