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CATH Superfamily 1.10.1330.10

Dockerin domain

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:

"
Dockerin domain
".

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 775: Carbohydrate binding family 6

There are 16 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
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.
 47 A0A0U5JRH0 A0A1E3BWR9 A0A1E3BXN6 A0A1E3BXR7 A0A1E3BZ32 A0A1E3C3C4 A3DBF5 A3DC29 A3DC34 A3DCG4
(37 more...)
Endo-1,4-beta-xylanase. [EC: 3.2.1.8]
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
    		 44 A0A173M083 A0A1E3BW67 A0A1E3C055 A0A1E3C0F8 A0A1E3C2D9 A0A1E3C3B7 A0A1E3C3D4 A0A1K1LJJ6 A3DDW7 A3DGI0
    (34 more...)
    Alpha-galactosidase. [EC: 3.2.1.22]
    Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha- D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
    • Also hydrolyzes alpha-D-fucosides.
    		 9 B8I0L8 B8I2F6 F1T8Q0 F1TDA1 H2JC34 H2JDC4 Q0PRN2 Q8VV86 U4R6T5
    Arabinogalactan endo-beta-1,4-galactanase. [EC: 3.2.1.89]
    The enzyme specifically hydrolyzes (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.
    • This enzyme, isolated from the bacterium Bacillus subtilis, hydrolyzes the beta(1->4) bonds found in type I plant arabinogalactans, which are a component of the primary cell walls of dicots.
    • The predominant product is a tetrasaccharide.
    • Cf. EC 3.2.1.181.
    		 6 A0A1E3BYZ4 A3DFA2 B8I434 G8LST5 H2JFK1 W4V323
    Mannan endo-1,4-beta-mannosidase. [EC: 3.2.1.78]
    Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
      		 6 D9SS67 F1TDF6 Q9F1T9 Q9LAJ3 Q9REC7 W6S145
      Pectinesterase. [EC: 3.1.1.11]
      Pectin + n H(2)O = n methanol + pectate.
        		 6 A0A1E3C265 A3DJL8 F1T8R0 G8LWH5 H2JDD4 U4QZD7
        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.
          		 4 A3DCH1 G8M3C3 O65986 P0C2S1
          Licheninase. [EC: 3.2.1.73]
          Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
          • Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
          		 2 A3DBX3 Q84C00
          Non-reducing end alpha-L-arabinofuranosidase. [EC: 3.2.1.55]
          Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
          • Acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans.
          • Some EC 3.2.1.23 and EC 3.2.1.38 enzymes also hydrolyze alpha-L- arabinosides.
          • cf. EC 3.2.1.185.
          • Formerly EC 3.2.1.79.
          		 2 F1T8P9 F1TAH5
          Cellulose 1,4-beta-cellobiosidase (reducing end). [EC: 3.2.1.176]
          Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
          • Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48), act at the reducing ends of cellulose and similar substrates.
          • The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism.
          • It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism.
          • Different from EC 3.2.1.91, which attacks cellulose from the non- reducing end.
          		 2 A3DH67 P0C2S5
          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.
          		 2 R7NL76 R7NNJ4
          Chitinase. [EC: 3.2.1.14]
          Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta- linkages in chitin and chitodextrins.
          • The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo- chitodextrinases can act.
          • Activity is greatly stimulated in the presence of EC 1.14.99.53, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase.
          • Cf. EC 3.2.1.202.
          		 1 Q59326
          Pectate lyase. [EC: 4.2.2.2]
          Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
          • Favors pectate, the anion, over pectin, the methyl ester (which is the preferred substrate of EC 4.2.2.10).
          • Formerly EC 4.2.99.3.
          		 1 Q9AQF3
          Glucuronoarabinoxylan endo-1,4-beta-xylanase. [EC: 3.2.1.136]
          Endohydrolysis of (1->4)-beta-D-xylosyl links in some glucuronoarabinoxylans.
          • High activity toward feruloylated arabinoxylans from cereal plant cell walls.
          		 1 F1TBY8
          Thermitase. [EC: 3.4.21.66]
          Hydrolysis of proteins, including collagen.
          • From Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate.
          • The N-terminal extension of the polypeptide chain relative to subtilisin contributes to calcium-binding and the high thermostability.
          • The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus are closely similar.
          • Belongs to peptidase family S8.
          • Formerly EC 3.4.4.16.
          		 1 A0A0L6JJE0
          Acetylxylan esterase. [EC: 3.1.1.72]
          Deacetylation of xylans and xylo-oligosaccharides.
          • Catalyzes the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-napthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol.
          • Does not act on acetylated mannan or pectin.
          		 1 P10477