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Protein

CTP pyrophosphohydrolase

Gene

nudG

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

Functioni

Hydrolase with a preference for pyrimidine substrates. Has high activity with 5-methyl-dCTP, and much lower activity with CTP, dCTP, 5-hydroxy-dCTP, 2-hydroxy-dATP and 8-hydroxy-dGTP.3 Publications

Catalytic activityi

CTP + H2O = CMP + diphosphate.4 Publications
dCTP + H2O = dCMP + diphosphate.4 Publications

Cofactori

Mg2+2 Publications, Mn2+2 PublicationsNote: Divalent metal ions. Mg2+ or Mn2+.2 Publications

Kineticsi

  1. KM=0.028 mM for 5-methyl-dCTP2 Publications
  2. KM=0.027 mM for 2-hydroxy-dATP2 Publications
  3. KM=0.41 mM for 8-hydroxy-dGTP2 Publications
  4. KM=0.99 mM for dCTP2 Publications

    pH dependencei

    Optimum pH is 8.5-9.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei72SubstrateCurated1
    Binding sitei118SubstrateCurated1

    GO - Molecular functioni

    • hydrolase activity Source: EcoCyc

    GO - Biological processi

    • DNA repair Source: EcoCyc

    Keywordsi

    Molecular functionHydrolase
    LigandMagnesium, Manganese

    Enzyme and pathway databases

    BioCyciEcoCyc:G6954-MONOMER.
    MetaCyc:G6954-MONOMER.
    BRENDAi3.6.1.65. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CTP pyrophosphohydrolase (EC:3.6.1.654 Publications)
    Gene namesi
    Name:nudG
    Synonyms:ynjG
    Ordered Locus Names:b1759, JW1748
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14009. nudG.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi33E → A or Q: Increases enzyme activity with 2-hydroxy-ATP. Decreases enzyme activity with dCTP, 5-methyl-dCTP and 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi33E → D: Decreases enzyme activity with 2-hydroxy-ATP, dCTP, 5-dmethyl-CTP and 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi36G → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi37G → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi38K → A or R: Strongly reduces enzyme activity with dCTP, and to a lesser degree with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi43E → A: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi51R → A: Abolishes enzyme activity with dCTP. Nearly abolishes enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi52E → A, D or Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi53L → A: Reduces enzyme activity. 1 Publication1
    Mutagenesisi55E → A: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi55E → D or Q: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication1
    Mutagenesisi56E → A, D or Q: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi72R → A: Strongly decreases the activity with 2-hydroxy-ATP. 1 Publication1
    Mutagenesisi77R → A: No effect. 1 Publication1
    Mutagenesisi118D → A or N: Abolishes enzyme activity with 2-hydroxy-ATP. No effect on activity with dCTP, 5-methyl-dCTP and 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi118D → A: Abolishes enzyme activity with dCTP and 2-hydroxy-ATP and decreases activity with 5-methyl-dCTP. Increases activity with 8-hydroxy-ATP. 1 Publication1
    Mutagenesisi118D → E: Increases the activity with 2-hydroxy-ATP. Strongly decreases activity with 8-hydroxy-ATP. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000569901 – 135CTP pyrophosphohydrolaseAdd BLAST135

    Proteomic databases

    PaxDbiP77788.
    PRIDEiP77788.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4260320. 120 interactors.
    DIPiDIP-10376N.
    IntActiP77788. 3 interactors.
    STRINGi316385.ECDH10B_1897.

    Structurei

    Secondary structure

    1135
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 13Combined sources11
    Beta strandi16 – 21Combined sources6
    Beta strandi36 – 38Combined sources3
    Helixi45 – 56Combined sources12
    Beta strandi59 – 62Combined sources4
    Beta strandi65 – 74Combined sources10
    Beta strandi77 – 91Combined sources15
    Beta strandi101 – 104Combined sources4
    Helixi106 – 109Combined sources4
    Helixi118 – 131Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2RRKNMR-A1-135[»]
    ProteinModelPortaliP77788.
    SMRiP77788.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini2 – 127Nudix hydrolasePROSITE-ProRule annotationAdd BLAST126

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni34 – 39Substrate bindingCurated6

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi37 – 58Nudix boxAdd BLAST22

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105M6F. Bacteria.
    COG0494. LUCA.
    HOGENOMiHOG000261967.
    InParanoidiP77788.
    KOiK08320.
    PhylomeDBiP77788.

    Family and domain databases

    InterProiView protein in InterPro
    IPR020476. Nudix_hydrolase.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    PfamiView protein in Pfam
    PF00293. NUDIX. 1 hit.
    PRINTSiPR00502. NUDIXFAMILY.
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiView protein in PROSITE
    PS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P77788-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKMIEVVAAI IERDGKILLA QRPAQSDQAG LWEFAGGKVE PDESQRQALV
    60 70 80 90 100
    RELREELGIE ATVGEYVASH QREVSGRIIH LHAWHVPDFH GTLQAHEHQA
    110 120 130
    LVWCSPEEAL QYPLAPADIP LLEAFMALRA ARPAD
    Length:135
    Mass (Da):15,046
    Last modified:February 1, 1997 - v1
    Checksum:iD85D8B3A6532CA82
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC74829.1.
    AP009048 Genomic DNA. Translation: BAA15549.1.
    PIRiG64935.
    RefSeqiNP_416273.1. NC_000913.3.
    WP_000781888.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74829; AAC74829; b1759.
    BAA15549; BAA15549; BAA15549.
    GeneIDi946277.
    KEGGiecj:JW1748.
    eco:b1759.
    PATRICifig|1411691.4.peg.496.

    Similar proteinsi

    Entry informationi

    Entry nameiNUDG_ECOLI
    AccessioniPrimary (citable) accession number: P77788
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 1, 1997
    Last modified: July 5, 2017
    This is version 127 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, 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