UPP_CLOP1
ID UPP_CLOP1 Reviewed; 209 AA.
AC Q0TNB4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=CPF_2462;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000246; ABG84779.1; -; Genomic_DNA.
DR RefSeq; WP_003452430.1; NC_008261.1.
DR AlphaFoldDB; Q0TNB4; -.
DR SMR; Q0TNB4; -.
DR STRING; 195103.CPF_2462; -.
DR EnsemblBacteria; ABG84779; ABG84779; CPF_2462.
DR GeneID; 29570430; -.
DR KEGG; cpf:CPF_2462; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_9; -.
DR OMA; TYATRMP; -.
DR OrthoDB; 1581906at2; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000001823; 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..209
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_1000053707"
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; 22986 MW; 739CE073D4C41CD1 CRC64;
MSKVTEITHP LILHKLAFIR DKNTGSKDFR ELVSEVSMLM AYEVTRNLPM EEIEIETPVC
KTKCKVLAGK KVAIVPILRA GLGMVDGMLQ LIPAAKVGHI GLYRDEETLQ PVEYFCKLPQ
DIAERDVIVV DPMLATGGSA ADAITLLKKR GAKQIRLMCL ISSPEGIEFV QKAHPDVDIY
VACIDEKLND HGYIVPGLGD AGDRLFGTK
