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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: -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)DescriptionActionsGraphical viewLength
Metal bindingi131MagnesiumSequence analysis1
Metal bindingi133MagnesiumSequence analysis1
Metal bindingi142MagnesiumSequence analysis1
Metal bindingi146MagnesiumSequence analysis1

GO - Molecular functioni

GO - Biological processi

  • 5-phosphoribose 1-diphosphate biosynthetic process Source: SGD
  • fungal-type cell wall organization Source: SGD
  • nucleoside metabolic process Source: InterPro
  • nucleotide biosynthetic process Source: UniProtKB-KW
  • ribonucleoside monophosphate biosynthetic process Source: InterPro

Keywordsi

Molecular functionKinase, Transferase
Biological processNucleotide biosynthesis
LigandATP-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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001410881 – 320Ribose-phosphate pyrophosphokinase 3Add BLAST320

Proteomic databases

MaxQBiP38689
PaxDbiP38689
PRIDEiP38689

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRS1P328955EBI-9877,EBI-9869

Protein-protein interaction databases

BioGridi36412, 51 interactors
DIPiDIP-4307N
IntActiP38689, 41 interactors
MINTiP38689
STRINGi4932.YHL011C

Structurei

3D structure databases

ProteinModelPortaliP38689
SMRiP38689
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074583
HOGENOMiHOG000210451
InParanoidiP38689
KOiK00948
OMAiNYSCTYK
OrthoDBiEOG092C2PL8

Family and domain databases

CDDicd06223 PRTases_typeI, 1 hit
InterProiView protein in InterPro
IPR000842 PRib_PP_synth_CS
IPR029099 Pribosyltran_N
IPR000836 PRibTrfase_dom
IPR029057 PRTase-like
IPR005946 Rib-P_diPkinase
PfamiView protein in Pfam
PF14572 Pribosyl_synth, 1 hit
PF13793 Pribosyltran_N, 1 hit
SUPFAMiSSF53271 SSF53271, 1 hit
TIGRFAMsiTIGR01251 ribP_PPkin, 1 hit
PROSITEiView protein in PROSITE
PS00114 PRPP_SYNTHASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiKPR3_YEAST
AccessioniPrimary (citable) accession number: P38689
Secondary accession number(s): D3DKQ2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 157 of the entry and version 1 of the sequence. See 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
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