ID A0A0R1WDP2_9LACO Unreviewed; 215 AA.
AC A0A0R1WDP2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011894, ECO:0000256|HAMAP-Rule:MF_01218};
DE EC=2.4.2.9 {ECO:0000256|ARBA:ARBA00011894, ECO:0000256|HAMAP-Rule:MF_01218};
DE AltName: Full=UMP pyrophosphorylase {ECO:0000256|ARBA:ARBA00031082, ECO:0000256|HAMAP-Rule:MF_01218};
DE AltName: Full=UPRTase {ECO:0000256|HAMAP-Rule:MF_01218};
GN Name=upp {ECO:0000256|HAMAP-Rule:MF_01218};
GN ORFNames=FC15_GL000117 {ECO:0000313|EMBL:KRM12918.1};
OS Lapidilactobacillus concavus DSM 17758.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lapidilactobacillus.
OX NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM12918.1, ECO:0000313|Proteomes:UP000051315};
RN [1] {ECO:0000313|EMBL:KRM12918.1, ECO:0000313|Proteomes:UP000051315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM12918.1,
RC ECO:0000313|Proteomes:UP000051315};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01218};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000256|HAMAP-Rule:MF_01218};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC {ECO:0000256|HAMAP-Rule:MF_01218}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1. {ECO:0000256|ARBA:ARBA00005180,
CC ECO:0000256|HAMAP-Rule:MF_01218}.
CC -!- SIMILARITY: Belongs to the UPRTase family.
CC {ECO:0000256|ARBA:ARBA00009516, ECO:0000256|HAMAP-Rule:MF_01218}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM12918.1}.
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DR EMBL; AZFX01000010; KRM12918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1WDP2; -.
DR STRING; 1423735.FC15_GL000117; -.
DR PATRIC; fig|1423735.3.peg.119; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000051315; Unassembled WGS sequence.
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 NCBIfam; TIGR01091; upp; 1.
DR PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR32315:SF4; URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC; 1.
DR Pfam; PF14681; UPRTase; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW Rule:MF_01218};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01218};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01218};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01218};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01218}; Reference proteome {ECO:0000313|Proteomes:UP000051315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01218}.
FT BINDING 85
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 110
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 137..145
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 200
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 205..207
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 206
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
SQ SEQUENCE 215 AA; 23459 MW; FFF29287B14FE278 CRC64;
MKGGKSMGKF TVLNHPLIQH KLTIIRDKAT GTKVFREVAN EIAELMVYEI TRDLPLVDVE
IETPMGKTVQ KQLSGKKLAV VPILRAGLGM VDGVLQLIPA AKVGHIGMYR DEQTLEPHEY
FVKMPPDIDQ RDLFIVDPML ATGGSANMAI DALKKRGAKN MRLVVLVAAP EGVKAVQEAH
PDVDIYAASL DEKLTDNGYI FPGLGDAGDR LFGTK
//
