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CATH Superfamily 2.60.40.1180

Golgi alpha-mannosidase II

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:

"
Golgi alpha-mannosidase II
".

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 13705: Glucan 1,6-alpha-glucosidase

There are 4 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
Glucan 1,6-alpha-glucosidase. [EC: 3.2.1.70]
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in (1->6)-alpha-D- glucans and derived oligosaccharides.
  • Hydrolysis is accompanied by inversion at C-1, so that new reducing ends are released in the beta-configuration.
  • Dextrans and isomaltosaccharides are hydrolyzed, as is isomaltose, but very slowly.
  • The enzyme from some sources also possesses the activity of EC 3.2.1.59.
 460 A0A064BZI2 A0A064BZI2 A0A081PNR0 A0A081PNR0 A0A081PWY7 A0A081PWY7 A0A081PYH7 A0A081PYH7 A0A081Q923 A0A081Q923
(450 more...)
Alpha-glucosidase. [EC: 3.2.1.20]
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
  • Group of enzymes whose specificity is directed mainly toward the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyze oligosaccharides rapidly, relative to polysaccharides, which are hydrolyzed relatively slowly, or not at all.
  • The intestinal enzyme also hydrolyzes polysaccharides, catalyzing the reactions of EC 3.2.1.3, and, more slowly, hydrolyzes 1,6-alpha-D- glucose links.
 10 A0A1N1YBI0 A0A1N1YBI0 E7S9L2 E7S9L2 E8K316 E8K316 J0YPS6 J0YPS6 Q9RIP4 Q9RIP4
Alpha,alpha-phosphotrehalase. [EC: 3.2.1.93]
Alpha,alpha-trehalose 6-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate.
    		 8 A0A0U0B726 A0A0U0B726 B1I961 B1I961 C1CBC1 C1CBC1 C1CCB5 C1CCB5
    Oligo-1,6-glucosidase. [EC: 3.2.1.10]
    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
    • This enzyme, like EC 3.2.1.33, can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41, EC 3.2.1.142, and EC 3.2.1.68 is maltose.
    • It also hydrolyzes isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin.
    • The enzyme from intestinal mucosa is a single polypeptide chain that also catalyzes the reaction of EC 3.2.1.48.
    • Differs from EC 3.2.1.33 in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
    		 4 A0A0C6G4S9 A0A0C6G4S9 Q99XX7 Q99XX7