ID   UPP_ROSCS               Reviewed;         208 AA.
AC   A7NRA6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Rcas_4070;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) 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: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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000804; ABU60102.1; -; Genomic_DNA.
DR   RefSeq; WP_012122523.1; NC_009767.1.
DR   AlphaFoldDB; A7NRA6; -.
DR   SMR; A7NRA6; -.
DR   STRING; 383372.Rcas_4070; -.
DR   EnsemblBacteria; ABU60102; ABU60102; Rcas_4070.
DR   KEGG; rca:Rcas_4070; -.
DR   eggNOG; COG0035; Bacteria.
DR   HOGENOM; CLU_067096_2_2_0; -.
DR   OMA; TYATRMP; -.
DR   OrthoDB; 1581906at2; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000000263; 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   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01091; upp; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Glycosyltransferase; GTP-binding; Magnesium;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..208
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_1000085633"
FT   BINDING         78
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         103
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         130..138
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         193
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         198..200
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         199
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   208 AA;  22876 MW;  FD5B887EA20F90CA CRC64;
     MKQVFISQHP LVHHKLTLLR RATTEPKKFR ELVSELSQFL LYEATLDLPL QERAIDTPLA
     PYHGHQIAER IGLVPILRAG LGMVDPILDL IPTAHVWHLG LYRDHATLQP VTYYNKLPPE
     VDVDLCLVLD PMLATGGSAV AAVSILKEWG ASRIKFLGLI AAPEGVRALH EAHPNVPIHL
     AALDDHLNDR GYIVPGLGDA GDRLFGTG