ID   B0SKG4_LEPBP            Unreviewed;       313 AA.
AC   B0SKG4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   16-OCT-2013, entry version 46.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase;
DE            Short=RPPK;
DE            EC=2.7.6.1;
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase;
GN   Name=prs; OrderedLocusNames=LEPBI_I0236;
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 /
OS   Paris).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=456481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C.,
RA   McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z.,
RA   Coppel R.L., Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome Sequence of the Saprophyte Leptospira biflexa Provides
RT   Insights into the Evolution of Leptospira and the Pathogenesis of
RT   Leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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; CP000786; ABZ96381.1; -; Genomic_DNA.
DR   RefSeq; YP_001837657.1; NC_010602.1.
DR   ProteinModelPortal; B0SKG4; -.
DR   STRING; 456481.LEPBI_I0236; -.
DR   EnsemblBacteria; ABZ96381; ABZ96381; LEPBI_I0236.
DR   GeneID; 6222071; -.
DR   KEGG; lbi:LEPBI_I0236; -.
DR   PATRIC; 22347166; VBILepBif123590_0238.
DR   eggNOG; COG0462; -.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; YVQIQES; -.
DR   ProtClustDB; PRK01259; -.
DR   BioCyc; LBIF456481:GCM0-235-MONOMER; -.
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      213    226       5-phosphoribose 1-diphosphate binding (By
FT                                similarity).
FT   METAL       130    130       Magnesium (By similarity).
FT   METAL       132    132       Magnesium (By similarity).
FT   METAL       145    145       Magnesium (By similarity).
SQ   SEQUENCE   313 AA;  34213 MW;  950A2469A64B5321 CRC64;
     MNPSEVVVFS GNANRPLAEE ICKNLKIPNG QISVKRFSDG ESSVKIEENV RGRDVFVVQS
     ISYPANDSLM ELLLIIDAAR RASARRITAV IPYYGYGRQD RKVEPRVPIS ARMVADLIET
     VGPDRVLTMD LHADQIQGFF RIPVDHLYFS PVLAEYINSL GMDDLVIVSP DSGGAERARN
     FGKKVNGSLA IIDKRRPKAN ESVVMHVIGD IKDKNCLLLD DMIDTGGTIA KAATALYENG
     AKSVLCCASH GVLSGEAPSK LNEAKFNPIV LSNSIVIPES KKINHLKTLS IAPLFAKAIE
     RIHNEESISS LFS
//