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Protein

Ribose-phosphate pyrophosphokinase 3

Gene

PRS3

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

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 bindingi131 – 1311MagnesiumSequence analysis
Metal bindingi133 – 1331MagnesiumSequence analysis
Metal bindingi142 – 1421MagnesiumSequence analysis
Metal bindingi146 – 1461MagnesiumSequence 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:YHL011C-MONOMER.
ReactomeiR-SCE-73843. 5-Phosphoribose 1-diphosphate biosynthesis.
UniPathwayiUPA00087; UER00172.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-phosphate pyrophosphokinase 3 (EC:2.7.6.1)
Alternative name(s):
Phosphoribosyl pyrophosphate synthase 3
Gene namesi
Name:PRS3
Synonyms:PRPS3
Ordered Locus Names:YHL011C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHL011C.
SGDiS000001003. PRS3.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells fail to arrest in G1, cells remain budded and a significant fraction has a G2 DNA content. In such conditions, deletion mutants have a disorganized actin cytoskeleton and actin accumulates in one or two intensely staining clumps per cell. Deletion mutants also show defects in ion homeostasis and cell integrity. They fail to grow on medium containing 1.0 M NaCl, 5 mM caffeine or when incubated at 37 degrees Celsius. The caffeine and temperature sensitivity are rescued by supplementing the growth medium with 1.0 M sorbitol.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 320320Ribose-phosphate pyrophosphokinase 3PRO_0000141088Add
BLAST

Proteomic databases

MaxQBiP38689.
PeptideAtlasiP38689.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRS1P328954EBI-9877,EBI-9869

Protein-protein interaction databases

BioGridi36412. 47 interactions.
DIPiDIP-4307N.
IntActiP38689. 37 interactions.
MINTiMINT-501416.

Structurei

3D structure databases

ProteinModelPortaliP38689.
SMRiP38689. Positions 5-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
InParanoidiP38689.
KOiK00948.
OMAiTVPFEDK.
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.

P38689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTNSIKLLA PDVHRGLAEL VAKRLGLQLT SSKLKRDPTG EVSFSIGESV
60 70 80 90 100
RDQDIFIITQ IGSGVVNDRV LELLIMINAS KTASARRITA IIPNFPYARQ
110 120 130 140 150
DRKDKSRAPI TAKLMADMLT TAGCDHVITM DLHASQIQGF FDVPVDNLYA
160 170 180 190 200
EPSVVRYIKE NVNYMDSIII SPDAGGAKRA ATLADRLDLN FALIHKERAR
210 220 230 240 250
ANEVSRMVLV GDVTDKICII VDDMADTCGT LAKAAEILLE NRAKSVIAIV
260 270 280 290 300
THGVLSGRAI ENINNSKLDR VVCTNTVPFE EKIKKCPKLA VIDISSVLAE
310 320
SIRRLHNGES ISYLFKNYPL
Length:320
Mass (Da):35,124
Last modified:February 1, 1995 - v1
Checksum:iD4839D217B7513C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74415 Genomic DNA. Translation: CAA52437.1.
U11582 Genomic DNA. Translation: AAB65063.1.
AY693094 Genomic DNA. Translation: AAT93113.1.
BK006934 Genomic DNA. Translation: DAA06675.1.
PIRiS46824.
RefSeqiNP_011852.1. NM_001179091.1.

Genome annotation databases

EnsemblFungiiYHL011C; YHL011C; YHL011C.
GeneIDi856375.
KEGGisce:YHL011C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74415 Genomic DNA. Translation: CAA52437.1.
U11582 Genomic DNA. Translation: AAB65063.1.
AY693094 Genomic DNA. Translation: AAT93113.1.
BK006934 Genomic DNA. Translation: DAA06675.1.
PIRiS46824.
RefSeqiNP_011852.1. NM_001179091.1.

3D structure databases

ProteinModelPortaliP38689.
SMRiP38689. Positions 5-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36412. 47 interactions.
DIPiDIP-4307N.
IntActiP38689. 37 interactions.
MINTiMINT-501416.

Proteomic databases

MaxQBiP38689.
PeptideAtlasiP38689.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHL011C; YHL011C; YHL011C.
GeneIDi856375.
KEGGisce:YHL011C.

Organism-specific databases

EuPathDBiFungiDB:YHL011C.
SGDiS000001003. PRS3.

Phylogenomic databases

GeneTreeiENSGT00550000074583.
HOGENOMiHOG000210451.
InParanoidiP38689.
KOiK00948.
OMAiTVPFEDK.
OrthoDBiEOG78M0B7.

Enzyme and pathway databases

UniPathwayiUPA00087; UER00172.
BioCyciYEAST:YHL011C-MONOMER.
ReactomeiR-SCE-73843. 5-Phosphoribose 1-diphosphate biosynthesis.

Miscellaneous databases

PROiP38689.

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. "Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in Saccharomyces cerevisiae."
    Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M.
    Yeast 10:1031-1044(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 44827 / SKQ2N.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "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.
  6. "The yeast PRS3 gene is required for cell integrity, cell cycle arrest upon nutrient deprivation, ion homeostasis and the proper organization of the actin cytoskeleton."
    Binley K.M., Radcliffe P.A., Trevethick J., Duffy K.A., Sudbery P.E.
    Yeast 15:1459-1469(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. "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: FUNCTION, ENZYME ACTIVITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKPR3_YEAST
AccessioniPrimary (citable) accession number: P38689
Secondary accession number(s): D3DKQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.