ID   NQOR_GEOUR              Reviewed;         203 AA.
AC   A5G4G8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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=Gura_2508;
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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: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; CP000698; ABQ26686.1; -; Genomic_DNA.
DR   RefSeq; WP_011939373.1; NC_009483.1.
DR   AlphaFoldDB; A5G4G8; -.
DR   SMR; A5G4G8; -.
DR   STRING; 351605.Gura_2508; -.
DR   EnsemblBacteria; ABQ26686; ABQ26686; Gura_2508.
DR   KEGG; gur:Gura_2508; -.
DR   HOGENOM; CLU_051402_0_2_7; -.
DR   OMA; KFADGNP; -.
DR   OrthoDB; 796211at2; -.
DR   Proteomes; UP000006695; 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;
KW   Reference proteome.
FT   CHAIN           1..203
FT                   /note="NAD(P)H dehydrogenase (quinone)"
FT                   /id="PRO_1000084140"
FT   DOMAIN          3..194
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT   BINDING         9..14
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT   BINDING         11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT   BINDING         82..84
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT   BINDING         117..123
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT   BINDING         138
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
SQ   SEQUENCE   203 AA;  21655 MW;  4A1B727A66CBD883 CRC64;
     MKVLIAYYSM YGHIHRMAEA VAEGAREVAG AEVLIRRVPE TLPADVLEKM GAVETQKKMA
     QIPVCTIGEL ADADAIIFGT PTRFGNMCGQ MRQFLDATGG LWMKGSLVGK LGSVFTSSAT
     QHGGQESTIL SFHITLLHQG MVVVGLPYAF QGQMRNDEII GGSPYGASTI AGTQGERSPS
     ENDLAAARYQ GKHVASIAAR LAR