NBZA_PSEOL
ID NBZA_PSEOL Reviewed; 227 AA.
AC Q6DLR9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Nitrobenzene nitroreductase {ECO:0000303|PubMed:7601851};
DE EC=1.7.1.16 {ECO:0000269|PubMed:7601851, ECO:0000269|PubMed:8368838};
DE AltName: Full=Oxygen-insensitive nitroreductase {ECO:0000303|PubMed:7601851};
DE AltName: Full=Type I nitroreductase {ECO:0000303|PubMed:7601851};
GN Name=nbzA {ECO:0000312|EMBL:AAT71308.1};
OS Pseudomonas oleovorans.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JS45;
RA Chae J.-C., Zylstra G.J.;
RT "Cloning and sequencing the Pseudomonas pseudoalcaligenes JS45 gene for
RT nitrobenzene nitroreductase.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-31, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=JS45;
RX PubMed=7601851; DOI=10.1128/jb.177.13.3837-3842.1995;
RA Somerville C.C., Nishino S.F., Spain J.C.;
RT "Purification and characterization of nitrobenzene nitroreductase from
RT Pseudomonas pseudoalcaligenes JS45.";
RL J. Bacteriol. 177:3837-3842(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, SUBSTRATE SPECIFICITY, AND
RP PATHWAY.
RC STRAIN=JS45;
RX PubMed=8368838; DOI=10.1128/aem.59.8.2520-2525.1993;
RA Nishino S.F., Spain J.C.;
RT "Degradation of nitrobenzene by a Pseudomonas pseudoalcaligenes.";
RL Appl. Environ. Microbiol. 59:2520-2525(1993).
CC -!- FUNCTION: Involved in the biodegradation of nitroaromatic compounds
CC (PubMed:8368838). Catalyzes the two-electron reduction of nitrobenzene
CC (NB) to produce a nitrosobenzene (NOB) intermediate, which is
CC immediately reduced to hydroxylaminobenzene (HAB) by a second two-
CC electron transfer (PubMed:7601851). Also active on menadione and
CC nitrofurazone (PubMed:7601851). Replacing NADPH with NADH results in a
CC 4-fold decrease in the reaction rate (PubMed:8368838).
CC {ECO:0000269|PubMed:7601851, ECO:0000269|PubMed:8368838}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-phenylhydroxylamine + 2 NADP(+) = 2 H(+) + 2 NADPH +
CC nitrobenzene; Xref=Rhea:RHEA:52884, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27798, ChEBI:CHEBI:28902,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.7.1.16;
CC Evidence={ECO:0000269|PubMed:7601851, ECO:0000269|PubMed:8368838};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:7601851};
CC Note=Binds 2 FMN per subunit. {ECO:0000269|PubMed:7601851};
CC -!- ACTIVITY REGULATION: Inhibited by dicumarol, p-hydroxymercuribenzoate
CC and salicyl hydroxamate. {ECO:0000269|PubMed:7601851}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for nitrobenzene {ECO:0000269|PubMed:7601851};
CC KM=9 uM for menadione {ECO:0000269|PubMed:7601851};
CC KM=64 uM for nitrofurazone {ECO:0000269|PubMed:7601851};
CC KM=183 uM for NADPH {ECO:0000269|PubMed:7601851};
CC KM=862 uM for 5-(aziridin-1-YL)-2,4-dinitrobenzamide
CC {ECO:0000269|PubMed:7601851};
CC Vmax=144 umol/min/mg enzyme with NADPH as substrate
CC {ECO:0000269|PubMed:7601851};
CC Vmax=92 umol/min/mg enzyme with nitrobenzene as substrate
CC {ECO:0000269|PubMed:7601851};
CC Vmax=12 umol/min/mg enzyme with menadione as substrate
CC {ECO:0000269|PubMed:7601851};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:7601851};
CC Temperature dependence:
CC Stable at 40 degrees Celsius and below, but it loses activity rapidly
CC at temperatures above 45 degrees Celsius.
CC {ECO:0000269|PubMed:7601851};
CC -!- PATHWAY: Xenobiotic degradation; nitrobenzene degradation.
CC {ECO:0000305|PubMed:8368838}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:7601851}.
CC -!- INDUCTION: By nitrobenzene. {ECO:0000269|PubMed:8368838}.
CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
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DR EMBL; AY664495; AAT71308.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6DLR9; -.
DR SMR; Q6DLR9; -.
DR BRENDA; 1.7.1.16; 5150.
DR UniPathway; UPA00923; -.
DR GO; GO:0018546; F:nitrobenzene nitroreductase activity; IEA:RHEA.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; Flavoprotein;
KW FMN; NADP; Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7601851"
FT CHAIN 2..227
FT /note="Nitrobenzene nitroreductase"
FT /id="PRO_0000441894"
FT BINDING 14..18
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0R6D0"
FT BINDING 44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0R6D0"
FT BINDING 109
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0R6D0"
FT BINDING 172..173
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0R6D0"
FT BINDING 215
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:A0R6D0"
SQ SEQUENCE 227 AA; 25980 MW; B0285016798346F7 CRC64;
MPTSPFIDDL IRDRRAKRGF LDQPVSIEMV KDILSAAKYA PSSSNTQPWR CYVITGEARE
RITTAAVEAY RAAPEGLPPE YPFFPQPLHE PYATRFNSFR GQLGDALGIP RSDITLRRRD
VERQFRFFDA PVGLIFTMDR RLEWASFICY GCFLQNIMLA AKGRGLDTCT QVFWSMQHPV
LRTELNLPDD QMVVAGMSLG WADNSLPENQ MSISKMELEE FTTFVHE
