UPP_ECOLI
ID UPP_ECOLI Reviewed; 208 AA.
AC P0A8F0; P25532; P78095; Q8XAC7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Uracil phosphoribosyltransferase;
DE EC=2.4.2.9;
DE AltName: Full=UMP pyrophosphorylase;
DE AltName: Full=UPRTase;
GN Name=upp; Synonyms=uraP; OrderedLocusNames=b2498, JW2483;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1371255; DOI=10.1111/j.1432-1033.1992.tb16604.x;
RA Anderson P.S., Smith J.M., Mygind B.;
RT "Characterization of the upp gene encoding uracil phosphoribosyltransferase
RT of Escherichia coli K12.";
RL Eur. J. Biochem. 204:51-56(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [7]
RP CATALYTIC ACTIVITY, CHARACTERIZATION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8856065; DOI=10.1111/j.1432-1033.1996.0637h.x;
RA Jensen K.F., Mygind B.;
RT "Different oligomeric states are involved in the allosteric behavior of
RT uracil phosphoribosyltransferase from Escherichia coli.";
RL Eur. J. Biochem. 240:637-645(1996).
RN [8]
RP MUTAGENESIS OF PRO-131, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10079076; DOI=10.1021/bi982279q;
RA Lundegaard C., Jensen K.F.;
RT "Kinetic mechanism of uracil phosphoribosyltransferase from Escherichia
RT coli and catalytic importance of the conserved proline in the PRPP binding
RT site.";
RL Biochemistry 38:3327-3334(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-208.
RG RIKEN structural genomics initiative (RSGI);
RT "Structure of uracil phosphoribosyl transferase.";
RL Submitted (FEB-2009) 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.
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:0000269|PubMed:8856065};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-
CC PRPP.;
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP.
CC {ECO:0000269|PubMed:8856065}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.53 uM for uracil {ECO:0000269|PubMed:10079076};
CC KM=58 uM for 5-phospho-alpha-D-ribose 1-diphosphate
CC {ECO:0000269|PubMed:10079076};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1.
CC -!- SUBUNIT: Homodimer or homotrimer in the absence of substrates, and
CC homopentamer or homohexamer in the presence of substrates.
CC {ECO:0000269|PubMed:8856065}.
CC -!- INTERACTION:
CC P0A8F0; P0A8F0: upp; NbExp=5; IntAct=EBI-909572, EBI-909572;
CC -!- INDUCTION: By pyrimidine starvation.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X57104; CAA40388.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75551.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA16386.1; -; Genomic_DNA.
DR PIR; A65026; A65026.
DR RefSeq; NP_416993.2; NC_000913.3.
DR RefSeq; WP_001295473.1; NZ_STEB01000011.1.
DR PDB; 2EHJ; X-ray; 2.80 A; A/B/C/D=2-208.
DR PDBsum; 2EHJ; -.
DR AlphaFoldDB; P0A8F0; -.
DR SMR; P0A8F0; -.
DR BioGRID; 4261438; 30.
DR BioGRID; 851318; 1.
DR DIP; DIP-36228N; -.
DR IntAct; P0A8F0; 6.
DR STRING; 511145.b2498; -.
DR BindingDB; P0A8F0; -.
DR ChEMBL; CHEMBL2233621; -.
DR DrugCentral; P0A8F0; -.
DR SWISS-2DPAGE; P0A8F0; -.
DR jPOST; P0A8F0; -.
DR PaxDb; P0A8F0; -.
DR PRIDE; P0A8F0; -.
DR EnsemblBacteria; AAC75551; AAC75551; b2498.
DR EnsemblBacteria; BAA16386; BAA16386; BAA16386.
DR GeneID; 67416878; -.
DR GeneID; 946979; -.
DR KEGG; ecj:JW2483; -.
DR KEGG; eco:b2498; -.
DR PATRIC; fig|1411691.4.peg.4241; -.
DR EchoBASE; EB1308; -.
DR eggNOG; COG0035; Bacteria.
DR HOGENOM; CLU_067096_2_2_6; -.
DR InParanoid; P0A8F0; -.
DR OMA; TYATRMP; -.
DR PhylomeDB; P0A8F0; -.
DR BioCyc; EcoCyc:URACIL-PRIBOSYLTRANS-MON; -.
DR BioCyc; MetaCyc:URACIL-PRIBOSYLTRANS-MON; -.
DR BRENDA; 2.4.2.9; 2026.
DR SABIO-RK; P0A8F0; -.
DR UniPathway; UPA00574; UER00636.
DR EvolutionaryTrace; P0A8F0; -.
DR PRO; PR:P0A8F0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IDA:EcoCyc.
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; Direct protein sequencing;
KW Glycosyltransferase; GTP-binding; Magnesium; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="Uracil phosphoribosyltransferase"
FT /id="PRO_0000120824"
FT BINDING 78
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 130..138
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 198..200
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT MUTAGEN 131
FT /note="P->D: 60-fold reduction of the catalytic rate, and
FT large decrease in uracil-binding affinity."
FT /evidence="ECO:0000269|PubMed:10079076"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:2EHJ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2EHJ"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2EHJ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2EHJ"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2EHJ"
SQ SEQUENCE 208 AA; 22533 MW; EF74D6E5B0216DC6 CRC64;
MKIVEVKHPL VKHKLGLMRE QDISTKRFRE LASEVGSLLT YEATADLETE KVTIEGWNGP
VEIDQIKGKK ITVVPILRAG LGMMDGVLEN VPSARISVVG MYRNEETLEP VPYFQKLVSN
IDERMALIVD PMLATGGSVI ATIDLLKKAG CSSIKVLVLV AAPEGIAALE KAHPDVELYT
ASIDQGLNEH GYIIPGLGDA GDKIFGTK
