ID   UPP_PORG3               Reviewed;         216 AA.
AC   B2RIV3; Q9ZNF8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Uracil phosphoribosyltransferase;
DE            EC=2.4.2.9;
DE   AltName: Full=UMP pyrophosphorylase;
DE   AltName: Full=UPRTase;
GN   Name=upp; OrderedLocusNames=PGN_0779;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nakayama K., Shi Y.;
RT   "PorT, upp, and prtQ genes of Porphyromonas gingivalis.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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; AB016085; BAA36601.1; -; Genomic_DNA.
DR   EMBL; AP009380; BAG33298.1; -; Genomic_DNA.
DR   RefSeq; WP_004585294.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RIV3; -.
DR   SMR; B2RIV3; -.
DR   STRING; 431947.PGN_0779; -.
DR   EnsemblBacteria; BAG33298; BAG33298; PGN_0779.
DR   GeneID; 29255998; -.
DR   KEGG; pgn:PGN_0779; -.
DR   eggNOG; COG0035; Bacteria.
DR   HOGENOM; CLU_067096_2_0_10; -.
DR   OMA; TYATRMP; -.
DR   BioCyc; PGIN431947:G1G2V-854-MON; -.
DR   UniPathway; UPA00574; UER00636.
DR   Proteomes; UP000008842; 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; Transferase.
FT   CHAIN           1..216
FT                   /note="Uracil phosphoribosyltransferase"
FT                   /id="PRO_0000370695"
FT   BINDING         81
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..143
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..207
FT                   /ligand="uracil"
FT                   /ligand_id="ChEBI:CHEBI:17568"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58017"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24371 MW;  7FA62BD4CFA1DFD2 CRC64;
     MEVIHLGAEH SLLNRFVMEM RDVTIQNDRL RFRRNIERVG EVMAYEISKK MTQQVRTVTT
     PLGEAECSVP QDKVVLATIL RAGLPFHHGF LNYFDYCENA FVSAYRKYKD RLNFDIHIEY
     IASPDITDKV LIISDPMLAT GSSMELAYKA LLTKGNPKHI HIASIIASQQ AVDYIRGVMP
     DNTTIWIAAI DPTIDEHSYI VPGLGDAGDL AYGEKL