KPR1_YEAST
ID KPR1_YEAST Reviewed; 427 AA.
AC P32895; D6VX20;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 1;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1;
GN Name=PRS1; Synonyms=PPS1, PRP1, PRPS, PRPS1; OrderedLocusNames=YKL181W;
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].
RX PubMed=8007970; DOI=10.1128/mcb.14.7.4671-4681.1994;
RA Blacketer M.J., Madaule P., Myers A.M.;
RT "The Saccharomyces cerevisiae mutation elm4-1 facilitates pseudohyphal
RT differentiation and interacts with a deficiency in
RT phosphoribosylpyrophosphate synthase activity to cause constitutive
RT pseudohyphal growth.";
RL Mol. Cell. Biol. 14:4671-4681(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [6]
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 [7]
RP ENZYME ACTIVITY.
RX PubMed=9108276; DOI=10.1007/s004380050402;
RA Carter A.T., Beiche F., Hove-Jensen B., Narbad A., Barker P.J.,
RA Schweizer L.M., Schweizer M.;
RT "PRS1 is a key member of the gene family encoding
RT phosphoribosylpyrophosphate synthetase in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 254:148-156(1997).
RN [8]
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 [9]
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 [10]
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).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-271 AND SER-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 ECO:0000269|PubMed:9108276};
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 P32895; P38689: PRS3; NbExp=5; IntAct=EBI-9869, EBI-9877;
CC P32895; P38063: PRS4; NbExp=4; IntAct=EBI-9869, EBI-9882;
CC P32895; Q12265: PRS5; NbExp=3; IntAct=EBI-9869, EBI-9886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; L04130; AAA21811.1; -; Genomic_DNA.
DR EMBL; X70069; CAA49674.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52257.1; -; Genomic_DNA.
DR EMBL; Z28181; CAA82024.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08986.1; -; Genomic_DNA.
DR PIR; S30558; S30558.
DR RefSeq; NP_012740.1; NM_001179747.1.
DR AlphaFoldDB; P32895; -.
DR SMR; P32895; -.
DR BioGRID; 33941; 55.
DR DIP; DIP-4857N; -.
DR IntAct; P32895; 10.
DR MINT; P32895; -.
DR STRING; 4932.YKL181W; -.
DR iPTMnet; P32895; -.
DR MaxQB; P32895; -.
DR PaxDb; P32895; -.
DR PRIDE; P32895; -.
DR EnsemblFungi; YKL181W_mRNA; YKL181W; YKL181W.
DR GeneID; 853654; -.
DR KEGG; sce:YKL181W; -.
DR SGD; S000001664; PRS1.
DR VEuPathDB; FungiDB:YKL181W; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR HOGENOM; CLU_033546_1_2_1; -.
DR InParanoid; P32895; -.
DR OMA; CKMKKHR; -.
DR BioCyc; YEAST:YKL181W-MON; -.
DR Reactome; R-SCE-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P32895; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32895; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; 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; -; 4.
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; 2.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 2.
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; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..427
FT /note="Ribose-phosphate pyrophosphokinase 1"
FT /id="PRO_0000141086"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 130
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 MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 427 AA; 47047 MW; F3E93ACB25E703FF CRC64;
MRKCKIFVGN SHPELGNMVC QRLGIEPAPC TLKKFANGET SVQIGVSVRD EDVYVIQSGS
PSINDDIMEL LILVSACRGG SARKITAVIP QFPYSKQCKM KRHRGAITAR MLANLLVMAG
ADHVVSMDLH ASQMQGFFTK PVDNLYGGPS LAKWIRENVE DYEDAVVVSK NPGGTKRVTA
LADSLKINFA MIHTDRRRSK DLYSQNKDLQ QLKLRKQSML RKNRPIIRQG DHPNEEENII
LSNGIQTARI RNGHVIGDDE ADDDEDAILE SDSELHSIDG LDSHGLGGTY DAVDSEDEEE
IPVLYREQLI TLVGNVRGRS AIILDDMIDR PGSFISAAEH LVQNCGAKKV YVVATHGIFT
GDCLEELEKS DAIDTIVVTN TYPISGERIA GSKKLVTIDV SPIFAECIRR DHYGESISVL
FDSLAAL
