EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.7.B5 | - |
Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.7.B5 | additional information | construction of two truncated forms of ThiI containing the N-terminal domain including NFLD and THUMP, and the C-terminal domain including the PP-loop and RLD domains, respectively. The N-domain can bind with both tRNAPhe and TPHE39A and recognizes the acceptor-stem region, whereas the C-domain cannot. The C-domain also affects RNA binding by its enthalpically favorable, but entropically unfavorable, contribution. The C-domain induces a conformation change in tRNAPhe | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.7.B5 | Escherichia coli | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.7.7.B5 | tRNA-uridine + ATP = adenylated-trNA-uridine + diphosphate | RNA binding mechanism of ThiI in which the N-terminal domain recognizes the acceptor-stem region and the C-terminal region causes a conformational change of RNA | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.7.B5 | ATP + TPHE39A | truncated tRNA consisting of 39 nucleotides derived from tRNAPhe, minimal RNA substrate for modification by ThiI. The crystal structure of TPHE39A shows that base pairs in the T-stem are almost completely disrupted, although those in the acceptor-stem are preserved. ThiI can efficiently bind with not only tRNAPhe but also TPHE39A | Escherichia coli | adenylated TPHE39A + diphosphate | - |
? |