ID   UPP_TREPA               Reviewed;         360 AA.
AC   O83462;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative uracil phosphoribosyltransferase;
DE            EC=2.4.2.9;
DE   AltName: Full=UMP pyrophosphorylase;
DE   AltName: Full=UPRTase;
GN   Name=upp; OrderedLocusNames=TP_0448;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC       ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000305}.
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:0000305};
CC       Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC       {ECO:0000305};
CC   -!- ACTIVITY REGULATION: Allosterically activated by GTP. {ECO:0000305}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uracil: step 1/1.
CC   -!- SIMILARITY: Belongs to the UPRTase family. Highly divergent.
CC       {ECO:0000305}.
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DR   EMBL; AE000520; AAC65434.1; -; Genomic_DNA.
DR   PIR; H71324; H71324.
DR   RefSeq; WP_010881896.1; NC_021490.2.
DR   AlphaFoldDB; O83462; -.
DR   SMR; O83462; -.
DR   STRING; 243276.TPANIC_0448; -.
DR   EnsemblBacteria; AAC65434; AAC65434; TP_0448.
DR   GeneID; 57878972; -.
DR   KEGG; tpa:TP_0448; -.
DR   eggNOG; COG0035; Bacteria.
DR   HOGENOM; CLU_067096_1_1_12; -.
DR   OMA; PSMIMSK; -.
DR   OrthoDB; 1581906at2; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000000811; Chromosome.
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; Magnesium;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..360
FT                   /note="Putative uracil phosphoribosyltransferase"
FT                   /id="PRO_0000120907"
FT   BINDING         205
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         242..250
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250"
FT   BINDING         312..314
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  41018 MW;  9E2CAB2E2FA3768C CRC64;
     MEGQTARRVI TEAKFLDDCL TERDSYYLSK LDELYSSAMS SFAQFEDQQN GARSARAEEN
     IIATYDSIGN LMQEICKELP ALKVYSFETQ RENHAEVSRV VSKLRNIHTG YSEFIYYTQR
     AFEMLFRLAY GGSHEEHKTY LITKTPVAFP VQNYAVHKIA NVDYKIENTV MCVMLRGALL
     PSMIVSKEIE EYSSHGYVTP FALFKIKRDD LRDERDMQYV FDLDKSYFSA RELDGKDLVF
     ADPMNATGGS LVTIVRYLQD LGVKPKSISC FHMISALKGA IRVVRSLENC TVYTLWMDPV
     LNARAYIMPG LGDAGDRVNG VDVEDYPRNI IQLLADYGSN ISGLYRSQLR KIEETVLGSR