KPRS_SALTY
ID KPRS_SALTY Reviewed; 315 AA.
AC P0A1V6; P15849;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583};
DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:4306285, ECO:0000305|PubMed:4324215, ECO:0000305|PubMed:4346344, ECO:0000305|PubMed:6277896};
DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:4306285};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:4306285};
DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:4306285};
DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:4306285};
DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:4306285};
GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583};
GN Synonyms=prsA {ECO:0000303|PubMed:2838463}; OrderedLocusNames=STM1780;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2838463; DOI=10.1128/jb.170.7.3243-3248.1988;
RA Bower S.G., Hove-Jensen B., Switzer R.L.;
RT "Structure of the gene encoding phosphoribosylpyrophosphate synthetase
RT (prsA) in Salmonella typhimurium.";
RL J. Bacteriol. 170:3243-3248(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RC STRAIN=LT2;
RX PubMed=4306285; DOI=10.1016/s0021-9258(18)91705-9;
RA Switzer R.L.;
RT "Regulation and mechanism of phosphoribosylpyrophosphate synthetase. I.
RT Purification and properties of the enzyme from Salmonella typhimurium.";
RL J. Biol. Chem. 244:2854-2863(1969).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RX PubMed=4324215; DOI=10.1016/s0021-9258(18)62308-7;
RA Switzer R.L.;
RT "Regulation and mechanism of phosphoribosylpyrophosphate synthetase. 3.
RT Kinetic studies of the reaction mechanism.";
RL J. Biol. Chem. 246:2447-2458(1971).
RN [5]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=4346344; DOI=10.1016/s0021-9258(19)44371-8;
RA Switzer R.L., Sogin D.C.;
RT "Regulation and mechanism of phosphoribosylpyrophosphate synthetase. V.
RT Inhibition by end products and regulation by adenosine diphosphate.";
RL J. Biol. Chem. 248:1063-1073(1973).
RN [6]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=6277896; DOI=10.1016/s0021-9258(18)34935-4;
RA Gibson K.J., Schubert K.R., Switzer R.L.;
RT "Binding of the substrates and the allosteric inhibitor adenosine 5'-
RT diphosphate to phosphoribosylpyrophosphate synthetase from Salmonella
RT typhimurium.";
RL J. Biol. Chem. 257:2391-2396(1982).
CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC 5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:4306285,
CC ECO:0000269|PubMed:4324215, ECO:0000305|PubMed:2838463}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00583, ECO:0000305|PubMed:4306285,
CC ECO:0000305|PubMed:4324215, ECO:0000305|PubMed:4346344,
CC ECO:0000305|PubMed:6277896};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000269|PubMed:4306285, ECO:0000269|PubMed:4324215};
CC Note=Binds 2 Mg(2+) ions per subunit (Potential). Can also use Mn(2+)
CC ions (PubMed:4306285). {ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000269|PubMed:4306285};
CC -!- ACTIVITY REGULATION: Activated by inorganic phosphate (PubMed:4306285,
CC PubMed:4324215). In addition to form a complex with ATP, Mg(2+) also
CC acts as a cofactor (PubMed:4306285, PubMed:4324215). Strongly inhibited
CC by ADP (or Mg-ADP) through competitive binding at the activation site
CC and at a specific allosteric site (PubMed:4324215, PubMed:4346344,
CC PubMed:6277896). Competitively inhibited by Ca(2+) (PubMed:4324215,
CC PubMed:4346344). {ECO:0000269|PubMed:4306285,
CC ECO:0000269|PubMed:4324215, ECO:0000269|PubMed:4346344,
CC ECO:0000269|PubMed:6277896}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=46 uM for ATP {ECO:0000269|PubMed:4324215};
CC KM=160 uM for Rib-5-P {ECO:0000269|PubMed:4324215};
CC pH dependence:
CC Optimum pH is 8.1-8.6. {ECO:0000269|PubMed:4306285};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00583}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- MISCELLANEOUS: This enzyme uses a steady state ordered mechanism, where
CC Mg(2+) binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.
CC {ECO:0000269|PubMed:4324215}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583}.
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DR EMBL; M19488; AAA27196.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20695.1; -; Genomic_DNA.
DR PIR; A30408; KIEBRT.
DR RefSeq; NP_460736.1; NC_003197.2.
DR RefSeq; WP_001518537.1; NC_003197.2.
DR AlphaFoldDB; P0A1V6; -.
DR SMR; P0A1V6; -.
DR STRING; 99287.STM1780; -.
DR PaxDb; P0A1V6; -.
DR PRIDE; P0A1V6; -.
DR EnsemblBacteria; AAL20695; AAL20695; STM1780.
DR GeneID; 1253299; -.
DR GeneID; 58320329; -.
DR GeneID; 64169977; -.
DR GeneID; 67515638; -.
DR KEGG; stm:STM1780; -.
DR PATRIC; fig|99287.12.peg.1877; -.
DR HOGENOM; CLU_033546_2_0_6; -.
DR OMA; FGWARQD; -.
DR PhylomeDB; P0A1V6; -.
DR BioCyc; SENT99287:STM1780-MON; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
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:UniProtKB-UniRule.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
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:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
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 InterPro; IPR037515; Rib-P_diPkinase_bac.
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 Allosteric enzyme; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0A717"
FT CHAIN 2..315
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000141184"
FT ACT_SITE 194
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 37..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 96..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 196
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 220
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 224..228
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
SQ SEQUENCE 315 AA; 34216 MW; 4F8E29B118FD6665 CRC64;
MPDMKLFAGN ATPELAQRIA NRLYTSLGDA AVGRFSDGEV SVQINENVRG GDIFIIQSTC
APTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR VRSARVPITA KVVADFLSSV
GVDRVLTVDL HAEQIQGFFD VPVDNVFGSP ILLEDMLQLN LDNPIVVSPD IGGVVRARAI
AKLLNDTDMA IIDKRRPRAN VSQVMHIIGD VAGRDCVLVD DMIDTGGTLC KAAEALKERG
AKRVFAYATH PIFSGNAANN LRNSVIDEVV VCDTIPLTDE IKALPNVRTL TLSGMLAEAI
RRISNEESIS AMFEH
