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Q01234

- NFNB_ENTCL

UniProt

Q01234 - NFNB_ENTCL

Protein

Oxygen-insensitive NAD(P)H nitroreductase

Gene

nfnB

Organism
Enterobacter cloacae
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred.

    Cofactori

    FMN.

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. oxidoreductase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN, NAD, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oxygen-insensitive NAD(P)H nitroreductase (EC:1.-.-.-)
    Short name:
    NR
    Gene namesi
    Name:nfnB
    Synonyms:nfsI
    OrganismiEnterobacter cloacae
    Taxonomic identifieri550 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217Oxygen-insensitive NAD(P)H nitroreductasePRO_0000072712Add
    BLAST

    Proteomic databases

    PRIDEiQ01234.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 97
    Helixi24 – 3613
    Helixi40 – 423
    Beta strandi46 – 516
    Helixi54 – 607
    Helixi61 – 633
    Helixi66 – 716
    Helixi72 – 776
    Beta strandi78 – 8912
    Helixi92 – 10413
    Helixi111 – 12919
    Turni130 – 1323
    Helixi135 – 15622
    Helixi169 – 1757
    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
    1KQBX-ray1.80A/B/C/D1-217[»]
    1KQCX-ray1.80A/B/C/D1-217[»]
    1KQDX-ray1.90A/B/C/D1-217[»]
    1NECX-ray1.95A/B/C/D2-217[»]
    ProteinModelPortaliQ01234.
    SMRiQ01234. Positions 2-217.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01234.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nitroreductase family.Curated

    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.

    Q01234-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDIISVALKR HSTKAFDASK KLTAEEAEKI KTLLQYSPSS TNSQPWHFIV    50
    ASTEEGKARV AKSAAGTYVF NERKMLDASH VVVFCAKTAM DDAWLERVVD 100
    QEEADGRFNT PEAKAANHKG RTYFADMHRV DLKDDDQWMA KQVYLNVGNF 150
    LLGVGAMGLD AVPIEGFDAA ILDEEFGLKE KGFTSLVVVP VGHHSVEDFN 200
    ATLPKSRLPL STIVTEC 217
    Length:217
    Mass (Da):23,950
    Last modified:July 1, 1993 - v1
    Checksum:iC42AA3DB184D5D9B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63808 Genomic DNA. Translation: AAA62801.1.
    PIRiA38686.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63808 Genomic DNA. Translation: AAA62801.1 .
    PIRi A38686.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KQB X-ray 1.80 A/B/C/D 1-217 [» ]
    1KQC X-ray 1.80 A/B/C/D 1-217 [» ]
    1KQD X-ray 1.90 A/B/C/D 1-217 [» ]
    1NEC X-ray 1.95 A/B/C/D 2-217 [» ]
    ProteinModelPortali Q01234.
    SMRi Q01234. Positions 2-217.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q01234.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q01234.

    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

    1. "Cloning, nucleotide sequence, and expression of the nitroreductase gene from Enterobacter cloacae."
      Bryant C., Hubbard L., McElroy W.D.
      J. Biol. Chem. 266:4126-4130(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 43560 / 96-3.
    2. "Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae."
      Bryant C., Deluca M.
      J. Biol. Chem. 266:4119-4125(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    3. "Structures of nitroreductase in three states: effects of inhibitor binding and reduction."
      Haynes C.A., Koder R.L., Miller A.-F., Rodgers D.W.
      J. Biol. Chem. 277:11513-11520(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH FMN; ACETATE AND BENZOIC ACID, SUBUNIT.

    Entry informationi

    Entry nameiNFNB_ENTCL
    AccessioniPrimary (citable) accession number: Q01234
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 65 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The nitroreductase might be involved in the quinone metabolism.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3