ID   UPP_MYCAP               Reviewed;         208 AA.
AC   A5IYF5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=MAG3660;
OS   Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS   agalactiae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=347257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX   PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA   Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA   Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA   Blanchard A., Citti C.;
RT   "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT   bacterial genome.";
RL   PLoS Genet. 3:744-758(2007).
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; CU179680; CAL59064.1; -; Genomic_DNA.
DR   RefSeq; WP_011949539.1; NC_009497.1.
DR   AlphaFoldDB; A5IYF5; -.
DR   SMR; A5IYF5; -.
DR   STRING; 347257.MAG3660; -.
DR   EnsemblBacteria; CAL59064; CAL59064; MAG3660.
DR   KEGG; maa:MAG3660; -.
DR   HOGENOM; CLU_067096_2_2_14; -.
DR   OMA; TYATRMP; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000007065; 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; Reference proteome; Transferase.
FT   CHAIN           1..208
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_1000139143"
FT   BINDING         77
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         102
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         129..137
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         193
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         198..200
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         199
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   208 AA;  23553 MW;  903FC042CF17B5CA CRC64;
     MLKVLDHPLI KIKLTNMRNR ESGHSVFRQN LNEIGSLMVY EILRDYQTKR KEIITSINKK
     YLGYEFDKDV VFVPILRAGL GMIDGLLKLI PEAKVGHIGM SRDETTFKPT EYFYKIPEVP
     KDSYIFVVDP MLATGNSAVD AITRLRKDGF NNISLVCLVG VKEGVDNVEK HFGHDINIYL
     AALDECLNKD KYIEPGLGDA GDRIFGTK