CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.150 | Divalent-metal-dependent TIM barrel enzymes |
Domain Context
CATH Clusters
| Superfamily | Divalent-metal-dependent TIM barrel enzymes |
| Functional Family |
Enzyme Information
| 5.3.1.14 |
L-rhamnose isomerase.
based on mapping to UniProt Q9KCL9
L-rhamnopyranose = L-rhamnulose.
-!- The enzyme binds the closed ring form of the substrate and catalyzes ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. -!- Isomerization proceeds via a hydride-shift mechanism. -!- While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyzes the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose.
|
UniProtKB Entries (1)
| Q9KCL9 |
RHAA_BACHD
Bacillus halodurans C-125
L-rhamnose isomerase
|
PDB Structure
| PDB | 3UXI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure-based studies on the metal binding of two-metal-dependent sugar isomerases.
Febs J.
|
