CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.20 | Dihydropteroate synthase-like |
Domain Context
CATH Clusters
| Superfamily | Dihydropteroate synthase-like |
| Functional Family | Dihydropteroate synthase |
Enzyme Information
| 2.5.1.15 |
Dihydropteroate synthase.
based on mapping to UniProt P9WND1
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
-!- The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). -!- The enzyme exists in varying types of multifunctional proteins in different organisms. -!- The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.
|
UniProtKB Entries (1)
| P9WND1 |
DHPS1_MYCTU
Mycobacterium tuberculosis H37Rv
Dihydropteroate synthase
|
PDB Structure
| PDB | 1EYE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of Mycobacterium tuberculosis 7,8-dihydropteroate synthase in complex with pterin monophosphate: new insight into the enzymatic mechanism and sulfa-drug action.
J.Mol.Biol.
|
