Ribose-phosphate pyrophosphokinase 3 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P38689 (KPR3_YEAST)

Last modified February 9, 2010. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ribose-phosphate pyrophosphokinase 3
    EC=2.7.6.1
Alternative name(s):
    Phosphoribosyl pyrophosphate synthetase 3

Gene names

Name:	PRS3
Synonyms:	PRPS3
Ordered Locus Names:	YHL011C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	5-phosphoribose 1-diphosphate synthetase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthetases (PRS2, PRS3, PRS4 and PRS5). Ref.5 Ref.8
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.5 Ref.8
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.7.
Disruption phenotype	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. Ref.6
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.

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Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Ref.5 Ref.8 Inferred from mutant phenotype. Source: SGD fungal-type cell wall organization Inferred from physical interaction. Source: SGD nucleoside metabolic process Inferred from electronic annotation. Source: InterPro regulation of cell size Inferred from mutant phenotype. Source: SGD ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.7 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct kinase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribose phosphate diphosphokinase activity Ref.8 Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-9877,EBI-9877
PRS1	P32895	1	EBI-9877,EBI-9869
PRS5	Q12265	1	EBI-9877,EBI-9886
PTC5	Q12511	1	EBI-9877,EBI-36488

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 320

320

Ribose-phosphate pyrophosphokinase 3

PRO_0000141088

Sites

Metal binding

131

Magnesium Potential

Metal binding

133

Magnesium Potential

Metal binding

142

Magnesium Potential

Metal binding

146

Magnesium Potential

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Sequences

Sequence

Length

Mass (Da)

Tools

P38689-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: D4839D217B7513C4
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FASTA

320

35,124

        10         20         30         40         50         60 
MPTNSIKLLA PDVHRGLAEL VAKRLGLQLT SSKLKRDPTG EVSFSIGESV RDQDIFIITQ 

        70         80         90        100        110        120 
IGSGVVNDRV LELLIMINAS KTASARRITA IIPNFPYARQ DRKDKSRAPI TAKLMADMLT 

       130        140        150        160        170        180 
TAGCDHVITM DLHASQIQGF FDVPVDNLYA EPSVVRYIKE NVNYMDSIII SPDAGGAKRA 

       190        200        210        220        230        240 
ATLADRLDLN FALIHKERAR ANEVSRMVLV GDVTDKICII VDDMADTCGT LAKAAEILLE 

       250        260        270        280        290        300 
NRAKSVIAIV THGVLSGRAI ENINNSKLDR VVCTNTVPFE EKIKKCPKLA VIDISSVLAE 

       310        320 
SIRRLHNGES ISYLFKNYPL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7992503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 44827 / SKQ2N.
[2]	Erratum Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M. Yeast 11:191-191(1995)
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] 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: 10212224] [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: 10514564] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[7]	"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].
[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: 15280369] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X74415 Genomic DNA. Translation: CAA52437.1. U11582 Genomic DNA. Translation: AAB65063.1. AY693094 Genomic DNA. Translation: AAT93113.1.
PIR	S46824.
RefSeq	NP_011852.1.
3D structure databases
SMR	P38689. Positions 6-315.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4307N.
IntAct	P38689. 47 interactions.
STRING	P38689.
Proteomic databases
PeptideAtlas	P38689.
Genome annotation databases
Ensembl	YHL011C; YHL011C; YHL011C; Saccharomyces cerevisiae. [Genome view]
GeneID	856375.
KEGG	sce:YHL011C.
NMPDR	fig\|4932.3.peg.2992.
Organism-specific databases
CYGD	YHL011c.
SGD	S000001003. PRS3.
Phylogenomic databases
eggNOG	fuNOG04549.
HOGENOM	HBG519284.
OMA	LSYYGYA.
OrthoDB	EOG9JDJPX.
PhylomeDB	P38689.
Enzyme and pathway databases
BRENDA	2.7.6.1. 250.
Gene expression databases
ArrayExpress	P38689.
Genevestigator	P38689.
GermOnline	YHL011C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000842. PRib-PP_synthetase_CS. IPR000836. PRibTrfase. IPR005946. PRPP_kinase. [Graphical view]
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. ribP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHETASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	981861.

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Entry information

Entry name

KPR3_YEAST

Accession

Primary (citable) accession number: P38689

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	February 9, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome VIII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents