UPP_THET2
ID UPP_THET2 Reviewed; 208 AA.
AC Q72J35;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=TT_C0946;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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; AE017221; AAS81288.1; -; Genomic_DNA.
DR RefSeq; WP_011173367.1; NC_005835.1.
DR PDB; 1V9S; X-ray; 2.10 A; A/B/C/D=1-208.
DR PDBsum; 1V9S; -.
DR AlphaFoldDB; Q72J35; -.
DR SMR; Q72J35; -.
DR STRING; 262724.TT_C0946; -.
DR EnsemblBacteria; AAS81288; AAS81288; TT_C0946.
DR GeneID; 3168439; -.
DR KEGG; tth:TT_C0946; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_0; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; Q72J35; -.
DR Proteomes; UP000000592; 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 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Glycosyltransferase; GTP-binding;
KW Magnesium; Nucleotide-binding; Transferase.
FT CHAIN 1..208
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120905"
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"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:1V9S"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:1V9S"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1V9S"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1V9S"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1V9S"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:1V9S"
SQ SEQUENCE 208 AA; 22762 MW; A4864A09141522C5 CRC64;
MRITLVDHPL VQHKLAHLRD KRTGPKDFRE LAEEVAMLMA YEAMRDLELE ETTVETPIAP
ARVKVLSGKK LALVAILRAG LVMVEGILKL VPHARVGHIG LYRDPESLNP VQYYIKLPPD
IAERRAFLLD PMLATGGSAS LALSLLKERG ATGVKLMAIL AAPEGLERIA KDHPDTEVVV
AAIDERLNDH GYIVPGLGDA GDRIYGTK
