CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
| Superfamily | Dihydrodipicolinate Reductase; domain 2 |
| Functional Family | 4-hydroxy-tetrahydrodipicolinate reductase |
Enzyme Information
| 1.17.1.8 |
4-hydroxy-tetrahydrodipicolinate reductase.
based on mapping to UniProt Q9K1F1
(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H.
-!- Studies of the enzyme from the bacterium Escherichia coli have shown that the enzyme accepts (2S,4S)-4-hydroxy-2,3,4,5- tetrahydrodipicolinate and not (S)-2,3-dihydrodipicolinate as originally thought. -!- Formerly EC 1.3.1.26.
|
UniProtKB Entries (1)
| Q9K1F1 |
DAPB_NEIMB
Neisseria meningitidis MC58
4-hydroxy-tetrahydrodipicolinate reductase
|
PDB Structure
| PDB | 5UGJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly.
Biochem. J.
|
