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CATH Superfamily 2.60.120.200

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 25154: Glycosyl hydrolase, family 16

There are 6 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Beta-agarase. [EC: 3.2.1.81]
Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
  • Also acts on porphyran, but more slowly.
  • Cleaves the beta-(1->4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.
  • The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB.
 40 A0A0A0UT35 A0A0A0UT35 A0A0F7KPP2 A0A0F7KPP2 A0A0Q0G847 A0A0Q0G847 A0A1C3JGJ4 A0A1C3JGJ4 A4UMV9 A4UMV9
(30 more...)
Beta-porphyranase. [EC: 3.2.1.178]
Hydrolysis of beta-D-galactopyranose-(1->4)-alpha-L-galactopyranose-6- sulfate linkages in porphyran.
  • The backbone of porphyran consists largely (approximately 70%) of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked alpha- L-galactopyranose-6-sulfate (the other 30% are mostly agarobiose repeating units of (1->3)-linked beta-D-galactopyranose followed by (1->4)-linked 3,6-anhydro-alpha-L-galactopyranose).
  • This enzyme cleaves the (1->4) linkages between beta-D- galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D- galactose, although some longer oligosaccharides of even number of residues are also observed.
  • Since the enzyme is inactive on the non-sulfated agarose portion of the porphyran backbone, some agarose fragments are also included in the products.
  • Methylation of the D-galactose prevents its binding at position -1.
 8 B5CY92 B5CY92 D7GXF9 D7GXF9 D7GXG0 D7GXG0 D7GXG3 D7GXG3
Kappa-carrageenase. [EC: 3.2.1.83]
Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.
  • The main products of hydrolysis are neocarrabiose-sulfate and neocarratetraose-sulfate.
  • Unlike EC 3.2.1.157, but similar to EC 3.2.1.81, this enzyme proceeds with retention of the anomeric configuration.
 8 A0A0P9GMG3 A0A0P9GMG3 A0A0Q0HSL8 A0A0Q0HSL8 D5K195 D5K195 P43478 P43478
Keratan-sulfate endo-1,4-beta-galactosidase. [EC: 3.2.1.103]
Endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate.
  • Hydrolyzes the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N- acetyl-alpha-D-glucosaminyl residues.
  • Also acts on some non-sulfated oligosaccharides, but only acts on blood group substances when the 1,2-linked fucosyl residues have been removed (cf. EC 3.2.1.102).
 4 M5THW0 M5THW0 M5UCG7 M5UCG7
Exo-alpha-sialidase. [EC: 3.2.1.18]
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
  • The enzyme does not act on 4-O-acetylated sialic acids.
  • An endo-alpha-sialidase activity is listed as EC 3.2.1.129.
  • See also EC 4.2.2.15.
 2 A0A1B1QMT8 A0A1B1QMT8
Endo-1,3(4)-beta-glucanase. [EC: 3.2.1.6]
Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.
  • Substrates include laminarin, lichenin and cereal D-glucans.
  • Different from EC 3.2.1.39 and EC 3.2.1.52.
 2 A0A090VD72 A0A090VD72