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Protein

Diphosphoinositol polyphosphate phosphohydrolase DDP1

Gene

DDP1

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

May eliminate potentially toxic dinucleoside polyphosphates during sporulation. Most active against diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A). Can also hydrolyze diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A), adenosine 5'-pentaphosphate, and adenosine 5'-tetraphosphate are also substrates, but not diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols. Also cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate).

Catalytic activityi

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.1 Publication
P1,P(6)-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP.1 Publication
P1,P(5)-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP.1 Publication

Cofactori

Kineticsi

  1. KM=31 nM for PP-InsP51 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi80 – 801MagnesiumBy similarity
    Metal bindingi84 – 841MagnesiumBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • diadenosine polyphosphate catabolic process Source: SGD
    • inositol phosphate dephosphorylation Source: SGD
    • polyphosphate catabolic process Source: SGD
    • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YOR163W-MONOMER.
    BRENDAi3.6.1.B13. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diphosphoinositol polyphosphate phosphohydrolase DDP1 (EC:3.6.1.52)
    Alternative name(s):
    Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase
    Short name:
    Ap6A hydrolase
    Diadenosine and diphosphoinositol polyphosphate phosphohydrolase 1
    Diadenosine hexaphosphate hydrolase (AMP-forming) (EC:3.6.1.60)
    Gene namesi
    Name:DDP1
    Ordered Locus Names:YOR163W
    ORF Names:O3575
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome XV

    Organism-specific databases

    EuPathDBiFungiDB:YOR163W.
    SGDiS000005689. DDP1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 188187Diphosphoinositol polyphosphate phosphohydrolase DDP1PRO_0000057067Add
    BLAST

    Proteomic databases

    MaxQBiQ99321.
    PaxDbiQ99321.
    PeptideAtlasiQ99321.

    Interactioni

    Protein-protein interaction databases

    BioGridi34559. 23 interactions.
    IntActiQ99321. 3 interactions.
    MINTiMINT-2493420.
    STRINGi4932.YOR163W.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99321.
    SMRiQ99321. Positions 35-99.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 179150Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi65 – 8622Nudix boxAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0494.
    HOGENOMiHOG000165198.
    InParanoidiQ99321.
    KOiK07766.
    OMAiRVGRENQ.
    OrthoDBiEOG7WHHNP.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99321-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGKTADNHGP VRSETAREGR ENQVYSPVTG ARLVAGCICL TPDKKQVLMI
    60 70 80 90 100
    TSSAHKKRWI VPKGGVEKDE PNYETTAQRE TWEEAGCIGK IVANLGTVED
    110 120 130 140 150
    MRPPKDWNKD IKQFENSRKD SEVAKHPPRT EFHFYELEIE NLLDKFPECH
    160 170 180
    KRHRKLYSYT EAKQNLIDAK RPELLEALNR SAIIKDDK
    Length:188
    Mass (Da):21,572
    Last modified:January 23, 2007 - v3
    Checksum:i17A39EB060F03184
    GO

    Mass spectrometryi

    Molecular mass is 21443 Da from positions 2 - 188. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z75071 Genomic DNA. Translation: CAA99369.1.
    U55021 Genomic DNA. Translation: AAB47410.1.
    AY558436 Genomic DNA. Translation: AAS56762.1.
    BK006948 Genomic DNA. Translation: DAA10937.1.
    PIRiS67051.
    RefSeqiNP_014806.1. NM_001183582.1.

    Genome annotation databases

    EnsemblFungiiYOR163W; YOR163W; YOR163W.
    GeneIDi854334.
    KEGGisce:YOR163W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z75071 Genomic DNA. Translation: CAA99369.1.
    U55021 Genomic DNA. Translation: AAB47410.1.
    AY558436 Genomic DNA. Translation: AAS56762.1.
    BK006948 Genomic DNA. Translation: DAA10937.1.
    PIRiS67051.
    RefSeqiNP_014806.1. NM_001183582.1.

    3D structure databases

    ProteinModelPortaliQ99321.
    SMRiQ99321. Positions 35-99.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi34559. 23 interactions.
    IntActiQ99321. 3 interactions.
    MINTiMINT-2493420.
    STRINGi4932.YOR163W.

    Proteomic databases

    MaxQBiQ99321.
    PaxDbiQ99321.
    PeptideAtlasiQ99321.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYOR163W; YOR163W; YOR163W.
    GeneIDi854334.
    KEGGisce:YOR163W.

    Organism-specific databases

    EuPathDBiFungiDB:YOR163W.
    SGDiS000005689. DDP1.

    Phylogenomic databases

    eggNOGiCOG0494.
    HOGENOMiHOG000165198.
    InParanoidiQ99321.
    KOiK07766.
    OMAiRVGRENQ.
    OrthoDBiEOG7WHHNP.

    Enzyme and pathway databases

    BioCyciYEAST:YOR163W-MONOMER.
    BRENDAi3.6.1.B13. 984.

    Miscellaneous databases

    NextBioi976396.
    PROiQ99321.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Analysis of a 22,956 bp region on the right arm of Saccharomyces cerevisiae chromosome XV."
      Madania A., Poch O., Tarassov I.A., Winsor B., Martin R.P.
      Yeast 12:1563-1573(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S288c / FY1678.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "The Saccharomyces cerevisiae YOR163w gene encodes a diadenosine 5', 5'''-P1,P6-hexaphosphate (Ap6A) hydrolase member of the MutT motif (Nudix hydrolase) family."
      Cartwright J.L., McLennan A.G.
      J. Biol. Chem. 274:8604-8610(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 2-13, MASS SPECTROMETRY.
    6. "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein."
      Safrany S.T., Ingram S.W., Cartwright J.L., Falck J.R., McLennan A.G., Barnes L.D., Shears S.B.
      J. Biol. Chem. 274:21735-21740(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDDP1_YEAST
    AccessioniPrimary (citable) accession number: Q99321
    Secondary accession number(s): D6W2M1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: June 24, 2015
    This is version 137 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 3340 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3

    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 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.