NQOR_DEIRA
ID NQOR_DEIRA Reviewed; 200 AA.
AC Q9RYU4;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=NAD(P)H dehydrogenase (quinone);
DE EC=1.6.5.2 {ECO:0000250|UniProtKB:P0A8G6};
DE AltName: Full=Flavoprotein WrbA;
DE AltName: Full=NAD(P)H:quinone oxidoreductase;
DE Short=NQO;
GN OrderedLocusNames=DR_A0214;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2] {ECO:0007744|PDB:1YDG, ECO:0007744|PDB:1YRH}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-199 IN COMPLEX WITH FMN,
RP COFACTOR, AND SUBUNIT.
RX PubMed=16322580; DOI=10.1110/ps.051680805;
RA Gorman J., Shapiro L.;
RT "Crystal structures of the tryptophan repressor binding protein WrbA and
RT complexes with flavin mononucleotide.";
RL Protein Sci. 14:3004-3012(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:0000250|UniProtKB:P0A8G6};
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:0000250|UniProtKB:P0A8G6};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16322580};
CC Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:16322580};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16322580}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; AE001825; AAF12417.1; -; Genomic_DNA.
DR PIR; G75573; G75573.
DR RefSeq; NP_285537.1; NC_001264.1.
DR RefSeq; WP_010889473.1; NZ_CP015082.1.
DR PDB; 1YDG; X-ray; 2.00 A; A/B/C/D/E/F/G/H=2-199.
DR PDB; 1YRH; X-ray; 3.11 A; A/B/C/D/E/F/G/H=2-199.
DR PDBsum; 1YDG; -.
DR PDBsum; 1YRH; -.
DR AlphaFoldDB; Q9RYU4; -.
DR SMR; Q9RYU4; -.
DR STRING; 243230.DR_A0214; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR EnsemblBacteria; AAF12417; AAF12417; DR_A0214.
DR KEGG; dra:DR_A0214; -.
DR PATRIC; fig|243230.17.peg.3103; -.
DR eggNOG; COG0655; Bacteria.
DR HOGENOM; CLU_051402_0_2_0; -.
DR InParanoid; Q9RYU4; -.
DR OMA; KFADGNP; -.
DR OrthoDB; 796211at2; -.
DR EvolutionaryTrace; Q9RYU4; -.
DR Proteomes; UP000002524; Chromosome II.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR Gene3D; 3.40.50.360; -; 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 Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR TIGRFAMs; TIGR01755; flav_wrbA; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..200
FT /note="NAD(P)H dehydrogenase (quinone)"
FT /id="PRO_0000422321"
FT DOMAIN 7..199
FT /note="Flavodoxin-like"
FT BINDING 13..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT BINDING 86..88
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT BINDING 121..127
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT BINDING 142
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:1YDG"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:1YDG"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:1YDG"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:1YDG"
FT STRAND 78..87
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:1YDG"
FT TURN 108..113
FT /evidence="ECO:0007829|PDB:1YDG"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:1YDG"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1YDG"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1YDG"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1YDG"
FT HELIX 178..199
FT /evidence="ECO:0007829|PDB:1YDG"
SQ SEQUENCE 200 AA; 21298 MW; FD2FEA38E9775909 CRC64;
MTAPVKLAIV FYSSTGTGYA MAQEAAEAGR AAGAEVRLLK VRETAPQDVI DGQDAWKANI
EAMKDVPEAT PADLEWAEAI VFSSPTRFGG ATSQMRAFID TLGGLWSSGK LANKTFSAMT
SAQNVNGGQE TTLQTLYMTA MHWGAVLTPP GYTDEVIFKS GGNPYGASVT ANGQPLLEND
RASIRHQVRR QVELTAKLLG
