CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.150 | DNA polymerase; domain 1 |
|
1.10.150.290 | S-adenosyl-L-methionine-dependent methyltransferases |
Domain Context
CATH Clusters
| Superfamily | S-adenosyl-L-methionine-dependent methyltransferases |
| Functional Family |
Enzyme Information
| 2.1.1.144 |
Trans-aconitate 2-methyltransferase.
based on mapping to UniProt Q8UH15
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate.
-!- Also catalyzes the formation of the methyl monoester of cis- aconitate, isocitrate and citrate, but more slowly. -!- While the enzyme from Escherichia coli forms (E)-3-(methoxycarbonyl)- pent-2-enedioate as the product, that from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.145).
|
UniProtKB Entries (1)
| Q8UH15 |
TAM_AGRFC
Agrobacterium fabrum str. C58
Trans-aconitate 2-methyltransferase
|
PDB Structure
| PDB | 2P35 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens
To be Published
|