ID UPP_BACLD Reviewed; 209 AA. AC Q65DW6; Q62PD8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 121. 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}; GN OrderedLocusNames=BLi03934, BL03992; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000002; AAU25373.1; -; Genomic_DNA. DR EMBL; AE017333; AAU42748.1; -; Genomic_DNA. DR RefSeq; WP_003186017.1; NC_006322.1. DR AlphaFoldDB; Q65DW6; -. DR SMR; Q65DW6; -. DR STRING; 279010.BL03992; -. DR GeneID; 76975521; -. DR KEGG; bld:BLi03934; -. DR KEGG; bli:BL03992; -. DR eggNOG; COG0035; Bacteria. DR HOGENOM; CLU_067096_2_2_9; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000606; 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 NCBIfam; TIGR01091; upp; 1. DR PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR32315:SF4; URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC; 1. DR Pfam; PF14681; UPRTase; 1. DR SUPFAM; SSF53271; PRTase-like; 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_1000053677" 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; 23039 MW; A542FBC2D3F1EBBD CRC64; MGKVYVFDHP LIQHKLTYIR DVKTGTKEFR ELVDEVATLM AFEITRDLPL EEVNVETPVQ MAKSNVIAGK KLGVVPILRA GLGMVDGILK LIPAAKVGHV GLYRDPETLK PVEYYVKLPS DVEEREFIVV DPMLATGGSA VEALNSLKKR GAKNIRFMCL IAAPEGVDEV QKHHPDVDIY IAALDEKLNE KGYIVPGLGD AGDRMFGTK //