UPP_BACCL
ID UPP_BACCL Reviewed; 209 AA.
AC P70881;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 103.
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};
OS Bacillus caldolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 405 / NBRC 15313 / YP-T;
RX PubMed=9268683; DOI=10.1006/prep.1997.0755;
RA Jensen H.K., Mikkelsen N., Neuhard J.;
RT "Recombinant uracil phosphoribosyltransferase from the thermophile Bacillus
RT caldolyticus: expression, purification, and partial characterization.";
RL Protein Expr. Purif. 10:356-364(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH UMP, CATALYTIC
RP ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12037295; DOI=10.1107/s0907444902005024;
RA Kadziola A., Neuhard J., Larsen S.;
RT "Structure of product-bound Bacillus caldolyticus uracil
RT phosphoribosyltransferase confirms ordered sequential substrate binding.";
RL Acta Crystallogr. D 58:936-945(2002).
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, ECO:0000269|PubMed:12037295}.
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 ECO:0000269|PubMed:12037295};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 uM for uracil {ECO:0000269|PubMed:12037295};
CC KM=37 uM for 5-phospho-alpha-D-ribose 1-diphosphate
CC {ECO:0000269|PubMed:12037295};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01218}.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_01218}.
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DR EMBL; X99545; CAA67884.1; -; Genomic_DNA.
DR PIR; T48896; T48896.
DR PDB; 1I5E; X-ray; 3.00 A; A/B=1-209.
DR PDBsum; 1I5E; -.
DR AlphaFoldDB; P70881; -.
DR SMR; P70881; -.
DR BRENDA; 2.4.2.9; 642.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; P70881; -.
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; Transferase.
FT CHAIN 1..209
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120795"
FT BINDING 79
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 104
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 131..139
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 194
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT BINDING 199..201
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT BINDING 200
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 4..6
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 26..44
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1I5E"
FT TURN 120..124
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1I5E"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1I5E"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:1I5E"
SQ SEQUENCE 209 AA; 22859 MW; 0A46CA8A6DD6AAA0 CRC64;
MGKVYVFDHP LIQHKLTYIR DKNTGTKEFR ELVDEVATLM AFEITRDLPL EEVEIETPVS
KARAKVIAGK KLGVIPILRA GIGMVDGILK LIPAAKVGHI GLYRDPQTLK PVEYYVKLPS
DVEERDFIIV DPMLATGGSA VAAIDALKKR GAKSIKFMCL IAAPGRVKAV ETAHPDVDIY
IAALDERLND HGYIVPGLGD AGDRLFGTK
