(data stored in ACNUC10821 zone)

SWISSPROT: KPRS2_LISMF

ID   KPRS2_LISMF             Reviewed;         311 AA.
AC   Q723E1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=Putative ribose-phosphate pyrophosphokinase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=RPPK 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=P-Rib-PP synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPP synthase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPPase 2 {ECO:0000255|HAMAP-Rule:MF_00583};
GN   Name=prs2 {ECO:0000255|HAMAP-Rule:MF_00583};
GN   OrderedLocusNames=LMOf2365_0538;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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
CC       (Rib-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,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=2.7.6.1;
CC         Evidence={ECO:0000255|HAMAP-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-
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:0000255|HAMAP-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
CC       family. Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- CAUTION: Part of a set of proteins in which some residues
CC       (ACT_SITE, NP_BIND, REGION and BINDING) are not conserved.
CC       {ECO:0000255|HAMAP-Rule:MF_00583}.
DR   EMBL; AE017262; AAT03320.1; -; Genomic_DNA.
DR   RefSeq; WP_003725720.1; NC_002973.6.
DR   SMR; Q723E1; -.
DR   EnsemblBacteria; AAT03320; AAT03320; LMOf2365_0538.
DR   KEGG; lmf:LMOf2365_0538; -.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; NVNQAVM; -.
DR   BioCyc; LMON265669:G1G0V-553-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-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   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; 2.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q723E1.
DR   SWISS-2DPAGE; Q723E1.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN         1    311       Putative ribose-phosphate
FT                                pyrophosphokinase 2.
FT                                /FTId=PRO_0000141156.
FT   NP_BIND      38     40       ATP. {ECO:0000255|HAMAP-Rule:MF_00583}.
FT   NP_BIND      97     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00583}.
FT   METAL       131    131       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
FT   METAL       171    171       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     219    219       Ribose-5-phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   311 AA;  34346 MW;  82F9270DB1B0D529 CRC64;
     MAGKMKLFSV TSERPLATKI ADYLDIPLCE VELQKFSDGE VKINIEESIR GTNAYVVQSM
     NSNVNERLME LLIMVDALKR ASVHSINIIM PYYGYARQDR KARSREPITA KLMANLIQRA
     GADRLITVDL HAAQIQGFFN IPIDHLSAIP LIGDYLIENY GEKDVVVVAP DHSGVVRARR
     IADRLNAPIA ILNRKPRPHE DEIMSVIGDV KGKVAIVVDD IIDTGVRATT SADILLEKGA
     VEVIACATHS VMAGNATERL QNSNIKEVIT SDSIDLPEDK QFDKLTTISI GRILGRAIEG
     VQENRSLHPL F
//

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