(data stored in SCRATCH9089 zone)

SWISSPROT: KPRS_PASMU

ID   KPRS_PASMU              Reviewed;         315 AA.
AC   Q9CP22;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 115.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583};
DE            EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN   Name=prs {ECO:0000255|HAMAP-Rule:MF_00583}; Synonyms=prsA;
GN   OrderedLocusNames=PM0244;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 (Rib-
CC       5-P). {ECO:0000255|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, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC         ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00583};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00583};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00583};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC       1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC       D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00583}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583}.
DR   EMBL; AE004439; AAK02328.1; -; Genomic_DNA.
DR   RefSeq; WP_005724296.1; NC_002663.1.
DR   SMR; Q9CP22; -.
DR   PRIDE; Q9CP22; -.
DR   EnsemblBacteria; AAK02328; AAK02328; PM0244.
DR   GeneID; 29389446; -.
DR   KEGG; pmu:PM0244; -.
DR   eggNOG; ENOG4105C5T; Bacteria.
DR   eggNOG; COG0462; LUCA.
DR   HOGENOM; HOG000210452; -.
DR   KO; K00948; -.
DR   OMA; FGWARQD; -.
DR   BioCyc; PMUL272843:G1FZ8-255-MONOMER; -.
DR   UniPathway; UPA00087; UER00172.
DR   Proteomes; UP000000809; Chromosome.
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; 1.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CP22.
DR   SWISS-2DPAGE; Q9CP22.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..315
FT                   /note="Ribose-phosphate pyrophosphokinase"
FT                   /id="PRO_0000141170"
FT   NP_BIND         37..39
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   NP_BIND         96..97
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   REGION          225..229
FT                   /note="Ribose-5-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   METAL           131
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   METAL           171
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         197
FT                   /note="Ribose-5-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         221
FT                   /note="Ribose-5-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
SQ   SEQUENCE   315 AA;  34194 MW;  FCE414056A480E53 CRC64;
     MPDIKLFTGN ATPELAKRIS ERLYLSLGDA TVGRFSDGEI QVQINENVRG SDVFIIQSTC
     APTNDNLMEL IVMVDALRRA SAGRITAVIP YFGYARQDRR VRSARVPITA KVVADFLSSV
     GVDRVLTCDL HAEQIQGFFD VPVDNVFGSP VLVHDMLKKI DMQNPIVVSP DIGGVVRARA
     IAKLLNDTDM AIIDKRRPRA NVAQVMHIIG DVAGRDCILV DDMIDTGGTL CKAAEALKER
     GAKRVFAYAT HAVFSGSAAK NLASDALDEV VVTDTIPLSP EIKALNKVRV LTLSGMLAEA
     IRRISNEESI SAMFT
//

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