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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721SubstrateCurated
    Binding sitei118 – 1181SubstrateCurated

    GO - Molecular functioni

    • hydrolase activity Source: EcoCyc

    GO - Biological processi

    • DNA repair Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Manganese

    Enzyme and pathway databases

    BioCyciEcoCyc:G6954-MONOMER.
    ECOL316407:JW1748-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14009. nudG.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331E → A or Q: Increases enzyme activity with 2-hydroxy-ATP. Decreases enzyme activity with dCTP, 5-methyl-dCTP and 8-hydroxy-ATP. 1 Publication
    Mutagenesisi33 – 331E → D: Decreases enzyme activity with 2-hydroxy-ATP, dCTP, 5-dmethyl-CTP and 8-hydroxy-ATP. 1 Publication
    Mutagenesisi36 – 361G → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi37 – 371G → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi38 – 381K → A or R: Strongly reduces enzyme activity with dCTP, and to a lesser degree with 5-methyl-dCTP. 1 Publication
    Mutagenesisi43 – 431E → A: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication
    Mutagenesisi51 – 511R → A: Abolishes enzyme activity with dCTP. Nearly abolishes enzyme activity with 5-methyl-dCTP. 1 Publication
    Mutagenesisi52 – 521E → A, D or Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi53 – 531L → A: Reduces enzyme activity. 1 Publication
    Mutagenesisi55 – 551E → A: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication
    Mutagenesisi55 – 551E → D or Q: Abolishes enzyme activity with dCTP and reduces enzyme activity with 5-methyl-dCTP. 1 Publication
    Mutagenesisi56 – 561E → A, D or Q: Abolishes enzyme activity. 1 Publication
    Mutagenesisi72 – 721R → A: Strongly decreases the activity with 2-hydroxy-ATP. 1 Publication
    Mutagenesisi77 – 771R → A: No effect. 1 Publication
    Mutagenesisi118 – 1181D → A or N: Abolishes enzyme activity with 2-hydroxy-ATP. No effect on activity with dCTP, 5-methyl-dCTP and 8-hydroxy-ATP. 1 Publication
    Mutagenesisi118 – 1181D → A: Abolishes enzyme activity with dCTP and 2-hydroxy-ATP and decreases activity with 5-methyl-dCTP. Increases activity with 8-hydroxy-ATP. 1 Publication
    Mutagenesisi118 – 1181D → E: Increases the activity with 2-hydroxy-ATP. Strongly decreases activity with 8-hydroxy-ATP. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 135135CTP pyrophosphohydrolasePRO_0000056990Add
    BLAST

    Proteomic databases

    PaxDbiP77788.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi4260320. 120 interactions.
    DIPiDIP-10376N.
    IntActiP77788. 3 interactions.
    STRINGi511145.b1759.

    Structurei

    Secondary structure

    1
    135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1311Combined sources
    Beta strandi16 – 216Combined sources
    Beta strandi36 – 383Combined sources
    Helixi45 – 5612Combined sources
    Beta strandi59 – 624Combined sources
    Beta strandi65 – 7410Combined sources
    Beta strandi77 – 9115Combined sources
    Beta strandi101 – 1044Combined sources
    Helixi106 – 1094Combined sources
    Helixi118 – 13114Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RRKNMR-A1-135[»]
    ProteinModelPortaliP77788.
    SMRiP77788. Positions 1-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 127126Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni34 – 396Substrate bindingCurated

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 5822Nudix boxAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family.Curated
    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    Phylogenomic databases

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

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR020476. Nudix_hydrolase.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    PRINTSiPR00502. NUDIXFAMILY.
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]

    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.
    PATRICi32118829. VBIEscCol129921_1832.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RRKNMR-A1-135[»]
    ProteinModelPortaliP77788.
    SMRiP77788. Positions 1-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260320. 120 interactions.
    DIPiDIP-10376N.
    IntActiP77788. 3 interactions.
    STRINGi511145.b1759.

    Proteomic databases

    PaxDbiP77788.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74829; AAC74829; b1759.
    BAA15549; BAA15549; BAA15549.
    GeneIDi946277.
    KEGGiecj:JW1748.
    eco:b1759.
    PATRICi32118829. VBIEscCol129921_1832.

    Organism-specific databases

    EchoBASEiEB3765.
    EcoGeneiEG14009. nudG.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyciEcoCyc:G6954-MONOMER.
    ECOL316407:JW1748-MONOMER.
    MetaCyc:G6954-MONOMER.
    BRENDAi3.6.1.65. 2026.

    Miscellaneous databases

    PROiP77788.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR020476. Nudix_hydrolase.
    IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    PRINTSiPR00502. NUDIXFAMILY.
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiNUDG_ECOLI
    AccessioniPrimary (citable) accession number: P77788
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 1, 1997
    Last modified: September 7, 2016
    This is version 121 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

    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

    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.