ID A0A0N0UXD8_9BACI Unreviewed; 209 AA. AC A0A0N0UXD8; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 16-JAN-2019, entry version 24. DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS00709136}; DE EC=2.4.2.9 {ECO:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS00918612}; DE AltName: Full=UMP pyrophosphorylase {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; Firmicutes; Bacilli; Bacillales; Bacillaceae; OC 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., RA Shi H., 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- CC D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. CC {ECO:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS00709092}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1- CC diphosphate + uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; CC EC=2.4.2.9; Evidence={ECO:0000256|HAMAP-Rule:MF_01218, CC ECO:0000256|SAAS:SAAS01124291}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01218}; CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg- CC PRPP. {ECO:0000256|HAMAP-Rule:MF_01218}; CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. CC {ECO:0000256|HAMAP-Rule:MF_01218, ECO:0000256|SAAS:SAAS01124293}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage CC pathway; UMP from uracil: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01218, ECO:0000256|SAAS:SAAS00918634}. CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000256|HAMAP- CC Rule:MF_01218, ECO:0000256|SAAS:SAAS00918654}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KOY83927; KOY83927; ADM90_00500. DR PATRIC; fig|33935.3.peg.2940; -. DR OrthoDB; 1581906at2; -. 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 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 {ECO:0000256|HAMAP-Rule:MF_01218}; KW Complete proteome {ECO:0000313|Proteomes:UP000037977}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01218, KW ECO:0000256|SAAS:SAAS00918621, ECO:0000313|EMBL:KOY83927.1}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_01218, KW ECO:0000256|SAAS:SAAS00918618}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01218, KW ECO:0000256|SAAS:SAAS00709102}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01218, KW ECO:0000256|SAAS:SAAS00918615}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01218, KW ECO:0000256|SAAS:SAAS00918631, ECO:0000313|EMBL:KOY83927.1}. FT REGION 131 139 5-phospho-alpha-D-ribose 1-diphosphate FT binding. {ECO:0000256|HAMAP-Rule: FT MF_01218}. FT REGION 199 201 Uracil binding. {ECO:0000256|HAMAP-Rule: FT MF_01218}. FT BINDING 79 79 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000256|HAMAP-Rule:MF_01218}. FT BINDING 104 104 5-phospho-alpha-D-ribose 1-diphosphate. FT {ECO:0000256|HAMAP-Rule:MF_01218}. FT BINDING 194 194 Uracil; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01218}. FT BINDING 200 200 5-phospho-alpha-D-ribose 1-diphosphate. FT {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 //