CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.10800 | NadA-like |
Domain Context
CATH Clusters
| Superfamily | NadA-like |
| Functional Family |
Enzyme Information
| 2.5.1.72 |
Quinolinate synthase.
based on mapping to UniProt Q9X1X7
Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate.
-!- Quinolinate synthase catalyzes the second step in the de novo biosynthesis of NAD(+) from aspartate in some bacteria, with EC 1.4.3.16 catalyzing the first step and EC 2.4.2.19 the third step. -!- In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme.
|
UniProtKB Entries (1)
| Q9X1X7 |
NADA_THEMA
Thermotoga maritima MSB8
Quinolinate synthase A
|
PDB Structure
| PDB | 4P3X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The crystal structure of Fe4S4 quinolinate synthase unravels an enzymatic dehydration mechanism that uses tyrosine and a hydrolase-type triad.
J.Am.Chem.Soc.
|