UPP_BURPS
ID UPP_BURPS Reviewed; 216 AA.
AC Q63VS8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Uracil phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01218};
DE EC=2.4.2.9 {ECO:0000255|HAMAP-Rule:MF_01218};
DE AltName: Full=UMP pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01218};
DE AltName: Full=UPRTase {ECO:0000255|HAMAP-Rule:MF_01218};
GN Name=upp {ECO:0000255|HAMAP-Rule:MF_01218}; OrderedLocusNames=BPSL1166;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "2.6 A crystal structure of uracil phosphoribosyltransferase from
RT Burkholderia pseudomallei.";
RL Submitted (JUL-2008) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-
CC ribose 1-diphosphate (PRPP) to UMP and diphosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01218};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000255|HAMAP-Rule:MF_01218};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_01218}.
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DR EMBL; BX571965; CAH35161.1; -; Genomic_DNA.
DR RefSeq; WP_004186446.1; NZ_CP009538.1.
DR RefSeq; YP_107788.1; NC_006350.1.
DR PDB; 3DMP; X-ray; 2.60 A; A/B/C/D=1-216.
DR PDBsum; 3DMP; -.
DR AlphaFoldDB; Q63VS8; -.
DR SMR; Q63VS8; -.
DR STRING; 272560.BPSL1166; -.
DR EnsemblBacteria; CAH35161; CAH35161; BPSL1166.
DR GeneID; 56595096; -.
DR KEGG; bps:BPSL1166; -.
DR PATRIC; fig|272560.51.peg.371; -.
DR eggNOG; COG0035; Bacteria.
DR OMA; TYATRMP; -.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; Q63VS8; -.
DR Proteomes; UP000000605; Chromosome 1.
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 SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01091; upp; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Glycosyltransferase; GTP-binding;
KW Magnesium; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..216
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120809"
FT BINDING 85
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01218"
FT BINDING 135..143
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 200
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01218"
FT BINDING 205..207
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01218"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 32..50
FT /evidence="ECO:0007829|PDB:3DMP"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:3DMP"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:3DMP"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:3DMP"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3DMP"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3DMP"
SQ SEQUENCE 216 AA; 24075 MW; DA8F1B3A2ECFB56B CRC64;
MKQDSRFPNL FILDHPLIQH KLTHMRDKDT STRTFRELLR EITLLMGYEI TRNLPITTKR
VETPLVEIDA PVIAGKKLAI VPVLRAGVGM SDGLLELIPS ARVGHIGVYR ADDHRPVEYL
VRLPDLEDRI FILCDPMVAT GYSAAHAIDV LKRRGVPGER LMFLALVAAP EGVQVFQDAH
PDVKLYVASL DSHLDDHAYI VPGLGDAGDR LFGTKN
