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P38489

- NFNB_ECOLI

UniProt

P38489 - NFNB_ECOLI

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Protein

Oxygen-insensitive NAD(P)H nitroreductase

Gene

nfnB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

FMN.

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=350 µM for NADH1 Publication
  2. KM=1850 µM for nitrofurazone1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411NAD or NADP; via amide nitrogen
Binding sitei71 – 711FMN3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 145FMN3 Publications
Nucleotide bindingi153 – 1586NAD or NADPBy similarity
Nucleotide bindingi165 – 1662FMN3 Publications
Nucleotide bindingi205 – 2073FMN3 Publications

GO - Molecular functioni

  1. 6,7-dihydropteridine reductase activity Source: EcoCyc
  2. FAD binding Source: EcoCyc
  3. FMN binding Source: EcoCyc
  4. identical protein binding Source: IntAct
  5. NAD(P)H nitroreductase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NAD, NADP

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Oxygen-insensitive NAD(P)H nitroreductase (EC:1.-.-.-)
Alternative name(s):
Dihydropteridine reductase (EC:1.5.1.34)
FMN-dependent nitroreductase
Gene namesi
Name:nfnB
Synonyms:dprA, nfsB, nfsI, ntr
Ordered Locus Names:b0578, JW0567
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG20151. nfnB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Oxygen-insensitive NAD(P)H nitroreductasePRO_0000072711Add
BLAST

Proteomic databases

PaxDbiP38489.
PRIDEiP38489.

2D gel databases

SWISS-2DPAGEP38489.

Expressioni

Gene expression databases

GenevestigatoriP38489.

Interactioni

Subunit structurei

Homodimer.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-909296,EBI-909296

Protein-protein interaction databases

DIPiDIP-10330N.
IntActiP38489. 12 interactions.
STRINGi511145.b0578.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97
Beta strandi14 – 163
Helixi24 – 3613
Helixi40 – 423
Beta strandi46 – 516
Helixi54 – 618
Helixi62 – 643
Helixi66 – 716
Helixi72 – 776
Beta strandi78 – 8912
Helixi92 – 10413
Helixi111 – 13020
Helixi135 – 15622
Helixi169 – 1768
Helixi178 – 1814
Beta strandi183 – 19210
Helixi199 – 2013
Helixi210 – 2134
Beta strandi214 – 2174

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP38489.
SMRiP38489. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38489.

Family & Domainsi

Sequence similaritiesi

Belongs to the nitroreductase family.Curated

Phylogenomic databases

eggNOGiCOG0778.
HOGENOMiHOG000146740.
InParanoidiP38489.
KOiK10679.
OMAiYRSEEDF.
OrthoDBiEOG65QWJJ.
PhylomeDBiP38489.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

P38489-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV
60 70 80 90 100
ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD
110 120 130 140 150
QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF
160 170 180 190 200
LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN
210
ATLPKSRLPQ NITLTEV
Length:217
Mass (Da):23,905
Last modified:October 1, 1994 - v1
Checksum:iA516CEFC3D46AEAC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → C AA sequence (PubMed:3060113)Curated
Sequence conflicti10 – 123RHS → CIV AA sequence (PubMed:3060113)Curated
Sequence conflicti19 – 191S → M AA sequence (PubMed:3060113)Curated
Sequence conflicti21 – 211Missing AA sequence (PubMed:1472094)Curated
Sequence conflicti28 – 281E → D AA sequence (PubMed:1472094)Curated
Sequence conflicti180 – 1801E → I AA sequence (PubMed:1472094)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiI67685.
S01818.
RefSeqiNP_415110.1. NC_000913.3.
YP_488865.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73679; AAC73679; b0578.
BAA35218; BAA35218; BAA35218.
GeneIDi12933919.
945778.
KEGGiecj:Y75_p0565.
eco:b0578.
PATRICi32116324. VBIEscCol129921_0602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi I67685.
S01818.
RefSeqi NP_415110.1. NC_000913.3.
YP_488865.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DS7 X-ray 2.06 A/B 1-217 [» ]
1ICR X-ray 1.70 A/B 1-217 [» ]
1ICU X-ray 1.80 A/B/C/D 1-217 [» ]
1ICV X-ray 2.40 A/B/C/D 1-217 [» ]
1IDT X-ray 2.00 A/B 1-217 [» ]
1OO5 X-ray 2.50 A/B 1-217 [» ]
1OO6 X-ray 2.00 A/B 1-217 [» ]
1OON X-ray 2.49 A/B 1-217 [» ]
1OOQ X-ray 2.00 A/B 1-217 [» ]
1YKI X-ray 1.70 A/B/C/D 1-217 [» ]
1YLR X-ray 1.70 A/B 1-217 [» ]
1YLU X-ray 2.00 A/B 1-217 [» ]
ProteinModelPortali P38489.
SMRi P38489. Positions 1-217.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10330N.
IntActi P38489. 12 interactions.
STRINGi 511145.b0578.

Chemistry

ChEMBLi CHEMBL1075080.

2D gel databases

SWISS-2DPAGE P38489.

Proteomic databases

PaxDbi P38489.
PRIDEi P38489.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73679 ; AAC73679 ; b0578 .
BAA35218 ; BAA35218 ; BAA35218 .
GeneIDi 12933919.
945778.
KEGGi ecj:Y75_p0565.
eco:b0578.
PATRICi 32116324. VBIEscCol129921_0602.

Organism-specific databases

EchoBASEi EB4146.
EcoGenei EG20151. nfnB.

Phylogenomic databases

eggNOGi COG0778.
HOGENOMi HOG000146740.
InParanoidi P38489.
KOi K10679.
OMAi YRSEEDF.
OrthoDBi EOG65QWJJ.
PhylomeDBi P38489.

Enzyme and pathway databases

BioCyci EcoCyc:DIHYDROPTERIREDUCT-MONOMER.
ECOL316407:JW0567-MONOMER.
MetaCyc:DIHYDROPTERIREDUCT-MONOMER.

Miscellaneous databases

EvolutionaryTracei P38489.
PROi P38489.

Gene expression databases

Genevestigatori P38489.

Family and domain databases

Gene3Di 3.40.109.10. 1 hit.
InterProi IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view ]
Pfami PF00881. Nitroreductase. 1 hit.
[Graphical view ]
SUPFAMi SSF55469. SSF55469. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiNFNB_ECOLI
AccessioniPrimary (citable) accession number: P38489
Secondary accession number(s): P19575
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 29, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3