NQOR_ARCFU
ID NQOR_ARCFU Reviewed; 191 AA.
AC O29904;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=NAD(P)H dehydrogenase (quinone);
DE EC=1.6.5.2 {ECO:0000269|PubMed:16672604};
DE AltName: Full=Flavoprotein WrbA;
DE AltName: Full=NAD(P)H:quinone oxidoreductase;
DE Short=NQO;
GN OrderedLocusNames=AF_0343;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-6, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=16672604; DOI=10.1128/jb.188.10.3498-3506.2006;
RA Patridge E.V., Ferry J.G.;
RT "WrbA from Escherichia coli and Archaeoglobus fulgidus is an
RT NAD(P)H:quinone oxidoreductase.";
RL J. Bacteriol. 188:3498-3506(2006).
CC -!- FUNCTION: It seems to function in response to environmental stress when
CC various electron transfer chains are affected or when the environment
CC is highly oxidizing. It reduces quinones to the hydroquinone state to
CC prevent interaction of the semiquinone with O2 and production of
CC superoxide. It prefers NADH over NADPH. {ECO:0000269|PubMed:16672604}.
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:0000269|PubMed:16672604};
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:0000269|PubMed:16672604};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16672604};
CC Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:16672604};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19 uM for NADH {ECO:0000269|PubMed:16672604};
CC KM=37 uM for benzoquinone {ECO:0000269|PubMed:16672604};
CC -!- SUBUNIT: Homodimer and homotetramer; in equilibrium.
CC {ECO:0000269|PubMed:16672604}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; AE000782; AAB90893.1; -; Genomic_DNA.
DR PIR; G69292; G69292.
DR RefSeq; WP_010877850.1; NC_000917.1.
DR AlphaFoldDB; O29904; -.
DR SMR; O29904; -.
DR STRING; 224325.AF_0343; -.
DR DNASU; 1483557; -.
DR EnsemblBacteria; AAB90893; AAB90893; AF_0343.
DR GeneID; 24793882; -.
DR KEGG; afu:AF_0343; -.
DR eggNOG; arCOG00510; Archaea.
DR HOGENOM; CLU_051402_0_2_2; -.
DR OMA; KFADGNP; -.
DR OrthoDB; 66986at2157; -.
DR PhylomeDB; O29904; -.
DR BRENDA; 1.6.5.2; 414.
DR SABIO-RK; O29904; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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; IPR001226; Flavodoxin_CS.
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; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Flavoprotein; FMN; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16672604"
FT CHAIN 2..191
FT /note="NAD(P)H dehydrogenase (quinone)"
FT /id="PRO_0000422323"
FT DOMAIN 4..184
FT /note="Flavodoxin-like"
FT BINDING 10..15
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9RYU4"
FT BINDING 83..85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9RYU4"
FT BINDING 118..124
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9RYU4"
SQ SEQUENCE 191 AA; 20913 MW; 987796F4C9DAEA13 CRC64;
MARILVIFHS ITGNTMKLAK AVADGAREGG AEVAVKRVPE TIPAEILEKN PGYVKVREEL
ESFEVARPEE LQDYDAIIFG SPTRFGVMSS QMKQFIDMTG RLWMERRLEG KVGAVFTSNE
MPHGGKEATL LSMLLPLFAH GMIIVGLPPA KELYRAGSYY GAASTGVPKE DDLQVAKMLG
KRVAEVAEKL C
