CATH Classification
Domain Context
CATH Clusters
| Superfamily | 3.30.1130.10 |
| Functional Family | D-erythro-78-dihydroneopterin triphosphate epimerase FolX |
Enzyme Information
| 5.1.99.- |
Acting on other compounds.
based on mapping to UniProt P0AC19
|
| 5.-.-.- |
Isomerases.
based on mapping to UniProt P0AC19
|
| 4.1.2.25 |
Dihydroneopterin aldolase.
based on mapping to UniProt P0AC19
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)
| P0AC19 |
FOLX_ECOLI
Escherichia coli K-12
Dihydroneopterin triphosphate 2'-epimerase
|
PDB Structure
| PDB | 1B9L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of 7,8-dihydroneopterin triphosphate epimerase.
Structure Fold.Des.
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