ID   A0A0N0UXD8_9BACI        Unreviewed;       209 AA.
AC   A0A0N0UXD8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   07-JUN-2017, entry version 15.
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:SAAS00766734};
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: UMP + diphosphate = uracil + 5-phospho-alpha-
CC       D-ribose 1-diphosphate. {ECO:0000256|HAMAP-Rule:MF_01218,
CC       ECO:0000256|SAAS:SAAS00766714}.
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   -!- ENZYME REGULATION: Allosterically activated by GTP.
CC       {ECO:0000256|HAMAP-Rule:MF_01218}.
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:SAAS00766740}.
CC   -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01218, ECO:0000256|SAAS:SAAS00766750}.
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}.
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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   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-HAMAP.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP.
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   PANTHER; PTHR10285:SF104; PTHR10285:SF104; 1.
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:SAAS00766747, ECO:0000313|EMBL:KOY83927.1};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00766729};
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:SAAS00766721};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01218,
KW   ECO:0000256|SAAS:SAAS00766742, 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
//