CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.20 | Up-down Bundle | |
1.20.1090 | Dehydroquinate synthase-like, alpha domain | |
1.20.1090.10 | Dehydroquinate synthase-like - alpha domain |
Domain Context
CATH Clusters
Superfamily | Dehydroquinate synthase-like - alpha domain |
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.
|
2.7.1.71 |
Shikimate kinase.
based on mapping to UniProt P07547
ATP + shikimate = ADP + shikimate 3-phosphate.
|
2.5.1.19 |
3-phosphoshikimate 1-carboxyvinyltransferase.
based on mapping to UniProt P07547
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- (1-carboxyvinyl)-3-phosphoshikimate.
|
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
|