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Protein

NADPH-dependent 7-cyano-7-deazaguanine reductase

Gene

queF

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

Functioni

Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway. Is highly specific for its natural substrate preQ0, since it cannot use various aliphatic, aromatic, benzylic and heterocyclic nitriles, such as acetonitrile, benzonitrile, benzylcyanide and 2-cyanopyrrole, although it can reduce the substrate analog 5-cyanopyrrolo[2,3-d]pyrimidin-4-one with lesser efficiency.3 Publications

Catalytic activityi

7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2 NADPH.2 Publications

Kineticsi

KM for preQ0 appears to be inferior to 1.5 µM, and kcat is 0.1268 sec(-1) (PubMed:23410922). kcat is 6.5 min(-1) with preQ0 as substrate and 3.6 min(-1) with 5-cyanopyrrolo[2,3-d]pyrimidin-4-one as substrate (PubMed:23595998).2 Publications

  1. KM=36 µM for NADPH3 Publications
  2. KM=6.0 µM for NADPH3 Publications
  3. KM=6.1 µM for 7-cyano-7-deazaguanine3 Publications
  4. KM=176 µM for 5-cyanopyrrolo[2,3-d]pyrimidin-4-one3 Publications

    pH dependencei

    Optimum pH is 7. Retains less than 20% of activity at pH 9 (PubMed:23410922).1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius. Displays a half life of 28.2 hours and 12.8 hours at 37 and 40 degrees Celsius, respectively, but at 50 degrees Celsius the half life time drops to 6 minutes (PubMed:23410922).1 Publication

    Pathwayi: tRNA-queuosine biosynthesis

    This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.
    View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei190 – 1901Thioimide intermediate1 Publication
    Active sitei197 – 1971Proton donor1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi90 – 912NADPHBy similarity
    Nucleotide bindingi258 – 2592NADPHBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • queuosine biosynthetic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Queuosine biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:G7452-MONOMER.
    ECOL316407:JW2765-MONOMER.
    MetaCyc:G7452-MONOMER.
    BRENDAi1.7.1.13. 2026.
    UniPathwayiUPA00392.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADPH-dependent 7-cyano-7-deazaguanine reductase (EC:1.7.1.13)
    Alternative name(s):
    7-cyano-7-carbaguanine reductase
    NADPH-dependent nitrile oxidoreductase
    PreQ(0) reductase
    Gene namesi
    Name:queF
    Synonyms:yqcD
    Ordered Locus Names:b2794, JW2765
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13173. queF.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891E → A or L: Drastic decrease in activity. 1 Publication
    Mutagenesisi90 – 901S → A: 9-fold decrease in specific activity. 1 Publication
    Mutagenesisi190 – 1901C → A: Loss of catalytic activity. 1 Publication
    Mutagenesisi197 – 1971D → N: Loss of catalytic activity. 1 Publication
    Mutagenesisi228 – 2281F → W: 11-fold decrease in specific activity. 1 Publication
    Mutagenesisi229 – 2291H → A: 6.5-fold decrease in specific activity. 1 Publication
    Mutagenesisi230 – 2301E → Q: 26-fold decrease in specific activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282NADPH-dependent 7-cyano-7-deazaguanine reductasePRO_0000163031Add
    BLAST

    Proteomic databases

    PaxDbiQ46920.
    PRIDEiQ46920.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi4262149. 24 interactions.
    DIPiDIP-12848N.
    IntActiQ46920. 6 interactions.
    MINTiMINT-1288325.
    STRINGi511145.b2794.

    Structurei

    3D structure databases

    ProteinModelPortaliQ46920.
    SMRiQ46920. Positions 23-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni88 – 903Substrate bindingCurated
    Regioni229 – 2302Substrate bindingCurated

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107R1K. Bacteria.
    COG0780. LUCA.
    COG2904. LUCA.
    HOGENOMiHOG000273755.
    InParanoidiQ46920.
    KOiK06879.
    OMAiQCVERIY.

