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Q05788 (PNPH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Purine nucleoside phosphorylase

Short name=PNP
EC=2.4.2.1
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Gene names
Name:PNP1
Ordered Locus Names:YLR209C
ORF Names:L8167.19
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine By similarity.

Catalytic activity

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.

Pathway

Purine metabolism; purine nucleoside salvage.

Miscellaneous

Present with 1630 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SRP1Q028211EBI-13604,EBI-1797

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 311310Purine nucleoside phosphorylase
PRO_0000184538

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue2751Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q05788 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 159DB9F9EC393BCA

FASTA31133,755
        10         20         30         40         50         60 
MSDILNVSQQ REAITKAAAY ISAILEPHFK NTTNFEPPRT LIICGSGLGG ISTKLSRDNP 

        70         80         90        100        110        120 
PPVTVPYQDI PGFKKSTVPG HSGTLMFGSM NGSPVVLMNG RLHGYEGNTL FETTFPIRVL 

       130        140        150        160        170        180 
NHMGHVRNLI VTNAAGGINA KYQACDLMCI YDHLNIPGLA GQHPLRGPNL DEDGPRFLAL 

       190        200        210        220        230        240 
SDAYDLELRK LLFKKWKELK IQRPLHEGTY TFVSGPTFET RAESKMIRML GGDAVGMSTV 

       250        260        270        280        290        300 
PEVIVARHCG WRVLALSLIT NTCVVDSPAS ALDESPVPLE KGKATHAEVL ENGKIASNDV 

       310 
QNLIAAVMGE L 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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].
[5]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14913 Genomic DNA. Translation: AAB67440.1.
AY557950 Genomic DNA. Translation: AAS56276.1.
BK006945 Genomic DNA. Translation: DAA09526.1.
PIRS48560.
RefSeqNP_013310.1. NM_001182096.1.

3D structure databases

ProteinModelPortalQ05788.
SMRQ05788. Positions 12-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31477. 7 interactions.
DIPDIP-4300N.
IntActQ05788. 3 interactions.
MINTMINT-550315.
STRING4932.YLR209C.

Proteomic databases

PaxDbQ05788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR209C; YLR209C; YLR209C.
GeneID850906.
KEGGsce:YLR209C.

Organism-specific databases

CYGDYLR209c.
SGDS000004199. PNP1.

Phylogenomic databases

eggNOGCOG0005.
GeneTreeENSGT00550000074740.
HOGENOMHOG000045183.
KOK03783.
OMACGISCIT.
OrthoDBEOG72C59D.

Enzyme and pathway databases

BioCycYEAST:YLR209C-MONOMER.
UniPathwayUPA00606.

Gene expression databases

GenevestigatorQ05788.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
InterProIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFPIRSF000477. PurNPase. 1 hit.
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967302.
PROQ05788.

Entry information

Entry namePNPH_YEAST
AccessionPrimary (citable) accession number: Q05788
Secondary accession number(s): D6VYL0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways