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Protein

Ribose-phosphate pyrophosphokinase 4

Gene

PRS4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).2 Publications

Catalytic activityi

ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate.2 Publications

Pathwayi: 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I).
Proteins known to be involved in this subpathway in this organism are:
  1. Ribose-phosphate pyrophosphokinase 2 (PRS2), Ribose-phosphate pyrophosphokinase 4 (PRS4), Ribose-phosphate pyrophosphokinase 1 (PRS1), Ribose-phosphate pyrophosphokinase 5 (PRS5), Ribose-phosphate pyrophosphokinase 3 (PRS3)
This subpathway is part of the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I), the pathway 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi140 – 1401MagnesiumSequence analysis
Metal bindingi142 – 1421MagnesiumSequence analysis
Metal bindingi151 – 1511MagnesiumSequence analysis
Metal bindingi155 – 1551MagnesiumSequence analysis

GO - Molecular functioni

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: SGD
  • fungal-type cell wall organization Source: SGD
  • nucleotide biosynthetic process Source: UniProtKB-KW
  • ribonucleoside monophosphate biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YBL068W-MONOMER.
ReactomeiR-SCE-73843. 5-Phosphoribose 1-diphosphate biosynthesis.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 4 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 4
Gene namesi
Name:PRS4
Synonyms:PRPS4
Ordered Locus Names:YBL068W
ORF Names:YBL0619
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL068W.
SGDiS000000164. PRS4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • ribose phosphate diphosphokinase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Ribose-phosphate pyrophosphokinase 4PRO_0000141089Add
BLAST

Proteomic databases

MaxQBiP38063.
PeptideAtlasiP38063.

Interactioni

Protein-protein interaction databases

BioGridi32632. 34 interactions.
DIPiDIP-3945N.
IntActiP38063. 4 interactions.
MINTiMINT-529341.

Structurei

3D structure databases

ProteinModelPortaliP38063.
SMRiP38063. Positions 13-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
InParanoidiP38063.
KOiK00948.
OMAiKLDVNFA.
OrthoDBiEOG78M0B7.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSESREDMA INSIKLLAGN SHPDLAEQIS KKLGIPLSKV GVYQYSNKET
60 70 80 90 100
SVTIGESLRD EDVYIIQTGI GEQEINDFLM ELLILIHACK IASARKITTV
110 120 130 140 150
IPNFPYARQD KKDKSRAPIT AKLVANLLQT AGADHVITMD LHASQIQGFF
160 170 180 190 200
HIPVDNLYAE PSVLNYIRTK TDFDNAILVS PDAGGAKRVA ALADKLDLNF
210 220 230 240 250
ALIHKERQKA NEVSKMVLVG DVTNKSCLLV DDMADTCGTL VKACDTLMEH
260 270 280 290 300
GAKEVIAIVT HGIFSGSARE KLRNSRLSRI VCTNTVPVDL DLPIADQIDI
310 320
SPTFAEAIRR LHNGESVSYL FTHAPV
Length:326
Mass (Da):35,720
Last modified:July 27, 2011 - v3
Checksum:iB6335D5F1AB1A93C
GO

Sequence cautioni

The sequence CAA84888.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC04170.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901K → Q in CAA84888 (PubMed:7813418).Curated
Sequence conflicti169 – 1691T → AR in CAA84888 (PubMed:7813418).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245726 Genomic DNA. Translation: CAC04170.1. Different initiation.
Z35829 Genomic DNA. Translation: CAA84888.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07053.2.
PIRiS45804.
RefSeqiNP_009485.3. NM_001178308.2.

Genome annotation databases

EnsemblFungiiYBL068W; YBL068W; YBL068W.
GeneIDi852211.
KEGGisce:YBL068W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245726 Genomic DNA. Translation: CAC04170.1. Different initiation.
Z35829 Genomic DNA. Translation: CAA84888.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07053.2.
PIRiS45804.
RefSeqiNP_009485.3. NM_001178308.2.

3D structure databases

ProteinModelPortaliP38063.
SMRiP38063. Positions 13-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32632. 34 interactions.
DIPiDIP-3945N.
IntActiP38063. 4 interactions.
MINTiMINT-529341.

Proteomic databases

MaxQBiP38063.
PeptideAtlasiP38063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL068W; YBL068W; YBL068W.
GeneIDi852211.
KEGGisce:YBL068W.

Organism-specific databases

EuPathDBiFungiDB:YBL068W.
SGDiS000000164. PRS4.

Phylogenomic databases

GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
InParanoidiP38063.
KOiK00948.
OMAiKLDVNFA.
OrthoDBiEOG78M0B7.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciYEAST:YBL068W-MONOMER.
ReactomeiR-SCE-73843. 5-Phosphoribose 1-diphosphate biosynthesis.

Miscellaneous databases

PROiP38063.

Family and domain databases

Gene3Di3.40.50.2020. 2 hits.
InterProiIPR000842. PRib_PP_synth_CS.
IPR029099. Pribosyltran_N.
IPR029057. PRTase-like.
IPR005946. Rib-P_diPkinase.
[Graphical view]
PfamiPF14572. Pribosyl_synth. 1 hit.
PF13793. Pribosyltran_N. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01251. ribP_PPkin. 1 hit.
PROSITEiPS00114. PRPP_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKPR4_YEAST
AccessioniPrimary (citable) accession number: P38063
Secondary accession number(s): D6VPT3, Q9HGQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5280 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

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 one 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.