ID   KPRH_STRCO              Reviewed;         317 AA.
AC   Q9EWS0;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative ribose-phosphate pyrophosphokinase;
DE            Short=RPPK;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase;
DE            Short=P-Rib-PP synthase;
DE            Short=PRPP synthase;
GN   OrderedLocusNames=SCO0782; ORFNames=3SCF60.14c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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;
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This protein has lost two of the potential magnesium binding
CC       sites found in 5-phosphoribose 1-diphosphate synthases. It is also
CC       divergent from other prokaryotic member of the family. It may therefore
CC       have acquired another function. {ECO:0000305}.
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DR   EMBL; AL939106; CAC14347.1; -; Genomic_DNA.
DR   RefSeq; NP_625084.1; NC_003888.3.
DR   RefSeq; WP_011027351.1; NZ_VNID01000004.1.
DR   AlphaFoldDB; Q9EWS0; -.
DR   SMR; Q9EWS0; -.
DR   STRING; 100226.SCO0782; -.
DR   GeneID; 1096205; -.
DR   KEGG; sco:SCO0782; -.
DR   PATRIC; fig|100226.15.peg.774; -.
DR   eggNOG; COG0462; Bacteria.
DR   HOGENOM; CLU_033546_2_0_11; -.
DR   InParanoid; Q9EWS0; -.
DR   OMA; HYAYARS; -.
DR   PhylomeDB; Q9EWS0; -.
DR   Proteomes; UP000001973; 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:InterPro.
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   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..317
FT                   /note="Putative ribose-phosphate pyrophosphokinase"
FT                   /id="PRO_0000141232"
FT   REGION          211..224
FT                   /note="Binding of phosphoribosylpyrophosphate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   317 AA;  33959 MW;  BB117B7399811204 CRC64;
     MRDIAVFSGS AHPDLAEEVC AQLGVPLSPT RVSRFANDCL EVQLMANCRE RDVFLVQPLV
     TPVQEHLVEL LMMCDAARGA SAGRITVVMP HYSYARSDKK DAPRISLGGR LVADLLVAAG
     ASRVLAMTLH SPQVHGFFSV PVDHLHALRE LAAHFRQYDL SRATVVSPDL GNAKEAAAFA
     RMLGAQVAAG AKQRYADDRV SISSVIGDVA GRDVIVLDDE IAKGSTVLEL LDRLRESGPR
     TIRLACTHGL FAAGALGRLS EQPDVLEIVC TNTVPVPADD HTDKLRILSI APALAEAVRR
     IHNGESVSAL FDARPAG