ID   G5JUA5_9STRE            Unreviewed;       326 AA.
AC   G5JUA5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   07-SEP-2016, entry version 30.
DE   RecName: Full=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};
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 ribose 1,5-bisphosphate.
CC       Catalyzes the transfer of pyrophosphoryl group from ATP to ribose-
CC       5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP.
CC       {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC       alpha-D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_00583}.
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family. {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_AEUW02000001.1.
DR   ProteinModelPortal; G5JUA5; -.
DR   STRING; 764298.STRMA_0646; -.
DR   EnsemblBacteria; EHJ51729; EHJ51729; STRMA_0646.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   OrthoDB; POG091H018X; -.
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-HAMAP.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP.
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:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP.
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   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   Complete proteome {ECO:0000313|Proteomes:UP000003573};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00583, ECO:0000313|EMBL:EHJ51729.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00583};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00583,
KW   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    105       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   REGION      227    234       Ribose-5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   METAL       134    134       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       136    136       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       145    145       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   METAL       149    149       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00583}.
FT   BINDING     110    110       Ribose-5-phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     136    136       ATP. {ECO:0000256|HAMAP-Rule:MF_00583}.
FT   BINDING     141    141       ATP. {ECO:0000256|HAMAP-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
//