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Protein

Inosine triphosphate pyrophosphatase

Gene

HAM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and 5-bromodeoxyuridine 5'-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.UniRule annotation3 Publications

Catalytic activityi

A nucleoside triphosphate + H2O = a nucleotide + diphosphate.UniRule annotation

Cofactori

Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 1 divalent metal cation per subunit; can use either Mg2+ or Mn2+.UniRule annotation

Kineticsi

Vmax values are similar for dITP, dHAPTP and dGTP.

  1. KM=13.4 µM for dITP1 Publication
  2. KM=26.9 µM for dHAPTP1 Publication
  3. KM=722 µM for dGTP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Magnesium or manganeseUniRule annotation
    Binding sitei58 – 581SubstrateUniRule annotation
    Metal bindingi76 – 761Magnesium or manganeseUniRule annotation
    Binding sitei175 – 1751SubstrateUniRule annotation

    GO - Molecular functioni

    • dATP pyrophosphohydrolase activity Source: SGD
    • dCTP diphosphatase activity Source: SGD
    • dGTP diphosphatase activity Source: SGD
    • dITP diphosphatase activity Source: SGD
    • dTTP diphosphatase activity Source: SGD
    • dUTP diphosphatase activity Source: SGD
    • GTP diphosphatase activity Source: SGD
    • ITP diphosphatase activity Source: SGD
    • metal ion binding Source: UniProtKB-KW
    • nucleotide binding Source: UniProtKB-KW
    • UTP diphosphatase activity Source: SGD
    • XTP diphosphatase activity Source: SGD

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31702-MONOMER.
    ReactomeiR-SCE-15869. Metabolism of nucleotides.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine triphosphate pyrophosphataseUniRule annotation (EC:3.6.1.19UniRule annotation)
    Short name:
    ITPaseUniRule annotation
    Short name:
    Inosine triphosphataseUniRule annotation
    Alternative name(s):
    Hydroxylaminopurine sensitivity protein 1
    Non-canonical purine NTP pyrophosphataseUniRule annotation
    Non-standard purine NTP pyrophosphataseUniRule annotation
    Nucleoside-triphosphate diphosphataseUniRule annotation
    Nucleoside-triphosphate pyrophosphataseUniRule annotation
    Short name:
    NTPaseUniRule annotation
    Gene namesi
    Name:HAM1UniRule annotation
    Ordered Locus Names:YJR069C
    ORF Names:J1811
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiFungiDB:YJR069C.
    SGDiS000003830. HAM1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 197197Inosine triphosphate pyrophosphatasePRO_0000178279Add
    BLAST

    Proteomic databases

    MaxQBiP47119.
    PeptideAtlasiP47119.

    PTM databases

    iPTMnetiP47119.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    BioGridi33826. 16 interactions.
    DIPiDIP-5491N.
    IntActiP47119. 5 interactions.
    MINTiMINT-476946.

    Structurei

    3D structure databases

    ProteinModelPortaliP47119.
    SMRiP47119. Positions 5-192.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni10 – 156Substrate bindingUniRule annotation
    Regioni76 – 772Substrate bindingUniRule annotation
    Regioni151 – 1544Substrate bindingUniRule annotation
    Regioni180 – 1812Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the HAM1 NTPase family.UniRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00390000015399.
    HOGENOMiHOG000293320.
    InParanoidiP47119.
    KOiK01519.
    OMAiIRFASIN.
    OrthoDBiEOG74R22R.

