ID X2GWJ1_9GAMM Unreviewed; 208 AA.
AC X2GWJ1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=A9G17_07585 {ECO:0000313|EMBL:OCF92984.1}, B6D08_08400
GN {ECO:0000313|EMBL:OTP99142.1}, FPQ15_08220
GN {ECO:0000313|EMBL:TSJ98487.1};
OS Gilliamella apicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC Gilliamella.
OX NCBI_TaxID=1196095 {ECO:0000313|EMBL:TSJ98487.1, ECO:0000313|Proteomes:UP000319483};
RN [1] {ECO:0000313|EMBL:OCF92984.1, ECO:0000313|Proteomes:UP000093149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WkB7 {ECO:0000313|EMBL:OCF92984.1}, and wkB7
RC {ECO:0000313|Proteomes:UP000093149};
RA Zheng H.;
RT "Genome sequence of Gilliamella apicola.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OTP99142.1, ECO:0000313|Proteomes:UP000194977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-7-12 {ECO:0000313|EMBL:OTP99142.1,
RC ECO:0000313|Proteomes:UP000194977};
RA Ludvigsen J., Porcellato D., Labee-Lund T.M., Amdam G.V., Rudi K.;
RT "Comparative genomics of honeybee gut symbionts reveal geographically
RT distinct and subgroup specific antibiotic resistance.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TSJ98487.1, ECO:0000313|Proteomes:UP000319483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W8127 {ECO:0000313|EMBL:TSJ98487.1,
RC ECO:0000313|Proteomes:UP000319483};
RA Zheng H.;
RT "Gilliamella genomes.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:TSJ98487.1}.
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DR EMBL; LZGG01000001; OCF92984.1; -; Genomic_DNA.
DR EMBL; NARP01000020; OTP99142.1; -; Genomic_DNA.
DR EMBL; VMHM01000010; TSJ98487.1; -; Genomic_DNA.
DR RefSeq; WP_025314320.1; NZ_VMHM01000010.1.
DR AlphaFoldDB; X2GWJ1; -.
DR GeneID; 29849341; -.
DR KEGG; gap:GAPWK_0071; -.
DR PATRIC; fig|1196095.8.peg.73; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_6; -.
DR OrthoDB; 9781675at2; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000093149; Chromosome.
DR Proteomes; UP000194977; Unassembled WGS sequence.
DR Proteomes; UP000319483; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01218}.
FT BINDING 78
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 103
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 130..138
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 193
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 198..200
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01218"
FT BINDING 199
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 208 AA; 22764 MW; E60E9A6E82CA0312 CRC64;
MKIVEVKHPL VRHKIGLMRE HDISTKDFRD LASEVGSLLT YEATANLPTE TVTIEGWCGP
VQVERIKGKK ITVVPILRAG LGMMDGVLEH VPSARISVVG FYRNEETLEP VPYFQKLTSD
IEERMALVVD PMLATGGSMV ATIDLLKKAG CKNIKVLVLV AAPEGIKTLE QAHPDVELYT
ASIDERLNDK GYILPGLGDA GDKIFGTK
//
