ID   K7RV53_PROA4            Unreviewed;       322 AA.
AC   K7RV53;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   16-OCT-2013, entry version 7.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase;
DE            Short=RPPK;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase;
GN   Name=prs; ORFNames=PACID_09940;
OS   Propionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM
OS   6432 / NBRC 12425 / NCIMB 8070).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Propionibacterineae; Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1171373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070;
RX   PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA   Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F.,
RA   Queiroz V.L., Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P.,
RA   Rincones J., Pereira G.A.;
RT   "The genome sequence of Propionibacterium acidipropionici provides
RT   insights into its biotechnological and industrial potential.";
RL   BMC Genomics 13:562-562(2012).
CC   -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho-
CC       alpha-D-ribose 1-diphosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family.
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DR   EMBL; CP003493; AFV88828.1; -; Genomic_DNA.
DR   RefSeq; YP_006980183.1; NC_019395.1.
DR   GeneID; 13948839; -.
DR   KEGG; pbo:PACID_09940; -.
DR   KO; K00948; -.
DR   UniPathway; UPA00087; UER00172.
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   HAMAP; MF_00583_B; RibP_PPkinase_B; 1; -.
DR   InterPro; IPR000842; PRib_PP_synth_CS.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW   Transferase.
FT   REGION      222    235       5-phosphoribose 1-diphosphate binding (By
FT                                similarity).
FT   METAL       136    136       Magnesium (By similarity).
FT   METAL       138    138       Magnesium (By similarity).
FT   METAL       147    147       Magnesium (By similarity).
FT   METAL       151    151       Magnesium (By similarity).
SQ   SEQUENCE   322 AA;  35018 MW;  2BD26BECC263B671 CRC64;
     MSGATRPNNK HLMLCSGRAY PELAEEIGKE LGVELVPSRQ VTYANSEIYV QFEESVRGCD
     AFVVQSHCAP VNEAMMEQLI MVDALKRASA KRITVVAPFY PYARQDKKHL GREPISARLM
     ADLFTAAGAD RIMAVDLHAA QIQGFFDGPV DHLWALPVLS DYVKDKYGQE DIVVVSPDAG
     RVRLADQWTD KLGCQLAIIH KRRDPNKANE ATTHEVVGKV KGKTCILVDD MIDTAGTICQ
     AAKALEDHGA TKVIAAATHP VLSGPAADRI NASPIQELVV TNTLQVPDGV EIPKMTVLSI
     APLIAKAIQQ VFEDGSVAQL FR
//