KPRS2_STRR6
ID KPRS2_STRR6 Reviewed; 319 AA.
AC P65242; Q97QV3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative ribose-phosphate pyrophosphokinase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=RPPK 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl diphosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=P-Rib-PP synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPP synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPPase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
GN Name=prs2 {ECO:0000255|HAMAP-Rule:MF_00583}; Synonyms=prs;
GN OrderedLocusNames=spr1002;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-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}.
CC -!- CAUTION: Part of a set of proteins in which some residues (ACT_SITE,
CC NP_BIND, REGION and BINDING) are not conserved. {ECO:0000255|HAMAP-
CC Rule:MF_00583}.
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DR EMBL; AE007317; AAK99806.1; -; Genomic_DNA.
DR PIR; B97997; B97997.
DR RefSeq; NP_358596.1; NC_003098.1.
DR RefSeq; WP_001283813.1; NC_003098.1.
DR AlphaFoldDB; P65242; -.
DR SMR; P65242; -.
DR STRING; 171101.spr1002; -.
DR EnsemblBacteria; AAK99806; AAK99806; spr1002.
DR GeneID; 60234166; -.
DR GeneID; 66806200; -.
DR KEGG; spr:spr1002; -.
DR PATRIC; fig|171101.6.peg.1090; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_1_0_9; -.
DR OMA; HYAYARS; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000000586; 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; 2.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..319
FT /note="Putative ribose-phosphate pyrophosphokinase 2"
FT /id="PRO_0000141207"
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 BINDING 133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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"
SQ SEQUENCE 319 AA; 35125 MW; D7927EADF6716645 CRC64;
MSDRKNMKLF ALNSNQEIAQ KIAQAVGVPL GKLSSRQFSD GEIQVNIEES VRGYDVYIIQ
STSFPVNNHL MELLIMVDAC VRASAHSINV VLPYFGYARQ DRIACPREPL TAKLVANMLV
KAGVDRILTL DLHAVQVQGF FDIPVDNLFT VPLFAKHYCD KGLLGSDVVV VSPKNSGVKR
ARSLAEYLDA PIAIIDYPQD DATRNEGYII GDVEGKKAIL IDDILNTGRT FSEASKIVER
EGATEIYAVS SHGLFVEGAA ELLDNTNIKE ILVTDSVATK EKTPKNVCYI TASELIGDAI
VRIHERKPVS PLFAYNKKK