    Family and domain databases

    HAMAPiMF_00817. QueF_type2. 1 hit.
    InterProiIPR029500. QueF.
    IPR029139. QueF_N.
    IPR016428. QueF_type2.
    [Graphical view]
    PfamiPF14489. QueF. 1 hit.
    PF14819. QueF_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004750. Nitrile_oxidored_YqcD_prd. 1 hit.
    TIGRFAMsiTIGR03138. QueF. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q46920-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSYANHQAL AGLTLGKSTD YRDTYDASLL QGVPRSLNRD PLGLKADNLP
    60 70 80 90 100
    FHGTDIWTLY ELSWLNAKGL PQVAVGHVEL DYTSVNLIES KSFKLYLNSF
    110 120 130 140 150
    NQTRFNNWDE VRQTLERDLS TCAQGKISVA LYRLDELEGQ PIGHFNGTCI
    160 170 180 190 200
    DDQDITIDNY EFTTDYLENA TCGEKVVEET LVSHLLKSNC LITHQPDWGS
    210 220 230 240 250
    LQIQYRGRQI DREKLLRYLV SFRHHNEFHE QCVERIFNDL LRFCQPEKLS
    260 270 280
    VYARYTRRGG LDINPWRSNS DFVPSTTRLV RQ
    Length:282
    Mass (Da):32,588
    Last modified:November 1, 1996 - v1
    Checksum:i3C22B9BA7AA3C79D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U29581 Genomic DNA. Translation: AAB40444.1.
    U00096 Genomic DNA. Translation: AAC75836.1.
    AP009048 Genomic DNA. Translation: BAE76866.1.
    PIRiF65061.
    RefSeqiNP_417274.1. NC_000913.3.
    WP_000100421.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75836; AAC75836; b2794.
    BAE76866; BAE76866; BAE76866.
    GeneIDi947270.
    KEGGiecj:JW2765.
    eco:b2794.
    PATRICi32121004. VBIEscCol129921_2894.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U29581 Genomic DNA. Translation: AAB40444.1.
    U00096 Genomic DNA. Translation: AAC75836.1.
    AP009048 Genomic DNA. Translation: BAE76866.1.
    PIRiF65061.
    RefSeqiNP_417274.1. NC_000913.3.
    WP_000100421.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliQ46920.
    SMRiQ46920. Positions 23-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4262149. 24 interactions.
    DIPiDIP-12848N.
    IntActiQ46920. 6 interactions.
    MINTiMINT-1288325.
    STRINGi511145.b2794.

    Proteomic databases

    PaxDbiQ46920.
    PRIDEiQ46920.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75836; AAC75836; b2794.
    BAE76866; BAE76866; BAE76866.
    GeneIDi947270.
    KEGGiecj:JW2765.
    eco:b2794.
    PATRICi32121004. VBIEscCol129921_2894.

    Organism-specific databases

    EchoBASEiEB2965.
    EcoGeneiEG13173. queF.

    Phylogenomic databases

    eggNOGiENOG4107R1K. Bacteria.
    COG0780. LUCA.
    COG2904. LUCA.
    HOGENOMiHOG000273755.
    InParanoidiQ46920.
    KOiK06879.
    OMAiQCVERIY.

    Enzyme and pathway databases

    UniPathwayiUPA00392.
    BioCyciEcoCyc:G7452-MONOMER.
    ECOL316407:JW2765-MONOMER.
    MetaCyc:G7452-MONOMER.
    BRENDAi1.7.1.13. 2026.

    Miscellaneous databases

    PROiQ46920.

    Family and domain databases

    HAMAPiMF_00817. QueF_type2. 1 hit.
    InterProiIPR029500. QueF.
    IPR029139. QueF_N.
    IPR016428. QueF_type2.
    [Graphical view]
    PfamiPF14489. QueF. 1 hit.
    PF14819. QueF_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004750. Nitrile_oxidored_YqcD_prd. 1 hit.
    TIGRFAMsiTIGR03138. QueF. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiQUEF_ECOLI
    AccessioniPrimary (citable) accession number: Q46920
    Secondary accession number(s): Q2MA40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: September 7, 2016
    This is version 125 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

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.