KPR2_YEAST
ID KPR2_YEAST Reviewed; 318 AA.
AC P38620; D3DM06;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 2;
GN Name=PRS2; Synonyms=PRPS2, PRS; OrderedLocusNames=YER099C;
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 [GENOMIC DNA], 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [5]
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 [6]
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 [7]
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 [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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8120 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74414; CAA52436.1; -; Genomic_DNA.
DR EMBL; X75075; CAA52969.1; -; Genomic_DNA.
DR EMBL; U18839; AAB64654.1; -; Genomic_DNA.
DR EMBL; AY692977; AAT92996.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07760.1; -; Genomic_DNA.
DR PIR; S37225; S37225.
DR RefSeq; NP_011025.3; NM_001178990.3.
DR AlphaFoldDB; P38620; -.
DR SMR; P38620; -.
DR BioGRID; 36845; 78.
DR DIP; DIP-1482N; -.
DR IntAct; P38620; 5.
DR MINT; P38620; -.
DR STRING; 4932.YER099C; -.
DR iPTMnet; P38620; -.
DR MaxQB; P38620; -.
DR PaxDb; P38620; -.
DR PRIDE; P38620; -.
DR EnsemblFungi; YER099C_mRNA; YER099C; YER099C.
DR GeneID; 856836; -.
DR KEGG; sce:YER099C; -.
DR SGD; S000000901; PRS2.
DR VEuPathDB; FungiDB:YER099C; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; P38620; -.
DR OMA; FGWARQD; -.
DR BioCyc; YEAST:YER099C-MON; -.
DR Reactome; R-SCE-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P38620; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P38620; 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: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..318
FT /note="Ribose-phosphate pyrophosphokinase 2"
FT /id="PRO_0000141087"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 318 AA; 34765 MW; 8B970E98084F5D71 CRC64;
MSTNSIKLLA GNSHPGLAEL ISQRLGVPLS KVGVYQYSNK ETSVTIGESI RDEDVYIIQT
GYGEHEINDF LMELLILIHA CKTASVRRIT AVIPNFPYAR QDKKDKSRAP ITAKLIANLL
ETAGCDHVIT MDLHASQIQG FFHIPVDNLY GEPSVLNYIR TKTDFNNAIL VSPDAGGAKR
VASLADKLDM NFALIHKERQ KANEVSRMLL VGDVAGKSCL LIDDMADTCG TLVKACDTLM
DHGAKEVIAI VTHGIFSGSA REKLINSRLS RIVCTNTVPV DLDLDIVDQV DISPTIAEAI
RRLHNGESVS YLFTHAPV
