ID   NQOR_METSB              Reviewed;         199 AA.
AC   B8EMJ5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Msil_3216;
OS   Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS   13906 / BL2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Beijerinckiaceae; Methylocella.
OX   NCBI_TaxID=395965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX   PubMed=20472789; DOI=10.1128/jb.00506-10;
RA   Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA   Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT   "Complete genome sequence of the aerobic facultative methanotroph
RT   Methylocella silvestris BL2.";
RL   J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK52123.1; -; Genomic_DNA.
DR   RefSeq; WP_012592192.1; NC_011666.1.
DR   AlphaFoldDB; B8EMJ5; -.
DR   SMR; B8EMJ5; -.
DR   STRING; 395965.Msil_3216; -.
DR   EnsemblBacteria; ACK52123; ACK52123; Msil_3216.
DR   KEGG; msl:Msil_3216; -.
DR   eggNOG; COG0655; Bacteria.
DR   HOGENOM; CLU_051402_0_2_5; -.
DR   OMA; LHFGMVI; -.
DR   OrthoDB; 796211at2; -.
DR   Proteomes; UP000002257; 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_1000149012"
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;  21000 MW;  10952C767A4915E4 CRC64;
     MAKVLVLYYS AYGHIEKMAE AVAEGAREAG AEVDIKRVPE LVPLEIAQKS HFKLDQAAPV
     ATIADLEHYD AIIVGTGTRF GRMSSQMANF LDQAGGLWMR GALNGKVGAA FTSTATQHGG
     QEVTLFSIIT NLLHFGLVIV GLDYGFAGQG RLDEITGGSP YGATTIAASD GSRQPSETEL
     AGARYQGRRV AEVAGKLKG