CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.160 | 3 Solenoid |
|
2.160.20 | Pectate Lyase C-like |
|
2.160.20.10 | Single-stranded right-handed beta-helix, Pectin lyase-like |
Domain Context
CATH Clusters
| Superfamily | Single-stranded right-handed beta-helix, Pectin lyase-like |
| Functional Family |
Enzyme Information
| 3.2.1.157 |
Iota-carrageenase.
based on mapping to UniProt Q9F5I8
Endohydrolysis of 1,4-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose-2-sulfate in iota-carrageenans.
-!- The main products of hydrolysis are iota-neocarratetraose sulfate and iota-neocarrahexaose sulfate. -!- Iota-neocarraoctaose is the shortest substrate oligomer that can be cleaved. -!- Unlike EC 3.2.1.81 and EC 3.2.1.83, this enzyme proceeds with inversion of the anomeric configuration. -!- Iota-carrageenan differs from kappa-carrageenan by possessing a sulfo group on O-2 of the 3,6-anhydro-D-galactose residues, in addition to that present in the kappa-compound on O-4 of the D-galactose residues.
|
UniProtKB Entries (1)
| Q9F5I8 |
CGIA_ALTFO
Alteromonas sp. ATCC 43554
Iota-carrageenase
|
PDB Structure
| PDB | 1H80 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Iota-Carrageenase of Alteromonas Fortis. A Beta-Helix Fold-Containing Enzyme for the Degradation of a Highly Polyanionic Polysaccharide
J.Biol.Chem.
|
