ID   UPP_TOBAC               Reviewed;         224 AA.
AC   P93394;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Uracil phosphoribosyltransferase;
DE            Short=UPRTase;
DE            EC=2.4.2.9;
DE   AltName: Full=UMP pyrophosphorylase;
GN   Name=UPP;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bright Yellow 2;
RA   Shen W.H., Gigot C.;
RT   "Uracil phosphoribosyltransferase protein of Nicotiana tabacum.";
RL   Submitted (FEB-1997) 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:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC       {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP. {ECO:0000250}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uracil: step 1/1.
CC   -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000305}.
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; Y11210; CAA72093.1; -; mRNA.
DR   PIR; T03969; T03969.
DR   AlphaFoldDB; P93394; -.
DR   SMR; P93394; -.
DR   STRING; 4097.P93394; -.
DR   PRIDE; P93394; -.
DR   ProMEX; P93394; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IBA:GO_Central.
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   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005765; Ura_phspho_trans.
DR   SUPFAM; SSF53271; SSF53271; 1.
DR   TIGRFAMs; TIGR01091; upp; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Glycosyltransferase; GTP-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..224
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_0000120785"
FT   BINDING         92
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         145..153
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..217
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   224 AA;  24195 MW;  EA4457CA6E445EAC CRC64;
     MAAQNKAMSG NRMLVFVPPH PLIKHWVSVL RNEQTPCPIF RNAMSELGRL LMYEASRDWL
     PIITGEIQSP MGVASVEFVD PREPVAIVPI LRAGLALAEH ASSILPATKT YHLGISRNEE
     TLQPSVYLNK LPDKFPEGSR VIVVDPMLAT GGTIVAAIDL IKERGVDNSQ IKVICAVGAP
     PALQKLSEKF PGLHVYAGIL DPTVNDKGFI IPGLGDAGDR SFGT