KPRS_BURPS
ID KPRS_BURPS Reviewed; 318 AA.
AC Q63XL8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
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};
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 OrderedLocusNames=BPSL0521 {ECO:0000312|EMBL:CAH34511.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH AMP AND SUBSTRATE
RP ANALOGS.
RX PubMed=23382856; DOI=10.1371/journal.pone.0053851;
RA Baugh L., Gallagher L.A., Patrapuvich R., Clifton M.C., Gardberg A.S.,
RA Edwards T.E., Armour B., Begley D.W., Dieterich S.H., Dranow D.M.,
RA Abendroth J., Fairman J.W., Fox D. III, Staker B.L., Phan I., Gillespie A.,
RA Choi R., Nakazawa-Hewitt S., Nguyen M.T., Napuli A., Barrett L.,
RA Buchko G.W., Stacy R., Myler P.J., Stewart L.J., Manoil C.,
RA Van Voorhis W.C.;
RT "Combining functional and structural genomics to sample the essential
RT Burkholderia structome.";
RL PLoS ONE 8:E53851-E53851(2013).
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 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: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
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; BX571965; CAH34511.1; -; Genomic_DNA.
DR RefSeq; WP_004195243.1; NZ_CP009538.1.
DR RefSeq; YP_107147.1; NC_006350.1.
DR PDB; 3DAH; X-ray; 2.30 A; A/B/C=1-318.
DR PDBsum; 3DAH; -.
DR AlphaFoldDB; Q63XL8; -.
DR SMR; Q63XL8; -.
DR STRING; 272560.BPSL0521; -.
DR EnsemblBacteria; CAH34511; CAH34511; BPSL0521.
DR GeneID; 56593812; -.
DR KEGG; bps:BPSL0521; -.
DR PATRIC; fig|272560.51.peg.1126; -.
DR eggNOG; COG0462; Bacteria.
DR OMA; FGWARQD; -.
DR UniPathway; UPA00087; UER00172.
DR EvolutionaryTrace; Q63XL8; -.
DR Proteomes; UP000000605; Chromosome 1.
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_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 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..318
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000441886"
FT ACT_SITE 196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 40..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 99..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:23382856, ECO:0007744|PDB:3DAH"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 198
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 222
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 226..230
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000305|PubMed:23382856, ECO:0007744|PDB:3DAH"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:3DAH"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 216..227
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:3DAH"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3DAH"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:3DAH"
SQ SEQUENCE 318 AA; 34211 MW; 610A0423F8988DA7 CRC64;
MSSHDGLMVF TGNANPALAQ EVVKILGIPL GKAMVSRFSD GEIQVEIQEN VRGKDVFVLQ
STCAPTNDNL MELMIMVDAL KRASAGRITA AIPYFGYARQ DRRPRSARVA ISAKVVANML
EIAGVERIIT MDLHADQIQG FFDIPVDNIY ATPILLGDLR KQNYPDLLVV SPDVGGVVRA
RALAKQLNCD LAIIDKRRPK ANVAEVMNII GEVEGRTCVI MDDMVDTAGT LCKAAQVLKE
RGAKQVFAYA THPVLSGGAA DRIAASALDE LVVTDTIPLS AESLACPKIR ALSSAGLLAE
TFSRIRRGDS VMSLFAES
