ID   G5JUA5_9STRE            Unreviewed;       326 AA.
AC   G5JUA5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   13-NOV-2019, entry version 48.
DE   RecName: Full=Putative ribose-phosphate pyrophosphokinase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=RPPK {ECO:0000256|HAMAP-Rule:MF_00583};
DE            EC=2.7.6.1 {ECO:0000256|HAMAP-Rule:MF_00583};
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000256|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=P-Rib-PP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=PRPP synthase {ECO:0000256|HAMAP-Rule:MF_00583};
DE            Short=PRPPase {ECO:0000256|HAMAP-Rule:MF_00583};
GN   Name=prs_1 {ECO:0000313|EMBL:EHJ51729.1};
GN   Synonyms=prs {ECO:0000256|HAMAP-Rule:MF_00583};
GN   ORFNames=STRMA_0646 {ECO:0000313|EMBL:EHJ51729.1};
OS   Streptococcus macacae NCTC 11558.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764298 {ECO:0000313|EMBL:EHJ51729.1, ECO:0000313|Proteomes:UP000003573};
RN   [1] {ECO:0000313|EMBL:EHJ51729.1, ECO:0000313|Proteomes:UP000003573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11558 {ECO:0000313|EMBL:EHJ51729.1,
RC   ECO:0000313|Proteomes:UP000003573};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X.,
RA   Weinstock G.M., Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
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
CC       (Rib-5-P). {ECO:0000256|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,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00583,
CC         ECO:0000256|SAAS:SAAS01115190};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00583};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00583};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
CC       ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
CC       diphosphate from D-ribose 5-phosphate (route I): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000256|SAAS:SAAS00956751}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family. Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CAUTION: Part of a set of proteins in which some residues
CC       (ACT_SITE, NP_BIND, REGION and BINDING) are not conserved.
CC       {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHJ51729.1}.
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DR   EMBL; AEUW02000001; EHJ51729.1; -; Genomic_DNA.
DR   RefSeq; WP_003078873.1; NZ_UHFV01000002.1.
DR   STRING; 764298.STRMA_0646; -.
DR   EnsemblBacteria; EHJ51729; EHJ51729; STRMA_0646.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   OrthoDB; 1011035at2; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000003573; Unassembled WGS sequence.
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:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; 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; 2.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956731};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003573};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956744, ECO:0000313|EMBL:EHJ51729.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956743};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956748};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956760};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956754};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003573};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   ECO:0000256|SAAS:SAAS00956753, ECO:0000313|EMBL:EHJ51729.1}.
FT   DOMAIN       10    126       Pribosyltran_N. {ECO:0000259|Pfam:
FT                                PF13793}.
FT   NP_BIND      43     45       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   NP_BIND     102    103       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      230    234       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       136    136       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     226    226       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   326 AA;  35602 MW;  91DAF21FC9F0BC4A CRC64;
     MLNACSDKQL KLFSLTSNTA IAEKIAEAAG LPLGKLSSRQ FSDGEIMINI EESVRGSDIY
     IIQSTSNPVN DHLWELLIMV DACKRASANS VNVVIPYFGY SRQDRIAAAR EPITAKLVAN
     MLVKAGVDRV LTLDLHTVQV QGFFDIPVDN LFTIPLFAKH YIQQGLFGEE VVVVSPKNSG
     IKRARSLAQY LDAPIAIIDY AQDDDSLREE GYIIGEVEGK KAILIDDILN TGKTFAEASK
     IVERGGATDI YAVASHGLFA GGATEMLQSA PIKDILITDS VCTNEKLPDN VHYLSASKLI
     ADAIIRIQER KPLSPLFAYD RKGDES
//