CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1300 | Pantoate--beta-alanine Ligase; Chain: A,domain 2 |
|
3.30.1300.20 | 7,8-dihydroneopterin aldolase (MptD) |
Domain Context
CATH Clusters
| Superfamily | 7,8-dihydroneopterin aldolase (MptD) |
| Functional Family |
Enzyme Information
| 4.1.2.25 |
Dihydroneopterin aldolase.
based on mapping to UniProt Q8TX89
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.
-!- The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. -!- The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8). -!- The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81. -!- The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15.
|
UniProtKB Entries (1)
| Q8TX89 |
MPTD_METKA
Methanopyrus kandleri AV19
Dihydroneopterin aldolase
|
PDB Structure
| PDB | 2IEC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of uncharacterized conserved archael protein from Methanopyrus kandleri
TO BE PUBLISHED
|