Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q05788

- PNPH_YEAST

UniProt

Q05788 - PNPH_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Purine nucleoside phosphorylase

Gene

PNP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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.
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 11-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
InParanoidiQ05788.
KOiK03783.
OMAiDHINMLP.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U14913 Genomic DNA. Translation: AAB67440.1 .
AY557950 Genomic DNA. Translation: AAS56276.1 .
BK006945 Genomic DNA. Translation: DAA09526.1 .
PIRi S48560.
RefSeqi NP_013310.1. NM_001182096.1.

3D structure databases

ProteinModelPortali Q05788.
SMRi Q05788. Positions 11-308.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31477. 8 interactions.
DIPi DIP-4300N.
IntActi Q05788. 3 interactions.
MINTi MINT-550315.
STRINGi 4932.YLR209C.

Proteomic databases

MaxQBi Q05788.
PaxDbi Q05788.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR209C ; YLR209C ; YLR209C .
GeneIDi 850906.
KEGGi sce:YLR209C.

Organism-specific databases

CYGDi YLR209c.
SGDi S000004199. PNP1.

Phylogenomic databases

eggNOGi COG0005.
GeneTreei ENSGT00550000074740.
HOGENOMi HOG000045183.
InParanoidi Q05788.
KOi K03783.
OMAi DHINMLP.
OrthoDBi EOG72C59D.

Enzyme and pathway databases

UniPathwayi UPA00606 .
BioCyci YEAST:YLR209C-MONOMER.

Miscellaneous databases

NextBioi 967302.
PROi Q05788.

Gene expression databases

Genevestigatori Q05788.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
InterProi IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000477. PurNPase. 1 hit.
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 125 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