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Protein

Purine nucleoside phosphorylase

Gene

PNP1

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

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).By similarity

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. inosine nucleosidase activity Source: SGD
  2. nicotinamide riboside hydrolase activity Source: SGD
  3. purine-nucleoside phosphorylase activity Source: SGD

GO - Biological processi

  1. guanosine catabolic process Source: SGD
  2. inosine catabolic process Source: SGD
  3. NAD biosynthesis via nicotinamide riboside salvage pathway Source: SGD
  4. nicotinate nucleotide salvage Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YLR209C-MONOMER.
ReactomeiREACT_236121. Purine catabolism.
REACT_240981. Purine salvage.
UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylase (EC:2.4.2.1)
Short name:
PNP
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Gene namesi
Name:PNP1
Ordered Locus Names:YLR209C
ORF Names:L8167.19
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR209c.
SGDiS000004199. PNP1.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 311310Purine nucleoside phosphorylasePRO_0000184538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei275 – 2751Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ05788.
PaxDbiQ05788.

Expressioni

Gene expression databases

GenevestigatoriQ05788.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SRP1Q028211EBI-13604,EBI-1797

Protein-protein interaction databases

BioGridi31477. 8 interactions.
DIPiDIP-4300N.
IntActiQ05788. 3 interactions.
MINTiMINT-550315.
STRINGi4932.YLR209C.

Structurei

3D structure databases

ProteinModelPortaliQ05788.
SMRiQ05788. Positions 12-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
InParanoidiQ05788.
KOiK03783.
OMAiIITDECF.
OrthoDBiEOG72C59D.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDILNVSQQ REAITKAAAY ISAILEPHFK NTTNFEPPRT LIICGSGLGG
60 70 80 90 100
ISTKLSRDNP PPVTVPYQDI PGFKKSTVPG HSGTLMFGSM NGSPVVLMNG
110 120 130 140 150
RLHGYEGNTL FETTFPIRVL NHMGHVRNLI VTNAAGGINA KYQACDLMCI
160 170 180 190 200
YDHLNIPGLA GQHPLRGPNL DEDGPRFLAL SDAYDLELRK LLFKKWKELK
210 220 230 240 250
IQRPLHEGTY TFVSGPTFET RAESKMIRML GGDAVGMSTV PEVIVARHCG
260 270 280 290 300
WRVLALSLIT NTCVVDSPAS ALDESPVPLE KGKATHAEVL ENGKIASNDV
310
QNLIAAVMGE L
Length:311
Mass (Da):33,755
Last modified:November 1, 1996 - v1
Checksum:i159DB9F9EC393BCA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67440.1.
AY557950 Genomic DNA. Translation: AAS56276.1.
BK006945 Genomic DNA. Translation: DAA09526.1.
PIRiS48560.
RefSeqiNP_013310.1. NM_001182096.1.

Genome annotation databases

EnsemblFungiiYLR209C; YLR209C; YLR209C.
GeneIDi850906.
KEGGisce:YLR209C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14913 Genomic DNA. Translation: AAB67440.1.
AY557950 Genomic DNA. Translation: AAS56276.1.
BK006945 Genomic DNA. Translation: DAA09526.1.
PIRiS48560.
RefSeqiNP_013310.1. NM_001182096.1.

3D structure databases

ProteinModelPortaliQ05788.
SMRiQ05788. Positions 12-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31477. 8 interactions.
DIPiDIP-4300N.
IntActiQ05788. 3 interactions.
MINTiMINT-550315.
STRINGi4932.YLR209C.

Proteomic databases

MaxQBiQ05788.
PaxDbiQ05788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR209C; YLR209C; YLR209C.
GeneIDi850906.
KEGGisce:YLR209C.

Organism-specific databases

CYGDiYLR209c.
SGDiS000004199. PNP1.

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
InParanoidiQ05788.
KOiK03783.
OMAiIITDECF.
OrthoDBiEOG72C59D.

Enzyme and pathway databases

UniPathwayiUPA00606.
BioCyciYEAST:YLR209C-MONOMER.
ReactomeiREACT_236121. Purine catabolism.
REACT_240981. Purine salvage.

Miscellaneous databases

NextBioi967302.
PROiQ05788.

Gene expression databases

GenevestigatoriQ05788.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPNPH_YEAST
AccessioniPrimary (citable) accession number: Q05788
Secondary accession number(s): D6VYL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: February 4, 2015
This is version 128 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 1630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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