ID D3V7C9_XENBS Unreviewed; 208 AA.
AC D3V7C9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 ECO:0000313|EMBL:CBJ81741.1};
GN OrderedLocusNames=XBJ1_2617 {ECO:0000313|EMBL:CBJ81741.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ81741.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ81741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ81741.1};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
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}.
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DR EMBL; FN667741; CBJ81741.1; -; Genomic_DNA.
DR RefSeq; WP_012989040.1; NC_013892.1.
DR AlphaFoldDB; D3V7C9; -.
DR STRING; 406818.XBJ1_2617; -.
DR KEGG; xbo:XBJ1_2617; -.
DR PATRIC; fig|406818.4.peg.2357; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_6; -.
DR UniPathway; UPA00574; UER00636.
DR Proteomes; UP000002045; 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 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; 22474 MW; 036E4491DB180D07 CRC64;
MKIVEVQHPL VKHKLGLMRA HDISTKRFRE LASEVGSLLT YEATADLEVE KVTIEGWCGP
VEIDQIKGKK ITVVPILRAG LGMMDGVLEN IPSARISVVG VYRDEETFEP VPYFQKLVSD
ISERMALVVD PMLATGGSMI ATIDLLKKAG CPVIKVLVLV AAPEGVAALA KVHPDVELFT
ASIDECLNEH GYIVPGLGDA GDKIFGTK
//
