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Protein

Oxygen-insensitive NADPH nitroreductase

Gene

nfsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Reduction of nitroaromatic compounds using NADH. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major component of the oxygen-insensitive nitroreductase activity in E.coli.

Cofactori

GO - Molecular functioni

  • chromate reductase activity Source: EcoCyc
  • FMN binding Source: EcoCyc
  • oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN, NAD

Enzyme and pathway databases

BioCyciEcoCyc:EG11261-MONOMER.
ECOL316407:JW0835-MONOMER.
MetaCyc:EG11261-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxygen-insensitive NADPH nitroreductase (EC:1.-.-.-)
Alternative name(s):
Modulator of drug activity A
Gene namesi
Name:nfsA
Synonyms:mda18, mdaA, ybjB
Ordered Locus Names:b0851, JW0835
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11261. nfsA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Chemistry

DrugBankiDB00698. Nitrofurantoin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Oxygen-insensitive NADPH nitroreductasePRO_0000205510Add
BLAST

Proteomic databases

EPDiP17117.
PaxDbiP17117.
PRIDEiP17117.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
holAP286303EBI-1120624,EBI-549153

Protein-protein interaction databases

BioGridi4259991. 10 interactions.
DIPiDIP-10334N.
IntActiP17117. 5 interactions.
STRINGi511145.b0851.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97Combined sources
Helixi24 – 3512Combined sources
Helixi40 – 423Combined sources
Beta strandi46 – 505Combined sources
Helixi54 – 6310Combined sources
Helixi69 – 724Combined sources
Beta strandi73 – 8210Combined sources
Helixi84 – 896Combined sources
Helixi98 – 12124Combined sources
Beta strandi125 – 1295Combined sources
Helixi130 – 1356Combined sources
Helixi136 – 1427Combined sources
Beta strandi149 – 15810Combined sources
Helixi172 – 1754Combined sources
Beta strandi176 – 1805Combined sources
Helixi186 – 20116Combined sources
Helixi212 – 2209Combined sources
Helixi228 – 2347Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F5VX-ray1.70A/B1-240[»]
ProteinModelPortaliP17117.
SMRiP17117. Positions 1-240.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17117.

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin oxidoreductase frp family.Curated

Phylogenomic databases

eggNOGiENOG4108DBC. Bacteria.
COG0778. LUCA.
HOGENOMiHOG000272869.
InParanoidiP17117.
KOiK10678.
OMAiAYYKERS.
OrthoDBiEOG6GBMFH.
PhylomeDBiP17117.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR016446. Flavin_OxRdtase_Frp.
IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
PIRSFiPIRSF005426. Frp. 1 hit.
SUPFAMiSSF55469. SSF55469. 1 hit.

Sequencei

Sequence statusi: Complete.

P17117-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPTIELICG HRSIRHFTDE PISEAQREAI INSARATSSS SFLQCSSIIR
60 70 80 90 100
ITDKALREEL VTLTGGQKHV AQAAEFWVFC ADFNRHLQIC PDAQLGLAEQ
110 120 130 140 150
LLLGVVDTAM MAQNALIAAE SLGLGGVYIG GLRNNIEAVT KLLKLPQHVL
160 170 180 190 200
PLFGLCLGWP ADNPDLKPRL PASILVHENS YQPLDKGALA QYDEQLAEYY
210 220 230 240
LTRGSNNRRD TWSDHIRRTI IKESRPFILD YLHKQGWATR
Length:240
Mass (Da):26,801
Last modified:February 1, 1995 - v2
Checksum:i3B389FCDB86DED1D
GO

Sequence cautioni

The sequence CAA33867.1 differs from that shown. Reason: Frameshift at positions 155, 161 and 187. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18655 Genomic DNA. Translation: AAC43450.1.
D38308 Genomic DNA. Translation: BAA07425.1.
U00096 Genomic DNA. Translation: AAC73938.1.
AP009048 Genomic DNA. Translation: BAA35562.1.
X15859 Genomic DNA. Translation: CAA33867.1. Frameshift.
PIRiI80318.
RefSeqiNP_415372.1. NC_000913.3.
WP_000189159.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73938; AAC73938; b0851.
BAA35562; BAA35562; BAA35562.
GeneIDi945483.
KEGGiecj:JW0835.
eco:b0851.
PATRICi32116907. VBIEscCol129921_0879.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18655 Genomic DNA. Translation: AAC43450.1.
D38308 Genomic DNA. Translation: BAA07425.1.
U00096 Genomic DNA. Translation: AAC73938.1.
AP009048 Genomic DNA. Translation: BAA35562.1.
X15859 Genomic DNA. Translation: CAA33867.1. Frameshift.
PIRiI80318.
RefSeqiNP_415372.1. NC_000913.3.
WP_000189159.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F5VX-ray1.70A/B1-240[»]
ProteinModelPortaliP17117.
SMRiP17117. Positions 1-240.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259991. 10 interactions.
DIPiDIP-10334N.
IntActiP17117. 5 interactions.
STRINGi511145.b0851.

Chemistry

DrugBankiDB00698. Nitrofurantoin.

Proteomic databases

EPDiP17117.
PaxDbiP17117.
PRIDEiP17117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73938; AAC73938; b0851.
BAA35562; BAA35562; BAA35562.
GeneIDi945483.
KEGGiecj:JW0835.
eco:b0851.
PATRICi32116907. VBIEscCol129921_0879.

Organism-specific databases

EchoBASEiEB1241.
EcoGeneiEG11261. nfsA.

Phylogenomic databases

eggNOGiENOG4108DBC. Bacteria.
COG0778. LUCA.
HOGENOMiHOG000272869.
InParanoidiP17117.
KOiK10678.
OMAiAYYKERS.
OrthoDBiEOG6GBMFH.
PhylomeDBiP17117.

Enzyme and pathway databases

BioCyciEcoCyc:EG11261-MONOMER.
ECOL316407:JW0835-MONOMER.
MetaCyc:EG11261-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP17117.
PROiP17117.

Family and domain databases

Gene3Di3.40.109.10. 1 hit.
InterProiIPR016446. Flavin_OxRdtase_Frp.
IPR029479. Nitroreductase.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamiPF00881. Nitroreductase. 1 hit.
[Graphical view]
PIRSFiPIRSF005426. Frp. 1 hit.
SUPFAMiSSF55469. SSF55469. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A general genetic approach in Escherichia coli for determining the mechanism(s) of action of tumoricidal agents: application to DMP 840, a tumoricidal agent."
    Chatterjee P.K., Sternberg N.L.
    Proc. Natl. Acad. Sci. U.S.A. 92:8950-8954(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase."
    Zenno S., Koike H., Kumar A.N., Jayaraman R., Tanokura M., Saigo K.
    J. Bacteriol. 178:4508-4514(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / AB1157.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12."
    Kang W.-K., Icho T., Isono S., Kitakawa M., Isono K.
    Mol. Gen. Genet. 217:281-288(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-240.
    Strain: K12.
  7. "Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution."
    Zenno S., Kobori T., Tanokura M., Saigo K.
    J. Bacteriol. 180:422-425(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  8. "Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution."
    Kobori T., Sasaki H., Lee W.C., Zenno S., Saigo K., Murphy M.E., Tanokura M.
    J. Biol. Chem. 276:2816-2823(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiNFSA_ECOLI
AccessioniPrimary (citable) accession number: P17117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1995
Last modified: March 16, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.