CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1970 |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.1970 |
| Functional Family | Pentafunctional AROM polypeptide |
Enzyme Information
| 1.1.1.25 |
Shikimate dehydrogenase.
based on mapping to UniProt P07547
Shikimate + NADP(+) = 3-dehydroshikimate + NADPH.
-!- NAD(+) cannot replace NADP(+). -!- In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10.
|
| 4.2.1.10 |
3-dehydroquinate dehydratase.
based on mapping to UniProt P07547
3-dehydroquinate = 3-dehydroshikimate + H(2)O.
|
| 4.2.3.4 |
3-dehydroquinate synthase.
based on mapping to UniProt P07547
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.
-!- The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products. -!- Formerly EC 4.6.1.3.
|
| 2.5.1.19 |
3-phosphoshikimate 1-carboxyvinyltransferase.
based on mapping to UniProt P07547
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate.
|
| 2.7.1.71 |
Shikimate kinase.
based on mapping to UniProt P07547
ATP + shikimate = ADP + shikimate 3-phosphate.
|
UniProtKB Entries (1)
| P07547 |
ARO1_EMENI
Aspergillus nidulans FGSC A4
Pentafunctional AROM polypeptide
|
PDB Structure
| PDB | 1DQS |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis.
Nature
|
