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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 13763: Oligo-1,6-glucosidase 3

There are 11 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,alpha-phosphotrehalase. [EC: 3.2.1.93]
Alpha,alpha-trehalose 6-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate.
    		 1496 A0A010SMS2 A0A010SMS2 A0A011SJP7 A0A011SJP7 A0A022PFY9 A0A022PFY9 A0A023DD54 A0A023DD54 A0A023P0F7 A0A023P0F7
    (1486 more...)
    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.
    		 780 A0A023P9D1 A0A023P9D1 A0A062XNK2 A0A062XNK2 A0A068NAK4 A0A068NAK4 A0A076W4V4 A0A076W4V4 A0A080UMI6 A0A080UMI6
    (770 more...)
    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.
    		 686 A0A011RQ00 A0A011RQ00 A0A011SIV9 A0A011SIV9 A0A023CS34 A0A023CS34 A0A023DIB9 A0A023DIB9 A0A024P453 A0A024P453
    (676 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.
    		 96 A0A068N5L7 A0A068N5L7 A0A0B5NQK4 A0A0B5NQK4 A0A0D1RG34 A0A0D1RG34 A0A0D6S4M4 A0A0D6S4M4 A0A0F5RK19 A0A0F5RK19
    (86 more...)
    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.
    		 26 A0A090R4H2 A0A090R4H2 A0A174FI72 A0A174FI72 A0A1A7UFF4 A0A1A7UFF4 A0A1L8X4D4 A0A1L8X4D4 D4JKE2 D4JKE2
    (16 more...)
    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.
    		 18 A0A0B5WX61 A0A0B5WX61 A0A0D0EIX4 A0A0D0EIX4 A0A0D0FV39 A0A0D0FV39 A0A0D0G033 A0A0D0G033 A0A150K8X8 A0A150K8X8
    (8 more...)
    Dextranase. [EC: 3.2.1.11]
    Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran.
      		 18 A0A0E7XVV2 A0A0E7XVV2 A0A0F2CWJ4 A0A0F2CWJ4 A0A0F2DP45 A0A0F2DP45 A0A0F2DTT4 A0A0F2DTT4 A0A0F2E9N9 A0A0F2E9N9
      (8 more...)
      Starch synthase. [EC: 2.4.1.21]
      ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D- glucosyl)(n+1).
      • The description (accepted name) varies according to the source of the enzyme and the nature of its synthetic product, e.g. starch synthase, bacterial glycogen synthase.
      • A similar enzyme utilizes UDP-alpha-D-glucose (cf. EC 2.4.1.11).
      		 4 A0A1H5XC74 A0A1H5XC74 F5LNK8 F5LNK8
      Maltose alpha-D-glucosyltransferase. [EC: 5.4.99.16]
      Maltose = alpha,alpha-trehalose.
        		 2 A0A1C7FDU5 A0A1C7FDU5
        Glutamate racemase. [EC: 5.1.1.3]
        L-glutamate = D-glutamate.
          		 2 A5LNV9 A5LNV9
          4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase. [EC: 3.2.1.141]
          Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)- alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D- glucan.
            		 2 A0A151ABR7 A0A151ABR7