CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.605 | Aldehyde Dehydrogenase; Chain A, domain 1 |
|
3.40.605.10 | Aldehyde Dehydrogenase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aldehyde Dehydrogenase; Chain A, domain 1 |
| Functional Family |
Enzyme Information
| 1.2.1.88 |
L-glutamate gamma-semialdehyde dehydrogenase.
based on mapping to UniProt P30038
L-glutamate 5-semialdehyde + NAD(+) + H(2)O = L-glutamate + NADH.
-!- This enzyme catalyzes the irreversible oxidation of glutamate-gamma- semialdehyde to glutamate as part of the proline degradation pathway. -!- (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. -!- In many bacterial species, both activities are carried out by a single bifunctional enzyme. -!- The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1- pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)- 1-pyrroline-5-carboxylate is converted into D-glutamate. -!- NADP(+) can also act as acceptor, but with lower activity. -!- Formerly EC 1.5.1.12.
|
UniProtKB Entries (1)
| P30038 |
AL4A1_HUMAN
Homo sapiens
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 3V9I |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Three-Dimensional Structural Basis of Type II Hyperprolinemia.
J.Mol.Biol.
|