    Family and domain databases

    Gene3Di3.90.950.10. 1 hit.
    HAMAPiMF_03148. HAM1_NTPase.
    InterProiIPR002637. Ham1p-like.
    IPR027502. ITPase.
    IPR029001. ITPase-like_fam.
    [Graphical view]
    PANTHERiPTHR11067. PTHR11067. 1 hit.
    PfamiPF01725. Ham1p_like. 1 hit.
    [Graphical view]
    SUPFAMiSSF52972. SSF52972. 1 hit.
    TIGRFAMsiTIGR00042. TIGR00042. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P47119-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSNNEIVFVT GNANKLKEVQ SILTQEVDNN NKTIHLINEA LDLEELQDTD
    60 70 80 90 100
    LNAIALAKGK QAVAALGKGK PVFVEDTALR FDEFNGLPGA YIKWFLKSMG
    110 120 130 140 150
    LEKIVKMLEP FENKNAEAVT TICFADSRGE YHFFQGITRG KIVPSRGPTT
    160 170 180 190
    FGWDSIFEPF DSHGLTYAEM SKDAKNAISH RGKAFAQFKE YLYQNDF
    Length:197
    Mass (Da):22,093
    Last modified:February 1, 1996 - v1
    Checksum:i1C7AA19465467C07
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z49569 Genomic DNA. Translation: CAA89597.1.
    L47993 Genomic DNA. Translation: AAB39295.1.
    AY557897 Genomic DNA. Translation: AAS56223.1.
    BK006943 Genomic DNA. Translation: DAA08856.1.
    PIRiS57088.
    RefSeqiNP_012603.1. NM_001181727.1.

    Genome annotation databases

    EnsemblFungiiYJR069C; YJR069C; YJR069C.
    GeneIDi853532.
    KEGGisce:YJR069C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z49569 Genomic DNA. Translation: CAA89597.1.
    L47993 Genomic DNA. Translation: AAB39295.1.
    AY557897 Genomic DNA. Translation: AAS56223.1.
    BK006943 Genomic DNA. Translation: DAA08856.1.
    PIRiS57088.
    RefSeqiNP_012603.1. NM_001181727.1.

    3D structure databases

    ProteinModelPortaliP47119.
    SMRiP47119. Positions 5-192.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33826. 16 interactions.
    DIPiDIP-5491N.
    IntActiP47119. 5 interactions.
    MINTiMINT-476946.

    PTM databases

    iPTMnetiP47119.

    Proteomic databases

    MaxQBiP47119.
    PeptideAtlasiP47119.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYJR069C; YJR069C; YJR069C.
    GeneIDi853532.
    KEGGisce:YJR069C.

    Organism-specific databases

    EuPathDBiFungiDB:YJR069C.
    SGDiS000003830. HAM1.

    Phylogenomic databases

    GeneTreeiENSGT00390000015399.
    HOGENOMiHOG000293320.
    InParanoidiP47119.
    KOiK01519.
    OMAiIRFASIN.
    OrthoDBiEOG74R22R.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31702-MONOMER.
    ReactomeiR-SCE-15869. Metabolism of nucleotides.

    Miscellaneous databases

    PROiP47119.

    Family and domain databases

    Gene3Di3.90.950.10. 1 hit.
    HAMAPiMF_03148. HAM1_NTPase.
    InterProiIPR002637. Ham1p-like.
    IPR027502. ITPase.
    IPR029001. ITPase-like_fam.
    [Graphical view]
    PANTHERiPTHR11067. PTHR11067. 1 hit.
    PfamiPF01725. Ham1p_like. 1 hit.
    [Graphical view]
    SUPFAMiSSF52972. SSF52972. 1 hit.
    TIGRFAMsiTIGR00042. TIGR00042. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity and mutagenesis in the yeast Saccharomyces cerevisiae."
      Noskov V.N., Staak K., Shcherbakova P.V., Kozmin S.G., Negishi K., Ono B.-C., Hayatsu H., Pavlov Y.I.
      Yeast 12:17-29(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI."
      Huang M.-E., Manus V., Chuat J.-C., Galibert F.
      Yeast 12:869-875(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Overexpression of the yeast HAM1 gene prevents 6-N-hydroxylaminopurine mutagenesis in Escherichia coli."
      Kozmin S.G., Leroy P., Pavlov Y.I.
      Acta Biochim. Pol. 45:645-652(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Overexpression of HAM1 gene detoxifies 5-bromodeoxyuridine in the yeast Saccharomyces cerevisiae."
      Takayama S., Fujii M., Kurosawa A., Adachi N., Ayusawa D.
      Curr. Genet. 52:203-211(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase."
      Burgis N.E., Cunningham R.P.
      J. Biol. Chem. 282:3531-3538(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiITPA_YEAST
    AccessioniPrimary (citable) accession number: P47119
    Secondary accession number(s): D6VWP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: June 8, 2016
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3490 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    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.