UPP_CLAM3
ID UPP_CLAM3 Reviewed; 212 AA.
AC A5CNC6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=CMM_0538;
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=443906;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382;
RX PubMed=18192381; DOI=10.1128/jb.01595-07;
RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(2008).
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}.
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; AM711867; CAN00563.1; -; Genomic_DNA.
DR RefSeq; WP_011931758.1; NC_009480.1.
DR AlphaFoldDB; A5CNC6; -.
DR SMR; A5CNC6; -.
DR STRING; 443906.CMM_0538; -.
DR EnsemblBacteria; CAN00563; CAN00563; CMM_0538.
DR GeneID; 56884821; -.
DR KEGG; cmi:CMM_0538; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_3_11; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000001564; 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; Transferase.
FT CHAIN 1..212
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_1000053701"
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 195
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 200..202
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 201
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 212 AA; 22785 MW; 1B9A0AB7A299CD67 CRC64;
MRVHVADHPL ITHKLTALRD RTTPSPVFRS LADELVTLLA YEATRDVRVE TITVQTPVAP
AEGLTLSDPK PLVVPILRAG LGMLDGLMRL MPSAEVGFLG MVRNEETLQP DIYAERLPTD
LSNRQCFVVD PMLATGGSLI AAIEYLFDRG AVDVTCICLI AAPEGLKAVE EATAGREVTI
VLGALDERLD EVGYIIPGLG DAGDRLYGTA AH