ID   UPP_POLNA               Reviewed;         209 AA.
AC   A1VN11;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Pnap_1726;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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; CP000529; ABM37039.1; -; Genomic_DNA.
DR   RefSeq; WP_011801125.1; NC_008781.1.
DR   AlphaFoldDB; A1VN11; -.
DR   SMR; A1VN11; -.
DR   STRING; 365044.Pnap_1726; -.
DR   EnsemblBacteria; ABM37039; ABM37039; Pnap_1726.
DR   KEGG; pna:Pnap_1726; -.
DR   eggNOG; COG0035; Bacteria.
DR   HOGENOM; CLU_067096_2_2_4; -.
DR   OMA; TYATRMP; -.
DR   OrthoDB; 1581906at2; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000000644; 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..209
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_1000053756"
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;  23123 MW;  C93AD0CB1A26B5A8 CRC64;
     MSNVHLISHP LVQHKLTLMR RKNASTSTFR TLLAELSNLM AYEVTRDMPL QDIEVETPLE
     TTTGKIIDGK KLVLVSILRA GNGFLDGFLN VVPGARVGHI GLYRDPETLS PVEYYFKMPQ
     EMQERDIVIV DPMLATGNSA IAAVDRLKQL KPRSIKFVCL LTCPEGVAAL QKAHPDVDIY
     TAAIDRQLNE HGYILPGLGD AGDRIFGTK