CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
4 | Few Secondary Structures |
|
4.10 | Irregular |
|
4.10.320 | Dihydrolipoamide Transferase |
|
4.10.320.10 | E3-binding domain |
Domain Context
CATH Clusters
| Superfamily | E3-binding domain |
| Functional Family | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex |
Enzyme Information
| 2.3.1.61 |
Dihydrolipoyllysine-residue succinyltransferase.
based on mapping to UniProt P0AFG6
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)- (S-succinyldihydrolipoyl)lysine.
-!- A multimer (24-mer) of this enzyme forms the core of the multienzyme complex, and binds tightly both EC 1.2.4.2 and EC 1.8.1.4. -!- The lipoyl group of this enzyme is reductively succinylated by EC 1.2.4.2, and the only observed direction catalyzed by EC 2.3.1.61 is that where this succinyl group is passed to coenzyme A.
|
UniProtKB Entries (1)
| P0AFG6 |
ODO2_ECOLI
Escherichia coli K-12
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
|
PDB Structure
| PDB | 2WXC |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
The Folding Mechanism of Bbl: Plasticity of Transition-State Structure Observed within an Ultrafast Folding Protein Family.
J.Mol.Biol.
|