NQOR_BURCJ
ID NQOR_BURCJ Reviewed; 200 AA.
AC B4EPK7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BceJ2315_63650; ORFNames=BCAS0090;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747722; CAR57023.1; -; Genomic_DNA.
DR RefSeq; WP_006490964.1; NC_011002.1.
DR AlphaFoldDB; B4EPK7; -.
DR SMR; B4EPK7; -.
DR STRING; 216591.BCAS0090; -.
DR EnsemblBacteria; CAR57023; CAR57023; BCAS0090.
DR GeneID; 56560471; -.
DR KEGG; bcj:BCAS0090; -.
DR eggNOG; COG0655; Bacteria.
DR HOGENOM; CLU_051402_0_2_4; -.
DR OMA; KFADGNP; -.
DR OrthoDB; 796211at2; -.
DR BioCyc; BCEN216591:G1G1V-7062-MON; -.
DR Proteomes; UP000001035; Chromosome 3.
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.
FT CHAIN 1..200
FT /note="NAD(P)H dehydrogenase (quinone)"
FT /id="PRO_1000200618"
FT DOMAIN 4..191
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 79..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 114..120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
FT BINDING 135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01017"
SQ SEQUENCE 200 AA; 21033 MW; CBF7CAEAF6EEFC55 CRC64;
MAKVLVLYYS SYGHVETMAQ HIVEGAKSVP GVEVTLKRVP ETIPVDQARA IGVKVDQAAP
VATVDELADY DAIIFGTPTR FGNMAGQMRT FLDQTGGLWM KGALVGKIGS VFASTGTQHG
GQETTITSFH TTLLHHGMVI VGVPYACSGL VNMNEITGGT PYGATTLAGA DGSRQPSANE
LDIARYQGKH VAELANKLAS
