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Protein

Oxygen-insensitive NADPH nitroreductase

Gene

nfsA

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

Functioni

Catalyzes the reduction of nitroaromatic compounds using NADPH. Has a broad electron acceptor specificity. Reduces nitrofurazone by a ping-pong bi-bi mechanism possibly to generate a two-electron transfer product. Major oxygen-insensitive nitroreductase in E.coli.1 Publication

Catalytic activityi

An oxidized nitroaromatic compound + NADPH = a reduced nitroaromatic compound + NADP+.1 Publication

Cofactori

FMN2 PublicationsNote: Binds 1 FMN per monomer.1 Publication

Kineticsi

  1. KM=11 µM for NADPH1 Publication
  2. KM=5.5 µM for nitrofurazone1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391FMN; via amide nitrogenCombined sources1 Publication
    Binding sitei67 – 671FMNCombined sources1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 155FMNCombined sources1 Publication
    Nucleotide bindingi128 – 1314FMNCombined sources1 Publication
    Nucleotide bindingi167 – 1693FMNCombined sources1 Publication

    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, NADP

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxygen-insensitive NADPH nitroreductaseCurated (EC:1.-.-.-1 Publication)
    Alternative name(s):
    Modulator of drug activity A
    Gene namesi
    Name:nfsA
    Synonyms:mda18, mdaA1 Publication, 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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi203 – 2031R → A: Strong decrease in activity. 1 Publication
    Mutagenesisi208 – 2081R → A: No change in activity. 1 Publication

    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

    Subunit structurei

    Homodimer.1 Publication

    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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
      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) IN COMPLEX WITH FMN, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-203 AND ARG-208.

    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: June 8, 2016
    This is version 131 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.