NQOR_PSEAE
ID NQOR_PSEAE Reviewed; 198 AA.
AC Q9I509;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=PA0949;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0007744|PDB:1ZWK, ECO:0007744|PDB:1ZWL}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-196 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).
RN [3] {ECO:0007744|PDB:2A5L}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND SUBUNIT.
RA Lunin V.V., Evdokimova E., Kudritska M., Osipiuk J., Joachimiak A.,
RA Edwards A.M., Savchenko A.;
RT "The crystal structure of the Trp repressor binding protein WrbA from
RT Pseudomonas aeruginosa.";
RL Submitted (JUN-2005) to the PDB data bank.
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: Homodimer. {ECO:0000269|PubMed:16322580, ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04338.1; -; Genomic_DNA.
DR PIR; D83526; D83526.
DR RefSeq; NP_249640.1; NC_002516.2.
DR RefSeq; WP_003115189.1; NZ_QZGE01000007.1.
DR PDB; 1ZWK; X-ray; 2.60 A; A/B=2-196.
DR PDB; 1ZWL; X-ray; 2.80 A; A=2-196.
DR PDB; 2A5L; X-ray; 1.70 A; A/B=1-198.
DR PDBsum; 1ZWK; -.
DR PDBsum; 1ZWL; -.
DR PDBsum; 2A5L; -.
DR AlphaFoldDB; Q9I509; -.
DR SMR; Q9I509; -.
DR STRING; 287.DR97_989; -.
DR PaxDb; Q9I509; -.
DR PRIDE; Q9I509; -.
DR DNASU; 882021; -.
DR EnsemblBacteria; AAG04338; AAG04338; PA0949.
DR GeneID; 882021; -.
DR KEGG; pae:PA0949; -.
DR PATRIC; fig|208964.12.peg.986; -.
DR PseudoCAP; PA0949; -.
DR HOGENOM; CLU_051402_0_2_6; -.
DR InParanoid; Q9I509; -.
DR OMA; HGMLIMG; -.
DR PhylomeDB; Q9I509; -.
DR BioCyc; PAER208964:G1FZ6-969-MON; -.
DR EvolutionaryTrace; Q9I509; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IMP:PseudoCAP.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:PseudoCAP.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PseudoCAP.
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 3D-structure; Flavoprotein; FMN; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..198
FT /note="NAD(P)H dehydrogenase (quinone)"
FT /id="PRO_0000422322"
FT DOMAIN 6..190
FT /note="Flavodoxin-like"
FT BINDING 12..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT BINDING 79..81
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT BINDING 114..120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT BINDING 135
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16322580"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2A5L"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:2A5L"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:2A5L"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2A5L"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:2A5L"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:2A5L"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:2A5L"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:2A5L"
FT TURN 102..106
FT /evidence="ECO:0007829|PDB:2A5L"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:2A5L"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:2A5L"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1ZWK"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1ZWL"
FT HELIX 176..197
FT /evidence="ECO:0007829|PDB:2A5L"
SQ SEQUENCE 198 AA; 20763 MW; DA5551A18259FD70 CRC64;
MSSPYILVLY YSRHGATAEM ARQIARGVEQ GGFEARVRTV PAVSTECEAV APDIPAEGAL
YATLEDLKNC AGLALGSPTR FGNMASPLKY FLDGTSSLWL TGSLVGKPAA VFTSTASLHG
GQETTQLSML LPLLHHGMLV LGIPYSEPAL LETRGGGTPY GASHFAGADG KRSLDEHELT
LCRALGKRLA ETAGKLGS
