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Protein

NADPH-dependent 7-cyano-7-deazaguanine reductase

Gene

queF

Organism
Bacillus subtilis (strain 168)
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.2 Publications

Catalytic activityi

7-aminomethyl-7-carbaguanine + 2 NADP+ = 7-cyano-7-carbaguanine + 2 NADPH.1 Publication

Cofactori

Note: Does not require a metal cofactor.

Enzyme regulationi

Activity is strongly inhibited by Cu2+ and Fe3+.1 Publication

Kineticsi

kcat is 0.66 min(-1) (at pH 7.5 and 30 degrees Celsius).

  1. KM=0.237 µM for 7-cyano-7-deazaguanine (at pH 7.5 and 30 degrees Celsius)1 Publication
  2. KM=19.2 µM for NADPH (at pH 7.5 and 30 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.5.1 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 sitei56 – 561Thioimide intermediate
    Active sitei63 – 631Proton donor
    Metal bindingi163 – 1631Magnesium or calcium
    Metal bindingi165 – 1651Magnesium or calcium

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Queuosine biosynthesis

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciBSUB:BSU13750-MONOMER.
    BRENDAi1.7.1.13. 658.
    SABIO-RKO31678.
    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:ykvM
    Ordered Locus Names:BSU13750
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561C → A or S: Loss of catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 165165NADPH-dependent 7-cyano-7-deazaguanine reductasePRO_0000162957Add
    BLAST

    Proteomic databases

    PaxDbiO31678.

    Interactioni

    Subunit structurei

    Forms an asymmetric tunnel-fold homodecamer of two head-to-head facing pentamers, harboring 10 active sites at the intersubunit interfaces.1 Publication

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100007611.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 303Combined sources
    Beta strandi33 – 353Combined sources
    Beta strandi44 – 5512Combined sources
    Beta strandi57 – 593Combined sources
    Beta strandi62 – 7211Combined sources
    Beta strandi74 – 785Combined sources
    Helixi80 – 889Combined sources
    Turni89 – 924Combined sources
    Helixi97 – 11216Combined sources
    Beta strandi115 – 1239Combined sources
    Beta strandi126 – 1294Combined sources
    Beta strandi134 – 1385Combined sources
    Helixi144 – 15714Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F8BX-ray2.50A/B/C/D/E1-165[»]
    4FGCX-ray2.50A/B/C/D/E1-165[»]
    ProteinModelPortaliO31678.
    SMRiO31678. Positions 7-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni78 – 803Substrate binding
    Regioni97 – 982Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CSD. Bacteria.
    COG0780. LUCA.
    HOGENOMiHOG000009528.
    InParanoidiO31678.
    KOiK09457.
    OMAiTLECKEF.
    PhylomeDBiO31678.

    Family and domain databases

    HAMAPiMF_00818. QueF_type1. 1 hit.
    InterProiIPR029500. QueF.
    IPR016856. QueF_type1.
    [Graphical view]
    PfamiPF14489. QueF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027377. Nitrile_oxidored_QueF. 1 hit.
    TIGRFAMsiTIGR03139. QueF-II. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O31678-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTTRKESELE GVTLLGNQGT NYLFEYAPDV LESFPNKHVN RDYFVKFNCP
    60 70 80 90 100
    EFTSLCPKTG QPDFATIYIS YIPDEKMVES KSLKLYLFSF RNHGDFHEDC
    110 120 130 140 150
    MNIIMNDLIE LMDPRYIEVW GKFTPRGGIS IDPYTNYGKP GTKYEKMAEY
    160
    RMMNHDLYPE TIDNR
    Length:165
    Mass (Da):19,375
    Last modified:January 1, 1998 - v1
    Checksum:iE1CEF14D1EAA007D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13248.1.
    PIRiD69868.
    RefSeqiNP_389258.1. NC_000964.3.
    WP_003218613.1. NZ_JNCM01000035.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13248; CAB13248; BSU13750.
    GeneIDi23409456.
    939296.
    KEGGibsu:BSU13750.
    PATRICi18974519. VBIBacSub10457_1451.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL009126 Genomic DNA. Translation: CAB13248.1.
    PIRiD69868.
    RefSeqiNP_389258.1. NC_000964.3.
    WP_003218613.1. NZ_JNCM01000035.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F8BX-ray2.50A/B/C/D/E1-165[»]
    4FGCX-ray2.50A/B/C/D/E1-165[»]
    ProteinModelPortaliO31678.
    SMRiO31678. Positions 7-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100007611.

    Proteomic databases

    PaxDbiO31678.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB13248; CAB13248; BSU13750.
    GeneIDi23409456.
    939296.
    KEGGibsu:BSU13750.
    PATRICi18974519. VBIBacSub10457_1451.

    Phylogenomic databases

    eggNOGiENOG4105CSD. Bacteria.
    COG0780. LUCA.
    HOGENOMiHOG000009528.
    InParanoidiO31678.
    KOiK09457.
    OMAiTLECKEF.
    PhylomeDBiO31678.

    Enzyme and pathway databases

    UniPathwayiUPA00392.
    BioCyciBSUB:BSU13750-MONOMER.
    BRENDAi1.7.1.13. 658.
    SABIO-RKO31678.

    Family and domain databases

    HAMAPiMF_00818. QueF_type1. 1 hit.
    InterProiIPR029500. QueF.
    IPR016856. QueF_type1.
    [Graphical view]
    PfamiPF14489. QueF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF027377. Nitrile_oxidored_QueF. 1 hit.
    TIGRFAMsiTIGR03139. QueF-II. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiQUEF_BACSU
    AccessioniPrimary (citable) accession number: O31678
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: January 1, 1998
    Last modified: September 7, 2016
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Crystallographic structure revealed that QueF enzyme forms an asymmetric tunnel-fold homodecamer (PubMed:22787148) and not a homododecamer as originally proposed (PubMed:15767583).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.