KPRS_THEVO
ID KPRS_THEVO Reviewed; 286 AA.
AC Q97CA5;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:21963988};
DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:21963988};
DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583};
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, ECO:0000303|PubMed:21963988};
DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; OrderedLocusNames=TV0197;
GN ORFNames=TVG0201915;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
RN [2]
RP REVIEW, AND COFACTOR.
RX PubMed=28031352; DOI=10.1128/mmbr.00040-16;
RA Hove-Jensen B., Andersen K.R., Kilstrup M., Martinussen J., Switzer R.L.,
RA Willemoes M.;
RT "Phosphoribosyl diphosphate (PRPP): biosynthesis, enzymology, utilization,
RT and metabolic significance.";
RL Microbiol. Mol. Biol. Rev. 81:E00040-E00040(2017).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=21963988; DOI=10.1016/j.jmb.2011.09.007;
RA Cherney M.M., Cherney L.T., Garen C.R., James M.N.;
RT "The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate
RT synthetase bound to ribose-5-phosphate and ATP analogs.";
RL J. Mol. Biol. 413:844-856(2011).
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}.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000303|PubMed:28031352};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00583};
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: Homodimer. {ECO:0000269|PubMed:21963988}.
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,
CC ECO:0000303|PubMed:28031352}.
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DR EMBL; BA000011; BAB59339.1; -; Genomic_DNA.
DR RefSeq; WP_010916453.1; NC_002689.2.
DR PDB; 3LPN; X-ray; 1.80 A; A/B=1-286.
DR PDB; 3LRT; X-ray; 1.53 A; A/B=1-286.
DR PDB; 3MBI; X-ray; 1.80 A; A/B/C/D=1-285.
DR PDB; 3NAG; X-ray; 1.75 A; A/B=1-286.
DR PDBsum; 3LPN; -.
DR PDBsum; 3LRT; -.
DR PDBsum; 3MBI; -.
DR PDBsum; 3NAG; -.
DR AlphaFoldDB; Q97CA5; -.
DR SMR; Q97CA5; -.
DR STRING; 273116.14324411; -.
DR EnsemblBacteria; BAB59339; BAB59339; BAB59339.
DR GeneID; 1441683; -.
DR KEGG; tvo:TVG0201915; -.
DR eggNOG; arCOG00067; Archaea.
DR HOGENOM; CLU_033546_2_2_2; -.
DR OMA; FGWARQD; -.
DR OrthoDB; 59314at2157; -.
DR PhylomeDB; Q97CA5; -.
DR BRENDA; 2.7.6.1; 6326.
DR UniPathway; UPA00087; UER00172.
DR EvolutionaryTrace; Q97CA5; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; PF00156; Pribosyltran; 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 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Transferase.
FT CHAIN 1..286
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000141251"
FT ACT_SITE 184
FT /evidence="ECO:0000305|PubMed:21963988,
FT ECO:0007744|PDB:3MBI"
FT BINDING 34..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3LPN,
FT ECO:0007744|PDB:3LRT, ECO:0007744|PDB:3MBI,
FT ECO:0007744|PDB:3NAG"
FT BINDING 91..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:21963988,
FT ECO:0007744|PDB:3LPN, ECO:0007744|PDB:3LRT,
FT ECO:0007744|PDB:3MBI, ECO:0007744|PDB:3NAG"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000303|PubMed:28031352"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 186
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3MBI"
FT BINDING 210
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3MBI"
FT BINDING 214..218
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3LPN,
FT ECO:0007744|PDB:3LRT, ECO:0007744|PDB:3MBI,
FT ECO:0007744|PDB:3NAG"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3LRT"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 205..215
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:3LRT"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:3LRT"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3LRT"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:3LRT"
SQ SEQUENCE 286 AA; 32177 MW; 2654A6641BAF9B66 CRC64;
MKIIALRSSL KLAARIAEEL KTEPVMPDER RFPDGELYLR YDEDLTGHNI FIIGNTHSDA
EVMEMILTLS AIQDYRTKSV NIIAPYYGYA RQHQRYKNGE PISSQILTEI YSSYSNSIAT
VDIHDEKTLS YSKVKFSDLH ANDAIVRYYK NVDVDYVVSP DDGGLARVAD ISAKLGKKHF
FIEKKRIDDR TVEMKVPNVD VNGKKLLIVD DIISTGGTIA KSSGLLREKG ASKIYVSAVH
GLFVNGSENK ILQNADEIHV TDTVESKFSD ISVYQEVCNY IRDIDA
