UPP_CHLMU
ID UPP_CHLMU Reviewed; 303 AA.
AC Q9PJJ6;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Uracil phosphoribosyltransferase;
DE EC=2.4.2.9;
DE AltName: Full=UMP pyrophosphorylase;
DE AltName: Full=UPRTase;
GN Name=upp; OrderedLocusNames=TC_0833;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000250}.
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; AE002160; AAF39633.1; -; Genomic_DNA.
DR PIR; H81658; H81658.
DR AlphaFoldDB; Q9PJJ6; -.
DR SMR; Q9PJJ6; -.
DR STRING; 243161.TC_0833; -.
DR EnsemblBacteria; AAF39633; AAF39633; TC_0833.
DR KEGG; cmu:TC_0833; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_0; -.
DR OMA; TYATRMP; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000000800; 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..303
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120813"
FT REGION 1..86
FT /note="Unknown"
FT REGION 87..303
FT /note="UPRTase"
FT BINDING 170
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 222..230
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 290..292
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
SQ SEQUENCE 303 AA; 32969 MW; 575469B1DEEDFF8B CRC64;
MHIIMKTILA TLCLILCASC CSKGACETRI KHTFSEKKFQ KYSPVPKHPL SEQTHLYAKS
CSIELEQTQL PTSTLTRYVS STPTDSLSSK PLAAVYVLSH PLIQHKASLL RNKNTKSKIF
RECLKEISLG VCYEATRDLA LKNISIQTPL MQAECPHLTG TKIVVIPVLR AGLGMVDGFL
ALVPNAKVGL IGMSRNHETF QPSSYCCKLP EDIADCHVFI VDPMLATGGS ASATIQLVKE
HGAKNITLLN VLAVPEGIER IQKDHPDVTI YVASLDEKLN ESAYILPGLG DAGDRLCGTS
NPS