ID   UPP_THEGJ               Reviewed;         224 AA.
AC   C5A6P6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=TGAM_1406;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS33908.1; -; Genomic_DNA.
DR   RefSeq; WP_015859019.1; NC_012804.1.
DR   AlphaFoldDB; C5A6P6; -.
DR   SMR; C5A6P6; -.
DR   STRING; 593117.TGAM_1406; -.
DR   PaxDb; C5A6P6; -.
DR   EnsemblBacteria; ACS33908; ACS33908; TGAM_1406.
DR   GeneID; 7988139; -.
DR   KEGG; tga:TGAM_1406; -.
DR   PATRIC; fig|593117.10.peg.1408; -.
DR   eggNOG; arCOG04128; Archaea.
DR   HOGENOM; CLU_067096_2_0_2; -.
DR   OMA; TYATRMP; -.
DR   OrthoDB; 85528at2157; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000001488; 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_A; Upp_A; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR034331; Upp_A.
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..224
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_1000213945"
FT   BINDING         38..42
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         87
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         112
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         140..148
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         204
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         209..211
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT   BINDING         210
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   224 AA;  25143 MW;  5B0D0697FE730A06 CRC64;
     MRRDERWDGV YSFEDSPFIM EILTELRDKN TDSIAFRKGL VKLGRYMGYE LTKTMDVEEI
     EVETPLEKTR GILVKDRRNV VIITVLRAAI PLMEGLIKVF EHARVGIVSA SRGKAPKFEI
     EMNYIKIPTV KPDDTVIVAD PMIATGSTLI RVLKEVSKYG RPKRLIILGV LAAPEGISRI
     KEAFPEAEIF VAKVDRELNE KGYILPGLGD AGDRAFGAPL KSPR