KPR4_YEAST
ID KPR4_YEAST Reviewed; 326 AA.
AC P38063; D6VPT3; Q9HGQ6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 4;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 4;
GN Name=PRS4; Synonyms=PRPS4; OrderedLocusNames=YBL068W; ORFNames=YBL0619;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 90 AND 169.
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 [4]
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 [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
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 [7]
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 -!- INTERACTION:
CC P38063; P32895: PRS1; NbExp=4; IntAct=EBI-9882, EBI-9869;
CC P38063; Q12265: PRS5; NbExp=3; IntAct=EBI-9882, EBI-9886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5280 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 -!- SEQUENCE CAUTION:
CC Sequence=CAA84888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC04170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ245726; CAC04170.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z35829; CAA84888.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07053.2; -; Genomic_DNA.
DR PIR; S45804; S45804.
DR RefSeq; NP_009485.3; NM_001178308.2.
DR AlphaFoldDB; P38063; -.
DR SMR; P38063; -.
DR BioGRID; 32632; 74.
DR DIP; DIP-3945N; -.
DR IntAct; P38063; 5.
DR MINT; P38063; -.
DR STRING; 4932.YBL068W; -.
DR MaxQB; P38063; -.
DR PaxDb; P38063; -.
DR PRIDE; P38063; -.
DR EnsemblFungi; YBL068W_mRNA; YBL068W; YBL068W.
DR GeneID; 852211; -.
DR KEGG; sce:YBL068W; -.
DR SGD; S000000164; PRS4.
DR VEuPathDB; FungiDB:YBL068W; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; P38063; -.
DR OMA; SESCARI; -.
DR BioCyc; YEAST:YBL068W-MON; -.
DR Reactome; R-SCE-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P38063; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38063; 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..326
FT /note="Ribose-phosphate pyrophosphokinase 4"
FT /id="PRO_0000141089"
FT BINDING 140
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 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT CONFLICT 90
FT /note="K -> Q (in Ref. 2; CAA84888)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="T -> AR (in Ref. 2; CAA84888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 35720 MW; B6335D5F1AB1A93C CRC64;
MNSESREDMA INSIKLLAGN SHPDLAEQIS KKLGIPLSKV GVYQYSNKET SVTIGESLRD
EDVYIIQTGI GEQEINDFLM ELLILIHACK IASARKITTV IPNFPYARQD KKDKSRAPIT
AKLVANLLQT AGADHVITMD LHASQIQGFF HIPVDNLYAE PSVLNYIRTK TDFDNAILVS
PDAGGAKRVA ALADKLDLNF ALIHKERQKA NEVSKMVLVG DVTNKSCLLV DDMADTCGTL
VKACDTLMEH GAKEVIAIVT HGIFSGSARE KLRNSRLSRI VCTNTVPVDL DLPIADQIDI
SPTFAEAIRR LHNGESVSYL FTHAPV
