ID UPP_MYCGE Reviewed; 206 AA. AC P47276; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 135. 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=MG030; OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-206. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71246.1; -; Genomic_DNA. DR EMBL; U01773; AAD10592.1; -; Genomic_DNA. DR PIR; C64203; C64203. DR RefSeq; WP_009885912.1; NZ_AAGX01000010.1. DR AlphaFoldDB; P47276; -. DR SMR; P47276; -. DR STRING; 243273.MG_030; -. DR KEGG; mge:MG_030; -. DR eggNOG; COG0035; Bacteria. DR HOGENOM; CLU_067096_2_2_14; -. DR InParanoid; P47276; -. DR OrthoDB; 9781675at2; -. DR BioCyc; MGEN243273:G1GJ2-30-MONOMER; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; IBA:GO_Central. 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..206 FT /note="Uracil phosphoribosyltransferase" FT /id="PRO_0000120850" FT BINDING 76 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 101 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 128..136 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 191 FT /ligand="uracil" FT /ligand_id="ChEBI:CHEBI:17568" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT BINDING 196..198 FT /ligand="uracil" FT /ligand_id="ChEBI:CHEBI:17568" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218" FT BINDING 197 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 206 AA; 22973 MW; 26B021599F8CC303 CRC64; MIKKVQHALI LNELTKLRDK NTTTSQFRMA LNQITSLLFF EATKQLPLAT VEVETPFAKT KGYKLKNDIV LVPIMRAGLG MIDAIVRYSD KIRVGHLGIY RQTQTTSVIS YYKKMPENIS DSHVIILDPM LATGTTLLTA IKSIKEDKPI KISVIAIVAA PEGINKVEKM HPHVDIFLAA IDEKLNDNRY IIPGLGDAGD RLFGTK //