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Q99321 (DDP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:DDP1
Ordered Locus Names:YOR163W
ORF Names:O3575
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate. Ref.6

P1,P(6)-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP. Ref.6

P1,P(5)-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP. Ref.6

Cofactor

Magnesium.

Subcellular location

Cytoplasm. Nucleus Ref.7.

Miscellaneous

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

Sequence similarities

Belongs to the Nudix hydrolase family. DIPP subfamily.

Contains 1 nudix hydrolase domain.

Biophysicochemical properties

Kinetic parameters:

KM=31 nM for PP-InsP5 Ref.6

Mass spectrometry

Molecular mass is 21443 Da from positions 2 - 188. Determined by ESI. Ref.5

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay PubMed 23353937. Source: GOC

diadenosine polyphosphate catabolic process

Inferred from direct assay Ref.5PubMed 9450008. Source: SGD

inositol phosphate dephosphorylation

Inferred from direct assay Ref.6. Source: SGD

polyphosphate catabolic process

Inferred from direct assay PubMed 21775424. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbis(5'-adenosyl)-hexaphosphatase activity

Inferred from direct assay Ref.5PubMed 9450008. Source: SGD

bis(5'-adenosyl)-pentaphosphatase activity

Inferred from direct assay Ref.5PubMed 9450008. Source: SGD

diphosphoinositol-polyphosphate diphosphatase activity

Inferred from direct assay Ref.6. Source: SGD

endopolyphosphatase activity

Inferred from direct assay PubMed 21775424. Source: SGD

inositol diphosphate tetrakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

m7G(5')pppN diphosphatase activity

Inferred from direct assay PubMed 23353937. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphodiesterase decapping endonuclease activity

Inferred from direct assay PubMed 23353937. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 188187Diphosphoinositol polyphosphate phosphohydrolase DDP1
PRO_0000057067

Regions

Domain30 – 179150Nudix hydrolase
Motif65 – 8622Nudix box

Sites

Metal binding801Magnesium By similarity
Metal binding841Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99321 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 17A39EB060F03184

FASTA18821,572
        10         20         30         40         50         60 
MGKTADNHGP VRSETAREGR ENQVYSPVTG ARLVAGCICL TPDKKQVLMI TSSAHKKRWI 

        70         80         90        100        110        120 
VPKGGVEKDE PNYETTAQRE TWEEAGCIGK IVANLGTVED MRPPKDWNKD IKQFENSRKD 

       130        140        150        160        170        180 
SEVAKHPPRT EFHFYELEIE NLLDKFPECH KRHRKLYSYT EAKQNLIDAK RPELLEALNR 


SAIIKDDK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z75071 Genomic DNA. Translation: CAA99369.1.
U55021 Genomic DNA. Translation: AAB47410.1.
AY558436 Genomic DNA. Translation: AAS56762.1.
BK006948 Genomic DNA. Translation: DAA10937.1.
PIRS67051.
RefSeqNP_014806.1. NM_001183582.1.

3D structure databases

ProteinModelPortalQ99321.
SMRQ99321. Positions 35-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34559. 21 interactions.
IntActQ99321. 3 interactions.
MINTMINT-2493420.
STRING4932.YOR163W.

Proteomic databases

MaxQBQ99321.
PaxDbQ99321.
PeptideAtlasQ99321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR163W; YOR163W; YOR163W.
GeneID854334.
KEGGsce:YOR163W.

Organism-specific databases

SGDS000005689. DDP1.

Phylogenomic databases

eggNOGCOG0494.
HOGENOMHOG000165198.
KOK01529.
OMAKSSEWLA.
OrthoDBEOG7WHHNP.

Enzyme and pathway databases

BioCycYEAST:YOR163W-MONOMER.

Gene expression databases

GenevestigatorQ99321.

Family and domain databases

Gene3D3.90.79.10. 1 hit.
InterProIPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. SSF55811. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976396.

Entry information

Entry nameDDP1_YEAST
AccessionPrimary (citable) accession number: Q99321
Secondary accession number(s): D6W2M1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families