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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

  1. bis(5'-adenosyl)-hexaphosphatase activity Source: SGD
  2. bis(5'-adenosyl)-pentaphosphatase activity Source: SGD
  3. diphosphoinositol-polyphosphate diphosphatase activity Source: SGD
  4. endopolyphosphatase activity Source: SGD
  5. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity Source: UniProtKB-EC
  6. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
  7. inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  8. inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
  9. inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  10. inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
  11. inositol diphosphate tetrakisphosphate diphosphatase activity Source: UniProtKB-EC
  12. m7G(5')pppN diphosphatase activity Source: SGD
  13. metal ion binding Source: UniProtKB-KW
  14. phosphodiesterase decapping endonuclease activity Source: SGD

GO - Biological processi

  1. diadenosine polyphosphate catabolic process Source: SGD
  2. inositol phosphate dephosphorylation Source: SGD
  3. polyphosphate catabolic process Source: SGD
  4. 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.

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: Chromosome XV

Organism-specific databases

SGDiS000005689. DDP1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
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.

Expressioni

Gene expression databases

GenevestigatoriQ99321.

Interactioni

Protein-protein interaction databases

BioGridi34559. 22 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. 22 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

SGDiS000005689. DDP1.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciYEAST:YOR163W-MONOMER.

Miscellaneous databases

NextBioi976396.

Gene expression databases

GenevestigatoriQ99321.

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: January 7, 2015
This is version 133 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.