Application | Comment | Organism |
---|---|---|
pharmacology | potential target for the development of new antibiotics | [Bacillus] caldolyticus |
Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, overexpression in enzyme-deficient Escherichia coli | [Bacillus] caldolyticus |
Crystallization (Comment) | Organism |
---|---|
vapour diffusion using hanging or sitting drops, room temperature, protein solution 20 mg/ml, pH 7.0, 5 mM phosphate, 0.003 ml + 0.003 ml reservoir solution, pH 7.5, 6-10% polyethylene glycol 4000, 0.1 M HEPES, crystals appeared after 3 weeks, structure determination and analysis | [Bacillus] caldolyticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
[Bacillus] caldolyticus | P70881 | gene upp | - |
[Bacillus] caldolyticus | P70881 | strain DSM 405 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate | modelling of enzyme-5-phospho-alpha-D-ribose 1-diphosphate complex | [Bacillus] caldolyticus | |
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate | active sites pointing away from each other, a long arm from each monomer subunit wraps around the other subunit | [Bacillus] caldolyticus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
uracil + 5-phospho-alpha-D-ribose 1-diphosphate | 5-phospho-alpha-D-ribose 1-diphosphate binding site | [Bacillus] caldolyticus | UMP + diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
[Bacillus] caldolyticus |
More | three-dimensional structure | [Bacillus] caldolyticus |
More | monomer subunit fold with UMP | [Bacillus] caldolyticus |
More | 2 conserved sequences: Asp131-Ser139 contains the 5-phosphoribose 1-diphosphate binding motif and binds the ribose 5'-phosphate part of UMP, Tyr193-Ala201 is specific for uracil phosphoribosyltransferases and binds the uracil part of UMP | [Bacillus] caldolyticus |