ID   NQOR_XANP2              Reviewed;         199 AA.
AC   A7IE31;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Xaut_1023;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000781; ABS66274.1; -; Genomic_DNA.
DR   RefSeq; WP_012113045.1; NC_009720.1.
DR   AlphaFoldDB; A7IE31; -.
DR   SMR; A7IE31; -.
DR   STRING; 78245.Xaut_1023; -.
DR   CAZy; AA6; Auxiliary Activities 6.
DR   EnsemblBacteria; ABS66274; ABS66274; Xaut_1023.
DR   KEGG; xau:Xaut_1023; -.
DR   eggNOG; COG0655; Bacteria.
DR   HOGENOM; CLU_051402_0_2_5; -.
DR   OMA; LHFGMVI; -.
DR   OrthoDB; 796211at2; -.
DR   PhylomeDB; A7IE31; -.
DR   Proteomes; UP000002417; 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..199
FT                   /note="NAD(P)H dehydrogenase (quinone)"
FT                   /id="PRO_1000200648"
FT   DOMAIN          4..190
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
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"
SQ   SEQUENCE   199 AA;  20824 MW;  75ABD94B1F00FFD5 CRC64;
     MAKVLVLYYS AYGHIEQMAE AAAAGAREAG ATVDIKRVPD LVPEEVAKSA HFKLDQKAPI
     ATVAELAEYD AIIVGVGTRF GRMASQMANF LDQAGGLWAR GALNGKVGGA FTSTATQHGG
     QEVTLFSIIT NLMHFGMVIV GLDYGYGAQM TLDEVTGGSP YGATTITGGD GSRQPSAIEL
     DGARYQGRKI AETAIKLHG