KPRS1_LISMO
ID KPRS1_LISMO Reviewed; 318 AA.
AC Q48793;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
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}; OrderedLocusNames=lmo0199;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=8039927; DOI=10.1128/iai.62.8.3550-3553.1994;
RA Gouin E., Mengaud J., Cossart P.;
RT "The virulence gene cluster of Listeria monocytogenes is also present in
RT Listeria ivanovii, an animal pathogen, and Listeria seeligeri, a
RT nonpathogenic species.";
RL Infect. Immun. 62:3550-3553(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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}.
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DR EMBL; M92842; AAA62181.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00726.1; -; Genomic_DNA.
DR PIR; AH1099; AH1099.
DR RefSeq; NP_463730.1; NC_003210.1.
DR RefSeq; WP_003722728.1; NZ_CP023861.1.
DR AlphaFoldDB; Q48793; -.
DR SMR; Q48793; -.
DR STRING; 169963.lmo0199; -.
DR PaxDb; Q48793; -.
DR EnsemblBacteria; CAD00726; CAD00726; CAD00726.
DR GeneID; 67411467; -.
DR GeneID; 987027; -.
DR KEGG; lmo:lmo0199; -.
DR PATRIC; fig|169963.11.peg.204; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_4_0_9; -.
DR OMA; FGWARQD; -.
DR PhylomeDB; Q48793; -.
DR BioCyc; LMON169963:LMO0199-MON; -.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
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;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..318
FT /note="Ribose-phosphate pyrophosphokinase 1"
FT /id="PRO_0000141157"
FT ACT_SITE 199
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 43..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 102..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 201
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 225
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 229..233
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-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
