CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.14 | L-fucose Isomerase; Chain A, domain 3 |
|
3.20.14.10 | L-fucose/L-arabinose isomerase, C-terminal |
Domain Context
CATH Clusters
| Superfamily | L-fucose/L-arabinose isomerase, C-terminal |
| Functional Family | L-fucose isomerase |
Enzyme Information
| 5.3.1.25 |
L-fucose isomerase.
based on mapping to UniProt P69922
L-fucopyranose = L-fuculose.
-!- The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene- diol mechanism. -!- The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose. -!- The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose.
|
| 5.3.1.3 |
D-arabinose isomerase.
based on mapping to UniProt P69922
D-arabinose = D-ribulose.
-!- The enzyme binds the closed form of the sugar and catalyzes ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene- diol mechanism. -!- The enzyme catalyzes the aldose-ketose isomerization of several sugars. -!- Most enzymes also catalyze the reaction of EC 5.3.1.25. -!- The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose. -!- Cf. EC 5.3.1.4.
|
UniProtKB Entries (1)
| P69922 |
FUCI_ECOLI
Escherichia coli K-12
L-fucose isomerase
|
PDB Structure
| PDB | 1FUI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure and mechanism of L-fucose isomerase from Escherichia coli.
J.Mol.Biol.
|