KPRS_THEKO
ID KPRS_THEKO Reviewed; 280 AA.
AC O52958;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|Ref.1};
DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|Ref.1};
DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref.1};
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};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583};
GN Synonyms=Pk-rppk {ECO:0000303|Ref.1}; OrderedLocusNames=TK2235;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RA Rashid N., Morikawa M., Imanaka T.;
RT "Gene cloning and characterization of recombinant ribose phosphate
RT pyrophosphokinase from a hyperthermophilic archaeon.";
RL J. Ferment. Bioeng. 83:412-418(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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). It can also use CTP and GTP as substrates in addition to ATP.
CC {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|Ref.1}.
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:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00583};
CC -!- ACTIVITY REGULATION: Activated by Co(2+) and Ni(2+) ions, however
CC Mg(2+) ion shows almost no significant effect on the activity. Equally
CC inhibited by ADP, CTP and GTP, while dTTP and UTP are less inhibitory.
CC {ECO:0000269|Ref.1}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Half-life of the enzyme
CC activity is 55 minutes at 70 degrees Celsius. {ECO:0000269|Ref.1};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class III (archaeal) subfamily. {ECO:0000255|HAMAP-Rule:MF_00583}.
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DR EMBL; D78364; BAA24158.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD86424.1; -; Genomic_DNA.
DR RefSeq; WP_011251185.1; NC_006624.1.
DR AlphaFoldDB; O52958; -.
DR SMR; O52958; -.
DR STRING; 69014.TK2235; -.
DR EnsemblBacteria; BAD86424; BAD86424; TK2235.
DR GeneID; 3235508; -.
DR KEGG; tko:TK2235; -.
DR PATRIC; fig|69014.16.peg.2190; -.
DR eggNOG; arCOG00067; Archaea.
DR HOGENOM; CLU_033546_2_2_2; -.
DR InParanoid; O52958; -.
DR OMA; FGWARQD; -.
DR OrthoDB; 59314at2157; -.
DR PhylomeDB; O52958; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000000536; 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_A; RibP_PPkinase_A; 1.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037514; Rib-P_diPkinase_arc.
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.
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..280
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000141246"
FT ACT_SITE 183
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 32..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 89..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 185
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 209
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 213..217
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
SQ SEQUENCE 280 AA; 31135 MW; 0117A9BD0E1DFF02 CRC64;
MFLLGSGGKH FEDELRNAGA KILEVEIKRF PDGEKYVRVM GNGDEATVVS STFYPQDEKI
VELLLLGDAL REKGFEKLKL VVPYFAYSRQ DRVTKDGEPI SVRAVMRALG IYYEELYIFD
THNPETLRFF PGKAVNVSPA RVIGEYFREK LGDGLVLAPD KGALERARAV AEVLGLEYSH
FEKRRISPTE VEMHPVDVDV KGKNVLIVDD IISTGGTMVR AAELLRKLGA KKIYVSATHG
VFAEGAIERV SRAVDELAVT NTIPTPVSRI SIVPELLKLE
