CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.287 | Helix Hairpins |
|
1.10.287.1150 | TPP helical domain |
Domain Context
CATH Clusters
| Superfamily | TPP helical domain |
| Functional Family |
Enzyme Information
| 2.2.1.5 |
2-hydroxy-3-oxoadipate synthase.
based on mapping to UniProt A0R2B1
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2).
-!- The product decarboxylates to 5-hydroxy-4-oxopentanoate. -!- The enzyme can decarboxylate 2-oxoglutarate. -!- Acetaldehyde can replace glyoxylate. -!- Formerly EC 4.1.3.15.
|
| 4.1.1.71 |
2-oxoglutarate decarboxylase.
based on mapping to UniProt A0R2B1
2-oxoglutarate = succinate semialdehyde + CO(2).
-!- Highly specific.
|
| 2.3.1.61 |
Dihydrolipoyllysine-residue succinyltransferase.
based on mapping to UniProt A0R2B1
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.
|
| 1.2.4.2 |
Oxoglutarate dehydrogenase (succinyl-transferring).
based on mapping to UniProt A0R2B1
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
-!- It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, which also binds multiple copies of EC 1.8.1.4. -!- It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
|
UniProtKB Entries (1)
| A0R2B1 |
KGD_MYCS2
Mycolicibacterium smegmatis MC2 155
Multifunctional 2-oxoglutarate metabolism enzyme
|
PDB Structure
| PDB | 3ZHQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A Dual Conformation of the Post-Decarboxylation Intermediate is Associated with Distinct Enzyme States in Mycobacterial Alpha-Ketoglutarate Decarboxylase (Kgd).
Biochem.J.
|
