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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 13847: Alpha-amylase, putative (AFU_orthologue AFUA_2G134...

There are 10 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
Alpha-amylase. [EC: 3.2.1.1]
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
  • Acts on starch, glycogen and related polysaccharides and oligosaccharides in a random manner; reducing groups are liberated in the alpha-configuration.
  • The term 'alpha' relates to the initial anomeric configuration of the free sugar group released and not to the configuration of the linkage hydrolyzed.
 2748 A0A011Q7A6 A0A011Q7A6 A0A014M361 A0A014M361 A0A015P0M1 A0A015P0M1 A0A015SB54 A0A015SB54 A0A015ST55 A0A015ST55
(2738 more...)
1,4-alpha-glucan branching enzyme. [EC: 2.4.1.18]
Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.
  • Converts amylose into amylopectin.
  • The description (official name) requires a qualification depending on the product, glycogen or amylopectin, e.g. glycogen branching enzyme, amylopectin branching enzyme.
  • The latter has frequently been termed Q-enzyme.
 168 A0A066YFH3 A0A066YFH3 A0A076MFA6 A0A076MFA6 A0A081XUX4 A0A081XUX4 A0A086GXX1 A0A086GXX1 A0A0B5DK43 A0A0B5DK43
(158 more...)
Glucan 1,4-alpha-maltohexaosidase. [EC: 3.2.1.98]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltohexaose residues from the non- reducing chain ends.
  • Cf. EC 3.2.1.3, which removes successive glucose residues.
  • Cf. EC 3.2.1.2, which removes successive maltose residues.
  • Cf. EC 3.2.1.116, which removes successive maltotriose residues.
  • Cf. EC 3.2.1.60, which removes successive maltotetraose residues.
  • The products have the alpha-configuration.
 152 A0A069SFY6 A0A069SFY6 A0A069XJU7 A0A069XJU7 A0A099KBI7 A0A099KBI7 A0A0B7GPQ1 A0A0B7GPQ1 A0A0C7KBY0 A0A0C7KBY0
(142 more...)
Cyclomaltodextrinase. [EC: 3.2.1.54]
Cyclomaltodextrin + H(2)O = linear maltodextrin.
  • Also hydrolyzes linear maltodextrin.
  • Formerly EC 3.2.1.12 and EC 3.2.1.13.
 8 B9K7K5 B9K7K5 G4FGM1 G4FGM1 O86959 O86959 Q9X2F4 Q9X2F4
Pullulanase. [EC: 3.2.1.41]
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
  • Different from EC 3.2.1.142 in its action on glycogen, and its rate of hydrolysis of limit dextrins.
  • Its action on amylopectin is complete.
  • Maltose is the smallest sugar that it can release from an alpha- (1->6)-linkage.
  • Formerly EC 3.2.1.69.
 6 A0A1M4NCG7 A0A1M4NCG7 B0XUD0 B0XUD0 Q4WI35 Q4WI35
Neopullulanase. [EC: 3.2.1.135]
Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
  • Cf. EC 3.2.1.41 and EC 3.2.1.57.
 4 G4FGM1 G4FGM1 Q9X2F4 Q9X2F4
Glucan 1,4-alpha-maltotriohydrolase. [EC: 3.2.1.116]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotriose residues from the non- reducing chain ends.
  • Cf. EC 3.2.1.2, EC 3.2.1.60, and EC 3.2.1.98.
  • The products of all these enzymes have the alpha-configuration.
 4 A0A0F4YYN2 A0A0F4YYN2 A0A0N9MVA4 A0A0N9MVA4
Purine nucleosidase. [EC: 3.2.2.1]
A purine nucleoside + H(2)O = D-ribose + a purine base.
  • The enzyme from the bacterium Ochrobactrum anthropi specifically catalyzes the irreversible N-riboside hydrolysis of purine nucleosides.
  • Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD(+), NADP(+) and nicotinaminde mononucleotide are not substrates.
 4 A0A1L6Z980 A0A1L6Z980 Q59222 Q59222
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.
 2 P07190 P07190
Glucan 1,4-alpha-maltohydrolase. [EC: 3.2.1.133]
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains.
  • Acts on starch and related polysaccharides and oligosaccharides.
  • The product is alpha-maltose; cf. EC 3.2.1.2.
 2 P32818 P32818
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