PNPB_PSEWB
ID PNPB_PSEWB Reviewed; 207 AA.
AC C1I202;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=p-benzoquinone reductase {ECO:0000303|PubMed:19218392};
DE EC=1.6.5.6 {ECO:0000269|PubMed:19218392};
DE AltName: Full=NAD(P)H dehydrogenase (quinone);
GN Name=pnpB;
OS Pseudomonas sp. (strain WBC-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=165468;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=19218392; DOI=10.1128/jb.01566-08;
RA Zhang J.J., Liu H., Xiao Y., Zhang X.E., Zhou N.Y.;
RT "Identification and characterization of catabolic para-nitrophenol 4-
RT monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain
RT WBC-3.";
RL J. Bacteriol. 191:2703-2710(2009).
RN [2] {ECO:0007744|PDB:4LA4}
RP X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).
RA Su J., Zhang C., Li N., Gu L.;
RT "Crystal structure of native PnpB.";
RL Submitted (JUN-2013) to the PDB data bank.
RN [3] {ECO:0007744|PDB:4LAF}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH FMN.
RA Su J., Zhang C., Li N., Gu L.;
RT "Crystal structure of PnpB complex with FMN.";
RL Submitted (JUN-2013) to the PDB data bank.
CC -!- FUNCTION: Involved in the degradation of para-nitrophenol (PNP).
CC Catalyzes the reduction of p-benzoquinone to hydroquinone.
CC {ECO:0000269|PubMed:19218392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,4-benzoquinone + H(+) + NADPH = hydroquinone + NADP(+);
CC Xref=Rhea:RHEA:23488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16509,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.5.6;
CC Evidence={ECO:0000269|PubMed:19218392};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:19218392};
CC Note=Binds 1 FMN per monomer. {ECO:0000269|PubMed:19218392};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 uM for p-benzoquinone {ECO:0000269|PubMed:19218392};
CC KM=181.6 uM for NADPH {ECO:0000269|PubMed:19218392};
CC -!- PATHWAY: Xenobiotic degradation; 4-nitrophenol degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19218392}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not completely unable
CC to grow on PNP. {ECO:0000269|PubMed:19218392}.
CC -!- SIMILARITY: Belongs to the WrbA family. {ECO:0000305}.
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DR EMBL; EF577044; ABU50909.1; -; Genomic_DNA.
DR PDB; 4LA4; X-ray; 2.07 A; A/B=1-207.
DR PDB; 4LAF; X-ray; 1.76 A; A/B/C/D=1-207.
DR PDBsum; 4LA4; -.
DR PDBsum; 4LAF; -.
DR AlphaFoldDB; C1I202; -.
DR SMR; C1I202; -.
DR CAZy; AA6; Auxiliary Activities 6.
DR KEGG; ag:ABU50909; -.
DR BioCyc; MetaCyc:MON-13026; -.
DR BRENDA; 1.6.5.6; 11433.
DR SABIO-RK; C1I202; -.
DR UniPathway; UPA01030; -.
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:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0018541; F:p-benzoquinone reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046196; P:4-nitrophenol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019439; P:aromatic compound catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; NADP; Oxidoreductase.
FT CHAIN 1..207
FT /note="p-benzoquinone reductase"
FT /id="PRO_0000422667"
FT DOMAIN 5..196
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000250"
FT BINDING 11..16
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P0A8G6"
FT BINDING 84..86
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 119..125
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 140
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.3"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4LAF"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:4LAF"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:4LAF"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:4LAF"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:4LAF"
FT TURN 106..111
FT /evidence="ECO:0007829|PDB:4LAF"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:4LAF"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4LAF"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:4LAF"
SQ SEQUENCE 207 AA; 22040 MW; B5A81571073C6A08 CRC64;
MPTKIQIVFY SSYGHIYKMA EAIAAGAREV GDVEVTLLQV PELMPEEVQV KSGIKGYRAA
FGSIPYATPE VLAEADAIIF GTPTRFGNMC SQMRNFLDQT GGLWMSGGLI GKVGSVFTST
ASQHGGQETT ITSFHTTLLH HGMVIVGVPY SEPGLTNMTE ISGGTPYGAS TLAGADGSRQ
PSENELQIAR FQGKHVATIA KRLANNK
