CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.160 | 3 Solenoid |
|
2.160.10 | UDP N-Acetylglucosamine Acyltransferase; domain 1 |
|
2.160.10.10 | Hexapeptide repeat proteins |
Domain Context
CATH Clusters
| Superfamily | Hexapeptide repeat proteins |
| Functional Family | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase |
Enzyme Information
| 1.5.5.2 |
Proline dehydrogenase.
based on mapping to UniProt P9WP21
L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.
-!- The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor. -!- In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88. -!- Both activities are carried out by the same enzyme in enterobacteria. -!- Formerly EC 1.5.99.8.
|
| 2.3.1.117 |
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase.
based on mapping to UniProt P9WP21
Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate.
-!- Involved in the biosynthesis of lysine in bacteria, cyanobacteria and higher plants. -!- Earlier erroneously called 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase.
|
UniProtKB Entries (1)
| P9WP21 |
DAPD_MYCTU
Mycobacterium tuberculosis H37Rv
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
|
PDB Structure
| PDB | 3FSX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The three-dimensional Structure of a mycobacterial DapD provides insights into DapD diversity and reveals unexpected particulars about the enzymatic mechanism.
J.Mol.Biol.
|
