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 | L-rhamnose isomerase |
Enzyme Information
| 5.3.1.14 |
L-rhamnose isomerase.
based on mapping to UniProt P32170
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)
| P32170 |
RHAA_ECOLI
Escherichia coli K-12
L-rhamnose isomerase
|
PDB Structure
| PDB | 1D8W |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution.
J.Mol.Biol.
|
