Ribose-phosphate pyrophosphokinase 2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P38620 (KPR2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 101. History...

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

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

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 2
EC=2.7.6.1

Alternative name(s):
Phosphoribosyl pyrophosphate synthase 2

Gene names

Name:	PRS2
Synonyms:	PRPS2, PRS
Ordered Locus Names:	YER099C

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	318 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.3 Ref.7
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.3 Ref.7
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 8120 molecules/cell in log phase SD medium. Ref.9
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Inferred from mutant phenotype Ref.7. 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.8. 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
PRS1	P32895	3	EBI-9873,EBI-9869
PRS5	Q12265	4	EBI-9873,EBI-9886

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 318

318

Ribose-phosphate pyrophosphokinase 2

PRO_0000141087

Sites

Metal binding

132

Magnesium Potential

Metal binding

134

Magnesium Potential

Metal binding

143

Magnesium Potential

Metal binding

147

Magnesium Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P38620 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 8B970E98084F5D71
Show »

FASTA

318

34,765

        10         20         30         40         50         60 
MSTNSIKLLA GNSHPGLAEL ISQRLGVPLS KVGVYQYSNK ETSVTIGESI RDEDVYIIQT 

        70         80         90        100        110        120 
GYGEHEINDF LMELLILIHA CKTASVRRIT AVIPNFPYAR QDKKDKSRAP ITAKLIANLL 

       130        140        150        160        170        180 
ETAGCDHVIT MDLHASQIQG FFHIPVDNLY GEPSVLNYIR TKTDFNNAIL VSPDAGGAKR 

       190        200        210        220        230        240 
VASLADKLDM NFALIHKERQ KANEVSRMLL VGDVAGKSCL LIDDMADTCG TLVKACDTLM 

       250        260        270        280        290        300 
DHGAKEVIAI VTHGIFSGSA REKLINSRLS RIVCTNTVPV DLDLDIVDQV DISPTIAEAI 

       310 
RRLHNGESVS YLFTHAPV

« Hide

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]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME ACTIVITY.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"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.
[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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74414 Genomic DNA. Translation: CAA52436.1. X75075 Genomic DNA. Translation: CAA52969.1. U18839 Genomic DNA. Translation: AAB64654.1. AY692977 Genomic DNA. Translation: AAT92996.1. BK006939 Genomic DNA. Translation: DAA07760.1.
PIR	S37225.
RefSeq	NP_011025.1. NM_001178990.1.
3D structure databases
ProteinModelPortal	P38620.
SMR	P38620. Positions 5-313.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1482N.
IntAct	P38620. 7 interactions.
MINT	MINT-404277.
STRING	P38620.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER099C; YER099C; YER099C.
GeneID	856836.
KEGG	sce:YER099C.
NMPDR	fig\|4932.3.peg.2100.
Organism-specific databases
CYGD	YER099c.
SGD	S000000901. PRS2.
Phylogenomic databases
eggNOG	fuNOG04549.
GeneTree	EFGT00050000003657.
HOGENOM	HBG519284.
OMA	HQGREPI.
OrthoDB	EOG4J9R7P.
Gene expression databases
ArrayExpress	P38620.
Genevestigator	P38620.
GermOnline	YER099C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000842. PRib_PP_synth_CS. IPR000836. PRibTrfase. IPR005946. Rib-P_diPkinase. [Graphical view]
KO	K00948.
Pfam	PF00156. Pribosyltran. 1 hit. [Graphical view]
TIGRFAMs	TIGR01251. RibP_PPkin. 1 hit.
PROSITE	PS00114. PRPP_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	983141.

Entry information

Entry name

KPR2_YEAST

Accession

Primary (citable) accession number: P38620
Secondary accession number(s): D3DM06

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	December 14, 2011
This is version 101 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

Yeast chromosome V

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

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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