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P38063 (KPR4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribose-phosphate pyrophosphokinase 4

EC=2.7.6.1
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 4
Gene names
Name:PRS4
Synonyms:PRPS4
Ordered Locus Names:YBL068W
ORF Names:YBL0619
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (PRS2, PRS3, PRS4 and PRS5). Ref.1 Ref.4

Catalytic activity

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.1 Ref.4

Pathway

Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.

Subcellular location

Cytoplasm Ref.6.

Miscellaneous

Present with 5280 molecules/cell in log phase SD medium. Ref.7

Sequence similarities

Belongs to the ribose-phosphate pyrophosphokinase family.

Sequence caution

The sequence CAA84888.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAC04170.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 326326Ribose-phosphate pyrophosphokinase 4
PRO_0000141089

Sites

Metal binding1401Magnesium Potential
Metal binding1421Magnesium Potential
Metal binding1511Magnesium Potential
Metal binding1551Magnesium Potential

Experimental info

Sequence conflict901K → Q in CAA84888. Ref.2
Sequence conflict1691T → AR in CAA84888. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P38063 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: B6335D5F1AB1A93C

FASTA32635,720
        10         20         30         40         50         60 
MNSESREDMA INSIKLLAGN SHPDLAEQIS KKLGIPLSKV GVYQYSNKET SVTIGESLRD 

        70         80         90        100        110        120 
EDVYIIQTGI GEQEINDFLM ELLILIHACK IASARKITTV IPNFPYARQD KKDKSRAPIT 

       130        140        150        160        170        180 
AKLVANLLQT AGADHVITMD LHASQIQGFF HIPVDNLYAE PSVLNYIRTK TDFDNAILVS 

       190        200        210        220        230        240 
PDAGGAKRVA ALADKLDLNF ALIHKERQKA NEVSKMVLVG DVTNKSCLLV DDMADTCGTL 

       250        260        270        280        290        300 
VKACDTLMEH GAKEVIAIVT HGIFSGSARE KLRNSRLSRI VCTNTVPVDL DLPIADQIDI 

       310        320 
SPTFAEAIRR LHNGESVSYL FTHAPV 

« Hide

References

« Hide 'large scale' references
[1]"Heterooligomeric phosphoribosyl diphosphate synthase of Saccharomyces cerevisiae: combinatorial expression of the five PRS genes in Escherichia coli."
Hove-Jensen B.
J. Biol. Chem. 279:40345-40350(2004) [PubMed: 15280369] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME ACTIVITY.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 90 AND 169.
Strain: ATCC 204508 / S288c.
[4]"Genetic analysis and enzyme activity suggest the existence of more than one minimal functional unit capable of synthesizing phosphoribosyl pyrophosphate in Saccharomyces cerevisiae."
Hernando Y., Carter A.T., Parr A., Hove-Jensen B., Schweizer M.
J. Biol. Chem. 274:12480-12487(1999) [PubMed: 10212224] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY.
[5]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed: 12748633] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[6]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ245726 Genomic DNA. Translation: CAC04170.1. Different initiation.
Z35829 Genomic DNA. Translation: CAA84888.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07053.2.
PIRS45804.
RefSeqNP_009485.3. NM_001178308.2.

3D structure databases

ProteinModelPortalP38063.
SMRP38063. Positions 13-321.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3945N.
IntActP38063. 4 interactions.
MINTMINT-529341.
STRINGP38063.

Proteomic databases

PeptideAtlasP38063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID852211.
KEGGsce:YBL068W.
NMPDRfig|4932.3.peg.174.

Organism-specific databases

CYGDYBL068w.
SGDS000000164. PRS4.

Phylogenomic databases

eggNOGfuNOG04549.
GeneTreeEFGT00050000003657.
HOGENOMHBG519284.
OMATGREPIS.
OrthoDBEOG4J9R7P.

Gene expression databases

ArrayExpressP38063.
GenevestigatorP38063.
GermOnlineYBL068W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000842. PRib_PP_synth_CS.
IPR000836. PRibTrfase.
IPR005946. Rib-P_diPkinase.
[Graphical view]
KOK00948.
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01251. RibP_PPkin. 1 hit.
PROSITEPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970715.

Entry information

Entry nameKPR4_YEAST
AccessionPrimary (citable) accession number: P38063
Secondary accession number(s): D6VPT3, Q9HGQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families