Reviewed, UniProtKB/Swiss-Prot P38063 (KPR4_YEAST)

Names and origin

Protein names

Recommended name:
    Ribose-phosphate pyrophosphokinase 4
    EC=2.7.6.1
Alternative name(s):
    Phosphoribosyl pyrophosphate synthetase 4

Gene names

Name:	PRS4
Synonyms:	PRPS4
Ordered Locus Names:	YBL068W
ORF Names:	YBL0619

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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.1 Ref.3
Catalytic activity	ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate. Ref.1 Ref.3
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.5.
Miscellaneous	Present with 5280 molecules/cell in log phase SD medium. Ref.6
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
Gene Ontology (GO)
Biological process	5-phosphoribose 1-diphosphate biosynthetic process Ref.1 Ref.3 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.5 Inferred from direct assay. 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: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribose phosphate diphosphokinase activity Ref.1 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRS1	P32895	1	EBI-9882,EBI-9869
PRS2	P38620	1	EBI-9882,EBI-9873
PRS5	Q12265	1	EBI-9882,EBI-9886

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 327	327	Ribose-phosphate pyrophosphokinase 4		PRO_0000141089
Sites
	Metal binding	140	1	Magnesium Potential
	Metal binding	142	1	Magnesium Potential
	Metal binding	151	1	Magnesium Potential
	Metal binding	155	1	Magnesium Potential
Experimental info
	Sequence conflict	90	1	Q → K in CAC04170. Ref.1
	Sequence conflict	169 – 170	2	AR → T in CAC04170. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38063-1 [UniParc]. Last modified September 5, 2006. Version 2. Checksum: CAC5ECEFCD76FF1E	FASTA	327	35,846
	10 20 30 40 50 60 MNSESREDMA INSIKLLAGN SHPDLAEQIS KKLGIPLSKV GVYQYSNKET SVTIGESLRD 70 80 90 100 110 120 EDVYIIQTGI GEQEINDFLM ELLILIHACQ IASARKITTV IPNFPYARQD KKDKSRAPIT 130 140 150 160 170 180 AKLVANLLQT AGADHVITMD LHASQIQGFF HIPVDNLYAE PSVLNYIRAR KTDFDNAILV 190 200 210 220 230 240 SPDAGGAKRV AALADKLDLN FALIHKERQK ANEVSKMVLV GDVTNKSCLL VDDMADTCGT 250 260 270 280 290 300 LVKACDTLME HGAKEVIAIV THGIFSGSAR EKLRNSRLSR IVCTNTVPVD LDLPIADQID 310 320 ISPTFAEAIR RLHNGESVSY LFTHAPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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.
[4]	"Sequencing and comparison of yeast species to identify genes and regulatory elements." Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S. Nature 423:241-254(2003) [PubMed: 12748633] [Abstract] Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[5]	"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].
[6]	"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	AJ245726 Genomic DNA. Translation: CAC04170.1. Different initiation. Z35829 Genomic DNA. Translation: CAA84888.1. Different initiation.
PIR	S45804.
RefSeq	NP_009485.2.
3D structure databases
SMR	P38063. Positions 13-326.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3945N.
IntAct	P38063. 4 interactions.
STRING	P38063.
Proteomic databases
PeptideAtlas	P38063.
PRIDE	P38063.
Genome annotation databases
Ensembl	YBL068W; YBL068W; YBL068W; Saccharomyces cerevisiae. [Genome view]
GeneID	852211.
KEGG	sce:YBL068W.
NMPDR	fig|4932.3.peg.174.
Organism-specific databases
CYGD	YBL068w.
SGD	S000000164. PRS4.
Phylogenomic databases
eggNOG	fuNOG04549.
HOGENOM	HBG519284.
OMA	TGGTMAT.
OrthoDB	EOG9JDJPX.
PhylomeDB	P38063.
Enzyme and pathway databases
BRENDA	2.7.6.1. 250.
Gene expression databases
ArrayExpress	P38063.
Genevestigator	P38063.
GermOnline	YBL068W. 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	970715.

Entry information

Entry name

KPR4_YEAST

Accession

Primary (citable) accession number: P38063
Secondary accession number(s): Q9HGQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	September 5, 2006
Last modified:	February 9, 2010
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)