ID A0A0N0UXD8_9BACI Unreviewed; 209 AA. AC A0A0N0UXD8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 28-JUN-2023, entry version 45. DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011894, ECO:0000256|HAMAP-Rule:MF_01218}; DE EC=2.4.2.9 {ECO:0000256|ARBA:ARBA00011894, ECO:0000256|HAMAP-Rule:MF_01218}; DE AltName: Full=UMP pyrophosphorylase {ECO:0000256|ARBA:ARBA00031082, ECO:0000256|HAMAP-Rule:MF_01218}; DE AltName: Full=UPRTase {ECO:0000256|HAMAP-Rule:MF_01218}; GN Name=upp {ECO:0000256|HAMAP-Rule:MF_01218, GN ECO:0000313|EMBL:KOY83927.1}; GN ORFNames=ADM90_00500 {ECO:0000313|EMBL:KOY83927.1}; OS Lysinibacillus macroides. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus. OX NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY83927.1, ECO:0000313|Proteomes:UP000037977}; RN [1] {ECO:0000313|EMBL:KOY83927.1, ECO:0000313|Proteomes:UP000037977} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 54 {ECO:0000313|EMBL:KOY83927.1, RC ECO:0000313|Proteomes:UP000037977}; RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H., RA Pan Z., Liu X.; RT "Genome sequencing project for genomic taxonomy and phylogenomics of RT Bacillus-like bacteria."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D- CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01218}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01218}; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP. CC {ECO:0000256|HAMAP-Rule:MF_01218}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. CC {ECO:0000256|HAMAP-Rule:MF_01218}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; CC UMP from uracil: step 1/1. {ECO:0000256|ARBA:ARBA00005180, CC ECO:0000256|HAMAP-Rule:MF_01218}. CC -!- SIMILARITY: Belongs to the UPRTase family. CC {ECO:0000256|ARBA:ARBA00009516, ECO:0000256|HAMAP-Rule:MF_01218}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KOY83927.1}. 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; LGCI01000002; KOY83927.1; -; Genomic_DNA. DR RefSeq; WP_053993121.1; NZ_LGCI01000002.1. DR AlphaFoldDB; A0A0N0UXD8; -. DR STRING; 33935.ADM90_00500; -. DR EnsemblBacteria; KOY83927; KOY83927; ADM90_00500. DR PATRIC; fig|33935.3.peg.2940; -. DR OrthoDB; 9781675at2; -. DR UniPathway; UPA00574; UER00636. DR Proteomes; UP000037977; Unassembled WGS sequence. 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 PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR32315:SF4; URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC; 1. DR Pfam; PF14681; UPRTase; 1. DR SUPFAM; SSF53271; PRTase-like; 1. DR TIGRFAMs; TIGR01091; upp; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP- KW Rule:MF_01218}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_01218}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01218}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01218}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01218}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01218}. FT BINDING 79 FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate" FT /ligand_id="ChEBI:CHEBI:58017" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01218" FT BINDING 194 FT /ligand="uracil" FT /ligand_id="ChEBI:CHEBI:17568" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218" FT BINDING 199..201 FT /ligand="uracil" FT /ligand_id="ChEBI:CHEBI:17568" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01218" SQ SEQUENCE 209 AA; 22950 MW; C8C33EB7C98297B2 CRC64; MSKVYVFDHP LIQHKLTYIR DKNTGTKEFR ELVDEVATLM AFEITRDMPV EEIEIETPVT VAKTKVLSGK KLAIVPILRA GIGMVDGVLK LIPAAKVGHI GLYRDPATLK PVEYYAKLPA DVEERDFIIV DPMLATGGSA VEAIHSLKKR GAKNIKFMCL IAAPEGVKAI QEEHADVDIY IAALDEKLND HGYIVPGLGD AGDRLFGTK //