UPP_STRE4
ID UPP_STRE4 Reviewed; 209 AA.
AC C0M7M9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218};
DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218};
DE AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218};
DE AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218};
GN Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; OrderedLocusNames=SEQ_1833;
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047;
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000255|HAMAP-
CC Rule:MF_01218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000255|HAMAP-Rule:MF_01218};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_01218}.
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DR EMBL; FM204883; CAW94986.1; -; Genomic_DNA.
DR RefSeq; WP_012516202.1; NC_012471.1.
DR AlphaFoldDB; C0M7M9; -.
DR SMR; C0M7M9; -.
DR PRIDE; C0M7M9; -.
DR EnsemblBacteria; CAW94986; CAW94986; SEQ_1833.
DR GeneID; 64010507; -.
DR KEGG; seu:SEQ_1833; -.
DR HOGENOM; CLU_067096_2_2_9; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000001365; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006223; P:uracil salvage; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_01218_B; Upp_B; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR034332; Upp_B.
DR InterPro; IPR005765; Ura_phspho_trans.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01091; upp; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Glycosyltransferase; GTP-binding; Magnesium;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..209
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_1000164836"
FT BINDING 79
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 104
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 131..139
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 194
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 199..201
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 200
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
SQ SEQUENCE 209 AA; 22894 MW; F075B745BA91DB9C CRC64;
MGKCQVISHP LIQHKLSILR RQDTSTKDFR ELVNEIAMLM GYEVSRDLPL EDVEIQTPVA
KTVQKQLAGK KLAIVPILRA GIGMVDGFLS LVPAAKVGHI GMYRNEETLE PVEYLVKLPE
DIDQRQIFIV DPMLATGGSA ILAVDSLKKR GAANIKFVCL VAAPEGVKKL QEAHPDVDIY
TAALDERLND HGYIVPGLGD AGDRLFGTK
