Ribose-phosphate pyrophosphokinase 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32895 (KPR1_YEAST)

Last modified November 3, 2009. Version 81. History...

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

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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 1
    EC=2.7.6.1
Alternative name(s):
    Phosphoribosyl pyrophosphate synthetase 1

Gene names

Name:	PRS1
Synonyms:	PPS1, PRP1, PRPS, PRPS1
Ordered Locus Names:	YKL181W

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	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.7 Ref.10
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.7 Ref.10 Ref.6
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.8
Miscellaneous	Present with 11700 molecules/cell in log phase SD medium. Ref.9
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
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Ref.7 Ref.10 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 ribonucleoside monophosphate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Ref.8 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.10 Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
itself		1	EBI-9869,EBI-9869
PRS2	P38620	2	EBI-9869,EBI-9873
PRS3	P38689	1	EBI-9869,EBI-9877
PRS4	P38063	1	EBI-9869,EBI-9882
PRS5	Q12265	1	EBI-9869,EBI-9886

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

Ribose-phosphate pyrophosphokinase 1

PRO_0000141086

Sites

Metal binding

128

Magnesium Potential

Metal binding

130

Magnesium Potential

Metal binding

143

Magnesium Potential

Amino acid modifications

Modified residue

199

Phosphoserine Ref.11 Ref.12

Modified residue

218

Phosphoserine Ref.11

Modified residue

271

Phosphoserine Ref.12

Modified residue

277

Phosphoserine Ref.12

Modified residue

290

Phosphotyrosine Ref.12

Modified residue

295

Phosphoserine Ref.12

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Sequences

Sequence

Length

Mass (Da)

Tools

P32895-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: F3E93ACB25E703FF
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FASTA

427

47,047

        10         20         30         40         50         60 
MRKCKIFVGN SHPELGNMVC QRLGIEPAPC TLKKFANGET SVQIGVSVRD EDVYVIQSGS 

        70         80         90        100        110        120 
PSINDDIMEL LILVSACRGG SARKITAVIP QFPYSKQCKM KRHRGAITAR MLANLLVMAG 

       130        140        150        160        170        180 
ADHVVSMDLH ASQMQGFFTK PVDNLYGGPS LAKWIRENVE DYEDAVVVSK NPGGTKRVTA 

       190        200        210        220        230        240 
LADSLKINFA MIHTDRRRSK DLYSQNKDLQ QLKLRKQSML RKNRPIIRQG DHPNEEENII 

       250        260        270        280        290        300 
LSNGIQTARI RNGHVIGDDE ADDDEDAILE SDSELHSIDG LDSHGLGGTY DAVDSEDEEE 

       310        320        330        340        350        360 
IPVLYREQLI TLVGNVRGRS AIILDDMIDR PGSFISAAEH LVQNCGAKKV YVVATHGIFT 

       370        380        390        400        410        420 
GDCLEELEKS DAIDTIVVTN TYPISGERIA GSKKLVTIDV SPIFAECIRR DHYGESISVL 


FDSLAAL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Saccharomyces cerevisiae mutation elm4-1 facilitates pseudohyphal differentiation and interacts with a deficiency in phosphoribosylpyrophosphate synthase activity to cause constitutive pseudohyphal growth." Blacketer M.J., Madaule P., Myers A.M. Mol. Cell. Biol. 14:4671-4681(1994) [PubMed: 8007970] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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 26786 / X2180-1A.
[3]	Erratum Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M. Yeast 11:191-191(1995)
[4]	"Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene." Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W. Yeast 9:1343-1348(1993) [PubMed: 8154185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"PRS1 is a key member of the gene family encoding phosphoribosylpyrophosphate synthetase in Saccharomyces cerevisiae." Carter A.T., Beiche F., Hove-Jensen B., Narbad A., Barker P.J., Schweizer L.M., Schweizer M. Mol. Gen. Genet. 254:148-156(1997) [PubMed: 9108276] [Abstract] Cited for: ENZYME ACTIVITY.
[7]	"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.
[8]	"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].
[9]	"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].
[10]	"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.
[11]	"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-199 AND SER-218, MASS SPECTROMETRY.
[12]	"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-199; SER-271; SER-277; TYR-290 AND SER-295, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	L04130 Genomic DNA. Translation: AAA21811.1. X70069 Genomic DNA. Translation: CAA49674.1. X74151 Genomic DNA. Translation: CAA52257.1. Z28181 Genomic DNA. Translation: CAA82024.1.
PIR	S30558.
RefSeq	NP_012740.1.
3D structure databases
HSSP	HSSP built from PDB template 1DKR based on UniProtKB P14193.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4857N.
IntAct	P32895. 9 interactions.
STRING	P32895.
Proteomic databases
PeptideAtlas	P32895.
PRIDE	P32895.
Genome annotation databases
Ensembl	YKL181W; YKL181W; YKL181W; Saccharomyces cerevisiae. [Genome view]
GeneID	853654.
GenomeReviews	Gene locus YKL181W in contig Y13137_GR.
KEGG	sce:YKL181W.
NMPDR	fig\|4932.3.peg.3718.
Organism-specific databases
CYGD	YKL181w.
SGD	S000001664. PRS1.
Phylogenomic databases
HOGENOM	P32895.
OMA	NDCLEVQ.
Enzyme and pathway databases
BRENDA	2.7.6.1. 250.
Gene expression databases
ArrayExpress	P32895.
Genevestigator	P32895.
GermOnline	YKL181W. 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	974572.

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Entry information

Entry name

KPR1_YEAST

Accession

Primary (citable) accession number: P32895

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 3, 2009
This is version 81 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 XI

Yeast (Saccharomyces cerevisiae) chromosome XI: 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

Amino acid modifications

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