Ribose-phosphate pyrophosphokinase 5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q12265 (KPR5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribose-phosphate pyrophosphokinase 5
EC=2.7.6.1

Alternative name(s):
Phosphoribosyl pyrophosphate synthase 5

Gene names

Name:	PRS5
Synonyms:	PRPS5
Ordered Locus Names:	YOL061W
ORF Names:	O1213

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4 Ref.5 Ref.9
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.4 Ref.5 Ref.9
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.
Miscellaneous	Present with 3310 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the ribose-phosphate pyrophosphokinase family.

Ontologies

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

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRS2	P38620	4	EBI-9886,EBI-9873

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 496

496

Ribose-phosphate pyrophosphokinase 5

PRO_0000141090

Sites

Metal binding

242

Magnesium Potential

Metal binding

244

Magnesium Potential

Metal binding

253

Magnesium Potential

Metal binding

257

Magnesium Potential

Amino acid modifications

Modified residue

119

Phosphotyrosine Ref.11

Modified residue

120

Phosphothreonine Ref.11

Modified residue

123

Phosphoserine Ref.11 Ref.13 Ref.14

Modified residue

127

Phosphothreonine Ref.11 Ref.13 Ref.14

Modified residue

154

Phosphothreonine Ref.14

Modified residue

165

Phosphothreonine Ref.14

Modified residue

183

Phosphoserine Ref.10 Ref.12

Modified residue

185

Phosphoserine Ref.12

Modified residue

328

Phosphoserine Ref.14

Modified residue

332

Phosphoserine Ref.14

Modified residue

364

Phosphoserine Ref.6

Modified residue

367

Phosphoserine Ref.6

Modified residue

369

Phosphoserine Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

Q12265 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 75C948D40D58256D
Show »

FASTA

496

53,505

        10         20         30         40         50         60 
MSMSNIVVFG GDSHPELVTK ICENLDIHPS KVELGKFSNG ETNIALRESV REKDVYIIQS 

        70         80         90        100        110        120 
GCGQVNDTFM QLLILISACK SASASRVTAV MPYLCYSRQP DIPYTAKGAP IISKPKENYT 

       130        140        150        160        170        180 
FESHPGTPVS SSLMTQRPGA ESSLKSLDSA IRSTINLENP QPIRTPNSSA TANNNFDIKK 

       190        200        210        220        230        240 
TLSFSRIPMI PGGKLQNTSN STDAGELFNA QNAGYKLWVV QAGTLIAHLL SAAGADHVIT 

       250        260        270        280        290        300 
MDLHDPQFPG FFDIPVDNLY CKPIAQNYIQ HRIPDYQDAV IVSPDAGGAK RATAIADALE 

       310        320        330        340        350        360 
LSFALIHKER RSQLLKGPPD ATLTSGGSLP VSPRPLVTTL VSSQNTTSSG ATGVAALEMK 

       370        380        390        400        410        420 
KTTSTSSTSS QSSNSSKFVQ TTMLVGDVRN KVCIIVDDLV DTSYTITRAA KLLKDQGSTK 

       430        440        450        460        470        480 
VYALITHGVF SGDALERIGQ SSIDKLIISN TVPQDRTLQY LGKDRVDVID VSCIIGEAIR 

       490 
RIHNGESISM LFEHGW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of a 26 kb region on the left arm of yeast chromosome XV." Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H. Yeast 12:67-76(1996) [PubMed: 8789261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 90843 / S288c / FY73.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"PRS5, the fifth member of the phosphoribosyl pyrophosphate synthetase gene family in Saccharomyces cerevisiae, is essential for cell viability in the absence of either PRS1 or PRS3." Hernando Y., Parr A., Schweizer M. J. Bacteriol. 180:6404-6407(1998) [PubMed: 9829955] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
[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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364; SER-367 AND SER-369, MASS SPECTROMETRY. Strain: 2124.
[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]	"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].
[9]	"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.
[10]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, MASS SPECTROMETRY. Strain: YAL6B.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-119; THR-120; SER-123 AND THR-127, MASS SPECTROMETRY. Strain: ADR376.
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-185, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND THR-127, MASS SPECTROMETRY.
[14]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; THR-127; THR-154; THR-165; SER-328 AND SER-332, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z74803 Genomic DNA. Translation: CAA99070.1. X91067 Genomic DNA. Translation: CAA62523.1. BK006948 Genomic DNA. Translation: DAA10722.1.
PIR	S61716.
RefSeq	NP_014580.1. NM_001183316.1.
3D structure databases
ProteinModelPortal	Q12265.
SMR	Q12265. Positions 5-495.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1532N.
IntAct	Q12265. 10 interactions.
MINT	MINT-404255.
STRING	Q12265.
Proteomic databases
PeptideAtlas	Q12265.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOL061W; YOL061W; YOL061W.
GeneID	854093.
KEGG	sce:YOL061W.
NMPDR	fig\|4932.3.peg.5672.
Organism-specific databases
CYGD	YOL061w.
SGD	S000005422. PRS5.
Phylogenomic databases
eggNOG	fuNOG07610.
GeneTree	EFGT00050000003657.
HOGENOM	HBG519284.
OMA	CIMISAC.
OrthoDB	EOG4CG3HW.
Gene expression databases
ArrayExpress	Q12265.
Genevestigator	Q12265.
GermOnline	YOL061W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase. [Graphical view]
KO	K00948.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	975752.

Entry information

Entry name

KPR5_YEAST

Accession

Primary (citable) accession number: Q12265
Secondary accession number(s): D6W206

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents