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 named:

"
YVTN repeat-like/Quinoprotein amine dehydrogenase
".

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 104709: Probable oligoxyloglucan-reducing end-specific xyl...

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
Oligoxyloglucan reducing-end-specific cellobiohydrolase. [EC: 3.2.1.150]
Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted.
  • The enzyme is found in the fungus Geotrichum sp. M128.
  • The substrate is a hemicellulose found in plant cell walls.
6 A1DAU0 A1DAU0 Q5BD38 Q5BD38 Q8J0D2 Q8J0D2
Xyloglucan-specific exo-beta-1,4-glucanase. [EC: 3.2.1.155]
Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end.
  • The enzyme removes XXXG heptasaccharides, XXLG/XLXG octasaccharides and XLLG nonasaccharides from the end of tamarind seed xyloglucan polymers in a processive manner.
  • Hydrolysis occurs at the unsubstituted D-glucopyranose residue in the main backbone.
  • It is not known whether the cleavage takes place at the reducing or non-reducing end of the polymer.
  • Very low activity with beta-D-glucans.
  • The enzyme from Chrysosporium lucknowense shifts to an endoglucanase mode when acting on linear substrates without bulky substituents on the polymeric backbone such as barley beta-glucan.
  • Formerly EC 3.2.1.160.
5 A0A024S9Z6 A0A084FYA9 A0A0F8CR49 M5C9Y8 Q7Z9M8
Cellulose 1,4-beta-cellobiosidase (non-reducing end). [EC: 3.2.1.91]
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
    3 A0A084FYA9 D9TFH5 E4SDC8
    Xyloglucan-specific endo-beta-1,4-glucanase. [EC: 3.2.1.151]
    Xyloglucan + H(2)O = xyloglucan oligosaccharides.
    • The enzyme from Aspergillus aculeatus is specific for xyloglucan and does not hydrolyze other cell-wall components.
    • The reaction involves endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues.
    2 U6NE87 W6SKM0
    Cellulase. [EC: 3.2.1.4]
    Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
    • Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
    1 A0A084FYA9
    Endo-1,4-beta-xylanase. [EC: 3.2.1.8]
    Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
      1 A0A0S4K3C0