PNPA_PSEWB
ID PNPA_PSEWB Reviewed; 403 AA.
AC C1I201;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Para-nitrophenol 4-monooxygenase;
DE EC=1.14.13.167;
GN Name=pnpA;
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, 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).
CC -!- FUNCTION: Involved in the degradation of para-nitrophenol (4-NP).
CC Catalyzes oxidation of 4-nitrophenol (4-NP) at position 4 with
CC concomitant removal of the nitro group as nitrite and production of
CC para-benzoquinone. {ECO:0000269|PubMed:19218392}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-nitrophenol + H(+) + NADPH + O2 = 1,4-benzoquinone + H2O +
CC NADP(+) + nitrite; Xref=Rhea:RHEA:34327, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:16509, ChEBI:CHEBI:57783, ChEBI:CHEBI:57917,
CC ChEBI:CHEBI:58349; EC=1.14.13.167;
CC Evidence={ECO:0000269|PubMed:19218392};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for 4-NP {ECO:0000269|PubMed:19218392};
CC KM=137.4 uM for NADP {ECO:0000269|PubMed:19218392};
CC -!- PATHWAY: Xenobiotic degradation; 4-nitrophenol degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19218392}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to grow on
CC 4-NP. {ECO:0000269|PubMed:19218392}.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; EF577044; ABU50908.1; -; Genomic_DNA.
DR AlphaFoldDB; C1I201; -.
DR SMR; C1I201; -.
DR KEGG; ag:ABU50908; -.
DR BioCyc; MetaCyc:MON-13030; -.
DR BRENDA; 1.14.13.166; 5085.
DR BRENDA; 1.14.13.167; 5085.
DR SABIO-RK; C1I201; -.
DR UniPathway; UPA01030; -.
DR GO; GO:0018632; F:4-nitrophenol 4-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
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; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase; NADP;
KW Oxidoreductase.
FT CHAIN 1..403
FT /note="Para-nitrophenol 4-monooxygenase"
FT /id="PRO_0000422666"
FT BINDING 6..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 279..289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 44867 MW; 45F863B5167FC990 CRC64;
METLDGVVVV GGGPVGLLTA LKLGKAGIKV VVLEAEPGVS PSPRAVAYMP PTAAALDRFG
LLQDIRKRAV MCPDFAYRHG NGELIAKMDW SVLSQDTQYP YMLLLGQNHV SNVIFQHLRE
LPNVEIRWNH RVEEVDQDDA YVTIETSSPG GTSRLRARWL AATDGARSTV RQKIGLTFDG
ITWDERLVAT NVFYDFSLHG YSRANFVHDP VDWAVVVQLD KTGLWRVCYG EDASLSDAEV
RRRLPERFKR LLPGAPTPDQ YRVDHLNPYR VHQRCAAEFR RGRVVLAGDA AHATNPMGGL
GLSGGVLDAE HLAEALIAVI KNGASTKTLD EYSIDRRKVF LEFTSPTATA NFTWMKESDP
AQRIRDDAMF KEAGTDRAVM RQFLLDLEKL NGRRVIEKKL KAA