UPP_CHRSD
ID UPP_CHRSD Reviewed; 209 AA.
AC Q1QVR2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=Csal_2095;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE59446.1; -; Genomic_DNA.
DR RefSeq; WP_011507392.1; NC_007963.1.
DR AlphaFoldDB; Q1QVR2; -.
DR SMR; Q1QVR2; -.
DR STRING; 290398.Csal_2095; -.
DR EnsemblBacteria; ABE59446; ABE59446; Csal_2095.
DR KEGG; csa:Csal_2095; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_6; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000000239; 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 3: Inferred from homology;
KW Allosteric enzyme; Glycosyltransferase; GTP-binding; Magnesium;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_1000053699"
FT BINDING 79
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 104
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 131..139
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 194
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 199..201
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 200
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 209 AA; 22718 MW; 15293E281078D8F5 CRC64;
MSVHAIQHPL VKHKLGLMRE AGISTKSFRE LASEVAKLLT YEATQDLETQ KTEIPGWSGE
MLEVELLKGK KVTVVPILRA GLGMLDGVTD LIPSARVSVV GLYRNEETLE PVPYFEKFVG
DLDERLAIVI DPMLATGGSM VATLDMLKAR GCPLVKVIVL VAAPEGIARV QEAYPDVEIY
TASIDERLDE NGYIVPGLGD AGDKIFGTR
