(data stored in ACNUC10821 zone)

SWISSPROT: KPRS1_LISMF

ID   KPRS1_LISMF             Reviewed;         318 AA.
AC   Q724L4;
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=Ribose-phosphate pyrophosphokinase 1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=RPPK 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase 1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase 1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=P-Rib-PP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE            Short=PRPPase 1 {ECO:0000255|HAMAP-Rule:MF_00583};
GN   Name=prs1 {ECO:0000255|HAMAP-Rule:MF_00583};
GN   OrderedLocusNames=LMOf2365_0210;
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}.
DR   EMBL; AE017262; AAT02997.1; -; Genomic_DNA.
DR   RefSeq; WP_003722728.1; NC_002973.6.
DR   SMR; Q724L4; -.
DR   PRIDE; Q724L4; -.
DR   EnsemblBacteria; AAT02997; AAT02997; LMOf2365_0210.
DR   KEGG; lmf:LMOf2365_0210; -.
DR   HOGENOM; HOG000210449; -.
DR   KO; K00948; -.
DR   OMA; FGWARQD; -.
DR   BioCyc; LMON265669:G1G0V-209-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; 1.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q724L4.
DR   SWISS-2DPAGE; Q724L4.
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Transferase.
FT   CHAIN         1    318       Ribose-phosphate pyrophosphokinase 1.
FT                                /FTId=PRO_0000141155.
FT   NP_BIND      43     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00583}.
FT   NP_BIND     102    103       ATP. {ECO:0000255|HAMAP-Rule:MF_00583}.
FT   REGION      229    233       Ribose-5-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00583}.
FT   ACT_SITE    199    199       {ECO:0000255|HAMAP-Rule:MF_00583}.
FT   METAL       136    136       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
FT   METAL       176    176       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     201    201       Ribose-5-phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
FT   BINDING     225    225       Ribose-5-phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00583}.
SQ   SEQUENCE   318 AA;  35069 MW;  AB286F742362FECD CRC64;
     MSNEYFDPKL KIFSLNSNRE LAEEIAKEVG IELGKSSVTH FSDGEIQINI EESIRGCHVY
     VIQSTSNPVN QNLMELLIMI DALKRASAAT INIVMPYYGY ARQDRKARSR EPITAKLVAN
     LIETAGATRM ITLDMHAPQI QGFFDIPIDH LNAVRLLSDY FSERHLGDDL VVVSPDHGGV
     TRARKMADRL KAPIAIIDKR RPRPNVAEVM NIVGNVEGKV CIIIDDIIDT AGTITLAAKA
     LREAGATKVY ACCSHPVLSG PAMKRIEESP IEKLVVTNSI ALPEEKWIDK MEQLSVAALL
     GEAIVRVHEN ASVSSLFE
//

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