UPP_LACKL
ID UPP_LACKL Reviewed; 216 AA.
AC A5H0J4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Uracil phosphoribosyltransferase;
DE Short=UPRTase;
DE EC=2.4.2.9;
DE AltName: Full=Pyrimidine-degrading protein 16;
DE AltName: Full=UMP pyrophosphorylase;
DE AltName: Full=Uracil catabolism protein 6;
GN Name=FUR1; Synonyms=PYD16, URC6;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=18550080; DOI=10.1016/j.jmb.2008.05.029;
RA Andersen G., Bjoernberg O., Polakova S., Pynyaha Y., Rasmussen A.,
RA Moeller K., Hofer A., Moritz T., Sandrini M.P., Merico A.M., Compagno C.,
RA Aekerlund H.E., Gojkovic Z., Piskur J.;
RT "A second pathway to degrade pyrimidine nucleic acid precursors in
RT eukaryotes.";
RL J. Mol. Biol. 380:656-666(2008).
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate.
CC {ECO:0000269|PubMed:18550080}.
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}.
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DR EMBL; DQ512720; ABF58892.1; -; Genomic_DNA.
DR AlphaFoldDB; A5H0J4; -.
DR SMR; A5H0J4; -.
DR UniPathway; UPA00574; UER00636.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR SUPFAM; SSF53271; SSF53271; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Glycosyltransferase; GTP-binding; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..216
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000372695"
FT BINDING 32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 75..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 110
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 137..145
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 137
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 201
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 207..209
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250|UniProtKB:Q26998"
FT BINDING 208
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 24373 MW; A3771E70B6994E3D CRC64;
MSSEPFKNVY LLPQTNQLLG LYTIIRDKKT KRPDFVFYSD RIIRLLVEEG LNHLPVTPNT
VETDTNQSFD GVSFLGKICG VSIVRAGESM EQGLRDCCRS VRIGKILIQR DEETALPKLF
YEKLPDDIAD RFVFLLDPML ATGGSAIMAT EVLIKRGVKP ERIFFLNLIC SKEGIENYHA
KFPTIKIVTG ALDKGLDANR YLIPGLGDFG DRYYCI
