AC   MF_01218;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_01218_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_01218_A; -; 1; level=0
XX
Names: Upp
XX
ID   UPP
DE   RecName: Full=Uracil phosphoribosyltransferase;
DE            EC=2.4.2.9;
DE   AltName: Full=UMP pyrophosphorylase;
DE   AltName: Full=UPRTase;
GN   Name=upp;
XX
CC   -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC       ribose 1-diphosphate (PRPP) to UMP and diphosphate.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-
CC       PRPP.;
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uracil: step 1/1.
CC   -!- SIMILARITY: Belongs to the UPRTase family.
XX
DR   Pfam; PF00156; Pribosyltran; 1; trigger=no
DR   NCBIfam; TIGR01091; Upp; 1; trigger=no
XX
KW   Allosteric enzyme
KW   Glycosyltransferase
KW   GTP-binding
KW   Magnesium
KW   Nucleotide-binding
KW   Transferase
XX
GO   GO:0000287; F:magnesium ion binding
GO   GO:0004845; F:uracil phosphoribosyltransferase activity
GO   GO:0008655; P:pyrimidine-containing compound salvage
XX
FT   From: UPP_BACCL (P70881)
case <OC:Bacteria>
FT   BINDING         131..139
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   BINDING         199..201
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT   Condition: G-x-[AIC]
FT   BINDING         79
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: R
FT   BINDING         104
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: [RK]
FT   BINDING         194
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT   Condition: [IV]
FT   BINDING         200
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: D
end case
FT   From: UPP_SACS2 (Q980Q4)
case <OC:Archaea>
FT   BINDING         30..34
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Optional; Condition: [KR]-x(3)-[RK]
FT   BINDING         140..148
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   BINDING         208..210
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT   Condition: G-x-[AIC]
FT   BINDING         80
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: R
FT   BINDING         105
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: [RK]
FT   BINDING         203
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT   Condition: [IV]
FT   BINDING         209
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT   Condition: D
end case
XX
case <OC:Bacteria>
Size: 206-218;
end case
case <OC:Archaea>
Size: 211-232;
end case
Related: None;
Template: P70881; P0A8F0; Q980Q4; P39149;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: None
Duplicate: None
Plasmid: None
Comments: Divergent PORGI and TREPA; sequences not included in alignment.
 Possible wrong start in STRCO.
XX
# Revision 1.34 2023/06/01
//