KPR3_YEAST
ID KPR3_YEAST Reviewed; 320 AA.
AC P38689; D3DKQ2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 3;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 3;
GN Name=PRS3; Synonyms=PRPS3; OrderedLocusNames=YHL011C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=7992503; DOI=10.1002/yea.320100805;
RA Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R.,
RA Schweizer M.;
RT "Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in
RT Saccharomyces cerevisiae.";
RL Yeast 10:1031-1044(1994).
RN [2]
RP ERRATUM OF PUBMED:7992503.
RA Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R.,
RA Schweizer M.;
RL Yeast 11:191-191(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=10212224; DOI=10.1074/jbc.274.18.12480;
RA Hernando Y., Carter A.T., Parr A., Hove-Jensen B., Schweizer M.;
RT "Genetic analysis and enzyme activity suggest the existence of more than
RT one minimal functional unit capable of synthesizing phosphoribosyl
RT pyrophosphate in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:12480-12487(1999).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=10514564;
RX DOI=10.1002/(sici)1097-0061(199910)15:14<1459::aid-yea472>3.0.co;2-a;
RA Binley K.M., Radcliffe P.A., Trevethick J., Duffy K.A., Sudbery P.E.;
RT "The yeast PRS3 gene is required for cell integrity, cell cycle arrest upon
RT nutrient deprivation, ion homeostasis and the proper organization of the
RT actin cytoskeleton.";
RL Yeast 15:1459-1469(1999).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP FUNCTION, AND ENZYME ACTIVITY.
RX PubMed=15280369; DOI=10.1074/jbc.m405480200;
RA Hove-Jensen B.;
RT "Heterooligomeric phosphoribosyl diphosphate synthase of Saccharomyces
RT cerevisiae: combinatorial expression of the five PRS genes in Escherichia
RT coli.";
RL J. Biol. Chem. 279:40345-40350(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: 5-phosphoribose 1-diphosphate synthase involved in
CC nucleotide, histidine, and tryptophan biosynthesis. Active in
CC heteromultimeric complexes with other 5-phosphoribose 1-diphosphate
CC synthases (PRS2, PRS3, PRS4 and PRS5). {ECO:0000269|PubMed:10212224,
CC ECO:0000269|PubMed:15280369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC Evidence={ECO:0000269|PubMed:10212224, ECO:0000269|PubMed:15280369};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC -!- INTERACTION:
CC P38689; P32895: PRS1; NbExp=5; IntAct=EBI-9877, EBI-9869;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Cells fail to arrest in G1, cells remain budded
CC and a significant fraction has a G2 DNA content. In such conditions,
CC deletion mutants have a disorganized actin cytoskeleton and actin
CC accumulates in one or two intensely staining clumps per cell. Deletion
CC mutants also show defects in ion homeostasis and cell integrity. They
CC fail to grow on medium containing 1.0 M NaCl, 5 mM caffeine or when
CC incubated at 37 degrees Celsius. The caffeine and temperature
CC sensitivity are rescued by supplementing the growth medium with 1.0 M
CC sorbitol. {ECO:0000269|PubMed:10514564}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; X74415; CAA52437.1; -; Genomic_DNA.
DR EMBL; U11582; AAB65063.1; -; Genomic_DNA.
DR EMBL; AY693094; AAT93113.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06675.1; -; Genomic_DNA.
DR PIR; S46824; S46824.
DR RefSeq; NP_011852.1; NM_001179091.1.
DR AlphaFoldDB; P38689; -.
DR SMR; P38689; -.
DR BioGRID; 36412; 59.
DR DIP; DIP-4307N; -.
DR IntAct; P38689; 41.
DR MINT; P38689; -.
DR STRING; 4932.YHL011C; -.
DR iPTMnet; P38689; -.
DR MaxQB; P38689; -.
DR PaxDb; P38689; -.
DR PRIDE; P38689; -.
DR EnsemblFungi; YHL011C_mRNA; YHL011C; YHL011C.
DR GeneID; 856375; -.
DR KEGG; sce:YHL011C; -.
DR SGD; S000001003; PRS3.
DR VEuPathDB; FungiDB:YHL011C; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; P38689; -.
DR OMA; LLMGTHT; -.
DR BioCyc; YEAST:YHL011C-MON; -.
DR Reactome; R-SCE-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P38689; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38689; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IPI:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..320
FT /note="Ribose-phosphate pyrophosphokinase 3"
FT /id="PRO_0000141088"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 320 AA; 35124 MW; D4839D217B7513C4 CRC64;
MPTNSIKLLA PDVHRGLAEL VAKRLGLQLT SSKLKRDPTG EVSFSIGESV RDQDIFIITQ
IGSGVVNDRV LELLIMINAS KTASARRITA IIPNFPYARQ DRKDKSRAPI TAKLMADMLT
TAGCDHVITM DLHASQIQGF FDVPVDNLYA EPSVVRYIKE NVNYMDSIII SPDAGGAKRA
ATLADRLDLN FALIHKERAR ANEVSRMVLV GDVTDKICII VDDMADTCGT LAKAAEILLE
NRAKSVIAIV THGVLSGRAI ENINNSKLDR VVCTNTVPFE EKIKKCPKLA VIDISSVLAE
SIRRLHNGES ISYLFKNYPL
