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Protein

Oxygen-insensitive NAD(P)H nitroreductase

Gene

nfsB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

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)DescriptionActionsGraphical viewLength
    Binding sitei41NAD or NADP; via amide nitrogen1
    Binding sitei71FMN3 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi10 – 14FMN3 Publications5
    Nucleotide bindingi153 – 158NAD or NADPBy similarity6
    Nucleotide bindingi165 – 166FMN3 Publications2
    Nucleotide bindingi205 – 207FMN3 Publications3

    GO - Molecular functioni

    • 6,7-dihydropteridine reductase activity Source: EcoCyc
    • FMN binding Source: EcoCyc
    • identical protein binding Source: IntAct
    • NAD(P)H nitroreductase activity Source: EcoCyc

    GO - Biological processi

    • 2,4,6-trinitrotoluene catabolic process Source: EcoCyc

    Keywordsi

    Molecular functionOxidoreductase
    LigandFlavoprotein, FMN, NAD, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:DIHYDROPTERIREDUCT-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:nfsB1 Publication
    Synonyms:dprA, nfnB1 Publication, nfsI, ntr
    Ordered Locus Names:b0578, JW0567
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG20151 nfsB

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    • membrane Source: UniProtKB

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL1075080
    DrugBankiDB04253 CB1954
    DB04272 Citric Acid
    DB03247 Riboflavin Monophosphate

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000727111 – 217Oxygen-insensitive NAD(P)H nitroreductaseAdd BLAST217

    Proteomic databases

    EPDiP38489
    PaxDbiP38489
    PRIDEiP38489

    2D gel databases

    SWISS-2DPAGEiP38489

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Binary interactionsi

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

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi426291320 interactors.
    DIPiDIP-10330N
    IntActiP38489 12 interactors.
    STRINGi316385.ECDH10B_0644

    Structurei

    Secondary structure

    1217
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 9Combined sources7
    Beta strandi14 – 16Combined sources3
    Helixi24 – 36Combined sources13
    Helixi40 – 42Combined sources3
    Beta strandi46 – 51Combined sources6
    Helixi54 – 61Combined sources8
    Helixi62 – 64Combined sources3
    Helixi66 – 71Combined sources6
    Helixi72 – 77Combined sources6
    Beta strandi78 – 89Combined sources12
    Helixi92 – 104Combined sources13
    Helixi111 – 130Combined sources20
    Helixi135 – 156Combined sources22
    Helixi169 – 176Combined sources8
    Helixi178 – 181Combined sources4
    Beta strandi183 – 192Combined sources10
    Helixi199 – 201Combined sources3
    Helixi210 – 213Combined sources4
    Beta strandi214 – 217Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    3X21X-ray3.00A/B/C/D/E/F/G/H/I/J1-217[»]
    3X22X-ray2.00A/B1-217[»]
    ProteinModelPortaliP38489
    SMRiP38489
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38489

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nitroreductase family.Curated

    Phylogenomic databases

    eggNOGiENOG4108RCM Bacteria
    COG0778 LUCA
    HOGENOMiHOG000146740
    InParanoidiP38489
    KOiK10679
    OMAiATKEFDP
    PhylomeDBiP38489

    Family and domain databases

    CDDicd02149 NfsB_like_nitroreductase, 1 hit
    Gene3Di3.40.109.101 hit
    InterProiView protein in InterPro
    IPR033878 NfsB-like
    IPR029479 Nitroreductase
    IPR000415 Nitroreductase-like
    PfamiView protein in Pfam
    PF00881 Nitroreductase, 1 hit
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti5S → C AA sequence (PubMed:3060113).Curated1
    Sequence conflicti10 – 12RHS → CIV AA sequence (PubMed:3060113).Curated3
    Sequence conflicti19S → M AA sequence (PubMed:3060113).Curated1
    Sequence conflicti21Missing AA sequence (PubMed:1472094).Curated1
    Sequence conflicti28E → D AA sequence (PubMed:1472094).Curated1
    Sequence conflicti180E → I AA sequence (PubMed:1472094).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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
    WP_000351487.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC73679; AAC73679; b0578
    BAA35218; BAA35218; BAA35218
    GeneIDi945778
    KEGGiecj:JW0567
    eco:b0578
    PATRICifig|1411691.4.peg.1696

    Similar proteinsi

    Entry informationi

    Entry nameiNFSB_ECOLI
    AccessioniPrimary (citable) accession number: P38489
    Secondary accession number(s): P19575
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: March 28, 2018
    This is version 150 of the entry and version 1 of the sequence. See 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