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P38489 (NFNB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxygen-insensitive NAD(P)H nitroreductase

EC=1.-.-.-
Alternative name(s):
Dihydropteridine reductase
EC=1.5.1.34
FMN-dependent nitroreductase
Gene names
Name:nfnB
Synonyms:dprA, nfsB, nfsI, ntr
Ordered Locus Names:b0578, JW0567
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species. Ref.13

Catalytic activity

A 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H.

Cofactor

FMN.

Enzyme regulation

Subject to competitive inhibition by dicoumarol, nicotinic acid and acetate with respect to NADH. Subject to uncompetitive inhibition by dicoumarol, nicotinic acid and acetate with respect to nitrofurazone and nitrofurantoin. Ref.13

Subunit structure

Homodimer. Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the nitroreductase family.

Biophysicochemical properties

Kinetic parameters:

KM=350 µM for NADH Ref.13

KM=1850 µM for nitrofurazone

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-909296,EBI-909296

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Oxygen-insensitive NAD(P)H nitroreductase
PRO_0000072711

Regions

Nucleotide binding10 – 145FMN
Nucleotide binding153 – 1586NAD or NADP By similarity
Nucleotide binding165 – 1662FMN
Nucleotide binding205 – 2073FMN

Sites

Binding site411NAD or NADP; via amide nitrogen
Binding site711FMN

Experimental info

Sequence conflict51S → C AA sequence Ref.9
Sequence conflict10 – 123RHS → CIV AA sequence Ref.9
Sequence conflict191S → M AA sequence Ref.9
Sequence conflict211Missing AA sequence Ref.7
Sequence conflict281E → D AA sequence Ref.7
Sequence conflict1801E → I AA sequence Ref.7

Secondary structure

.................................. 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38489 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: A516CEFC3D46AEAC

FASTA21723,905
        10         20         30         40         50         60 
MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV 

        70         80         90        100        110        120 
AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG 

       130        140        150        160        170        180 
RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE 

       190        200        210 
KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV 

« Hide

References

« Hide 'large scale' references
[1]"Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri."
Zenno S., Koike H., Tanokura M., Saigo K.
J. Biochem. 120:736-744(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
[2]"Physical characterisation of the Escherichia coli B gene encoding nitroreductase and its over-expression in Escherichia coli K12."
Michael N.P., Brehm J.K., Anlezark G.M., Minton N.P.
FEMS Microbiol. Lett. 124:195-202(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B.
[3]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954) -- I. Purification and properties of a nitroreductase enzyme from Escherichia coli -- a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT)."
Anlezark G.M., Melton R.G., Sherwood R.F., Coles B., Friedlos F., Knox R.J.
Biochem. Pharmacol. 44:2289-2295(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-31 AND 139-180, CHARACTERIZATION.
Strain: B.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[9]"Dihydropteridine reductase from Escherichia coli."
Vasudevan S.G., Shaw D.C., Armarego W.L.F.
Biochem. J. 255:581-588(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20, CHARACTERIZATION AS A DIHYDROPTERIDINE REDUCT.
[10]"Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme."
Parkinson G.N., Skelly J.V., Neidle S.
J. Med. Chem. 43:3624-3631(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT.
Strain: B.
[11]"The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution."
Lovering A.L., Hyde E.I., Searle P.F., White S.A.
J. Mol. Biol. 309:203-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NICOTININC ACID AND FMN, SUBUNIT.
Strain: K12 / DH5-alpha.
[12]"Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form."
Johansson E., Parkinson G.N., Denny W.A., Neidle S.
J. Med. Chem. 46:4009-4020(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH FMN; DICOUMAROL AND DINITROBENZAMIDE PRODRUGS, SUBUNIT.
[13]"Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme."
Race P.R., Lovering A.L., Green R.M., Ossor A., White S.A., Searle P.F., Wrighton C.J., Hyde E.I.
J. Biol. Chem. 280:13256-13264(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FMN; ACETATE AND THE ANTIBIOTIC NITROFURAZONE, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D25414 Genomic DNA. Translation: BAA05004.1.
U07860 Genomic DNA. Translation: AAC43263.1.
U82598 Genomic DNA. Translation: AAB40776.1.
U00096 Genomic DNA. Translation: AAC73679.1.
AP009048 Genomic DNA. Translation: BAA35218.1.
PIRI67685.
S01818.
RefSeqNP_415110.1. NC_000913.3.
YP_488865.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS7X-ray2.06A/B1-217[»]
1ICRX-ray1.70A/B1-217[»]
1ICUX-ray1.80A/B/C/D1-217[»]
1ICVX-ray2.40A/B/C/D1-217[»]
1IDTX-ray2.00A/B1-217[»]
1OO5X-ray2.50A/B1-217[»]
1OO6X-ray2.00A/B1-217[»]
1OONX-ray2.49A/B1-217[»]
1OOQX-ray2.00A/B1-217[»]
1YKIX-ray1.70A/B/C/D1-217[»]
1YLRX-ray1.70A/B1-217[»]
1YLUX-ray2.00A/B1-217[»]
ProteinModelPortalP38489.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10330N.
IntActP38489. 12 interactions.
STRING511145.b0578.

Chemistry

ChEMBLCHEMBL1075080.
DrugBankDB01093. Dimethyl sulfoxide.

2D gel databases

SWISS-2DPAGEP38489.

Proteomic databases

PaxDbP38489.
PRIDEP38489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73679; AAC73679; b0578.
BAA35218; BAA35218; BAA35218.
GeneID12933919.
945778.
KEGGecj:Y75_p0565.
eco:b0578.
PATRIC32116324. VBIEscCol129921_0602.

Organism-specific databases

EchoBASEEB4146.
EcoGeneEG20151. nfnB.

Phylogenomic databases

eggNOGCOG0778.
HOGENOMHOG000146740.
KOK10679.
OMAYRSEEDF.
OrthoDBEOG65QWJJ.
PhylomeDBP38489.

Enzyme and pathway databases

BioCycEcoCyc:DIHYDROPTERIREDUCT-MONOMER.
ECOL316407:JW0567-MONOMER.
MetaCyc:DIHYDROPTERIREDUCT-MONOMER.

Gene expression databases

GenevestigatorP38489.

Family and domain databases

Gene3D3.40.109.10. 1 hit.
InterProIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMSSF55469. SSF55469. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP38489.
PROP38489.

Entry information

Entry nameNFNB_ECOLI
AccessionPrimary (citable) accession number: P38489
Secondary accession number(s): P19575
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene