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CATH Superfamily 2.60.120.260

Galactose-binding domain-like

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:

"
Galactose-binding domain-like
".

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 35790: Carbohydrate binding family 6

There are 33 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
Endo-1,4-beta-xylanase. [EC: 3.2.1.8]
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
    		 188 A0A023ZY33 A0A023ZY33 A0A0B0HYN8 A0A0B0HYN8 A0A0B0HYN8 A0A0B0HYN8 A0A0C5VA54 A0A0C5VA54 A0A0C5VPR1 A0A0C5VPR1
    (178 more...)
    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.
    		 174 A0A078KN45 A0A078KN45 A0A080UVE0 A0A080UVE0 A0A090ZJW3 A0A090ZJW3 A0A0E3WIQ0 A0A0E3WIQ0 A0A0F6VYJ7 A0A0F6VYJ7
    (164 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.
    		 60 A0A095F6U3 A0A095F6U3 A0A0F0GSB5 A0A0F0GSB5 A0A0H3DEM0 A0A0H3DEM0 A0A0L6JPZ1 A0A0L6JPZ1 A0A0L8LGI4 A0A0L8LGI4
    (50 more...)
    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.
      		 34 A0A0P4UCK5 A0A0P4UCK5 A0A1E3L162 A0A1E3L162 B5YAS3 B5YAS3 B8DYX7 B8DYX7 C6KL35 C6KL35
      (24 more...)
      Glucan endo-1,3-beta-D-glucosidase. [EC: 3.2.1.39]
      Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
      • Very limited action on mixed-link (1->3,1->4)-beta-D-glucans.
      • Hydrolyzes laminarin, paramylon and pachyman.
      • Different from EC 3.2.1.6.
      		 32 A0A0N0MZZ5 A0A0N0MZZ5 A0A0T9MR56 A0A0T9MR56 A0A0U5LTB6 A0A0U5LTB6 A0A100J6Q5 A0A100J6Q5 A0A100JTU6 A0A100JTU6
      (22 more...)
      Beta-agarase. [EC: 3.2.1.81]
      Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product.
      • Also acts on porphyran, but more slowly.
      • Cleaves the beta-(1->4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place.
      • The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB.
      		 32 A0A059XEP7 A0A059XEP7 A0A059XK55 A0A059XK55 A0A059XK55 A0A059XK55 A0A090S773 A0A090S773 D5EIK7 D5EIK7
      (22 more...)
      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.
      		 28 A0A075UYG8 A0A075UYG8 A0A0K3BDF5 A0A0K3BDF5 A0A0L8V461 A0A0L8V461 A0A0P4UCK5 A0A0P4UCK5 A0A1B2TXE9 A0A1B2TXE9
      (18 more...)
      Alpha-D-xyloside xylohydrolase. [EC: 3.2.1.177]
      Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
      • The enzyme catalyzes hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide.
      • Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
      		 24 A0A0E9DS52 A0A0E9DS52 A0A174GYF4 A0A174GYF4 A0A174H1V1 A0A174H1V1 A0A174H1V1 A0A174H1V1 A0A174RCP2 A0A174RCP2
      (14 more...)
      Xylan 1,4-beta-xylosidase. [EC: 3.2.1.37]
      Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
      • Also hydrolyzes xylobiose.
      • Some other exoglycosidase activities have been found associated with this enzyme in sheep liver.
      		 22 A0A077XM08 A0A077XM08 A0A0E4HCE7 A0A0E4HCE7 A0A0H5SWN3 A0A0H5SWN3 A0A1B1YC13 A0A1B1YC13 A0A1B1YJ57 A0A1B1YJ57
      (12 more...)
      Beta-glucosidase. [EC: 3.2.1.21]
      Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
      • Wide specificity for beta-D-glucosides.
      • Some examples also hydrolyze one or more of the following: beta-D- galactosides, alpha-L-arabinosides, beta-D-xylosides and beta-D- fucosides.
      		 22 A0A0S2I2Y1 A0A0S2I2Y1 A0A173MZS9 A0A173MZS9 A0A1C5N4N1 A0A1C5N4N1 A0A1C5N4N1 A0A1C5N4N1 A0A1C5RZ91 A0A1C5RZ91
      (12 more...)
      Cycloisomaltooligosaccharide glucanotransferase. [EC: 2.4.1.248]
      Cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)- alpha-D-glucosidic bond.
      • Specific for (1->6)-alpha-D-glucans (dextrans) and, unlike cyclomaltodextrin glucanotransferase (EC 2.4.1.19), without activity toward (1->4)-alpha-D-glucans, such as amylose.
      • It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points.
      • The enzyme from Bacillus circulans T-3040 has been shown to form cycloisomalto-oligosaccharides of three sizes (7, 8 and 9 glucose units).
      • It will also catalyze the disproportionation of two isomalto- oligosaccharides molecules to yield a series of isomalto- oligosachharides and the addition of D-glucose to cycloisomalto- oligosaccharides with ring opening to form isomalto-oligosaccharides.
      		 22 A0A124C3S2 A0A124C3S2 A0A163S2Z1 A0A163S2Z1 A0A177I0J1 A0A177I0J1 A0A1B9ETX3 A0A1B9ETX3 A0A1D2ICW9 A0A1D2ICW9
      (12 more...)
      Pectate disaccharide-lyase. [EC: 4.2.2.9]
      Eliminative cleavage of 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D- galacturonate from the reducing end of pectate, i.e. de-esterified pectin.
        		 18 A0A0N1GSN4 A0A0N1GSN4 A0A0T9M2Y6 A0A0T9M2Y6 A0A100J3N2 A0A100J3N2 A0A124C508 A0A124C508 A0A177HUG2 A0A177HUG2
        (8 more...)
        Pectinesterase. [EC: 3.1.1.11]
        Pectin + n H(2)O = n methanol + pectate.
          		 16 A0A066WXR5 A0A066WXR5 A0A098LKC0 A0A098LKC0 A0A0L6JWT8 A0A0L6JWT8 A0A173MGD9 A0A173MGD9 C5BK67 C5BK67
          (6 more...)
          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.
          		 14 A0A1M6A2U5 A0A1M6A2U5 A0A1M7YXW9 A0A1M7YXW9 B3PDE6 B3PDE6 B3PJ22 B3PJ22 B5JCV6 B5JCV6
          (4 more...)
          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.
          		 14 A0A0S2FMW0 A0A0S2FMW0 A0A1M5XQ78 A0A1M5XQ78 A0A1M7Z308 A0A1M7Z308 A0A1N6M4U7 A0A1N6M4U7 G8S095 G8S095
          (4 more...)
          Exo-1,4-beta-D-glucosaminidase. [EC: 3.2.1.165]
          Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.
          • Chitosan is a partially or totally N-deacetylated chitin derivative that is found in the cell walls of some phytopathogenic fungi and comprises D-glucosamine residues with a variable content of GlcNAc residues.
          • Acts specifically on chitooligosaccharides and chitosan, having maximal activity on chitotetraose, chitopentaose and their corresponding alcohols.
          • Can degrade GlcN-GlcNAc but not GlcNAc-GlcNAc.
          		 10 A0A075URR6 A0A075URR6 A0A0F0LBL3 A0A0F0LBL3 A0A0U0Z2R8 A0A0U0Z2R8 A0A1C6HFK4 A0A1C6HFK4 Q56F26 Q56F26
          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.
          		 8 A0A0B0I8R1 A0A0B0I8R1 A0A1B2U3S3 A0A1B2U3S3 F7PGE0 F7PGE0 J1ADI5 J1ADI5
          Alpha-agarase. [EC: 3.2.1.158]
          Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product.
          • The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate.
          • The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer.
          • While the enzyme can also hydrolyze the highly sulfated agarose porphyran very efficiently, it cannot hydrolyze kappa-carrageenan and iota-carrageenan.
          		 8 A1IGV8 A1IGV8 A1IGV8 A1IGV8 Q9LAP7 Q9LAP7 Q9LAP7 Q9LAP7
          Endo-1,3(4)-beta-glucanase. [EC: 3.2.1.6]
          Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.
          • Substrates include laminarin, lichenin and cereal D-glucans.
          • Different from EC 3.2.1.39 and EC 3.2.1.52.
          		 8 E8U3C3 E8U3C3 F4H5F6 F4H5F6 Q8GRB4 Q8GRB4 Q8GRB4 Q8GRB4
          Glucan endo-1,6-beta-glucosidase. [EC: 3.2.1.75]
          Random hydrolysis of (1->6)-linkages in (1->6)-beta-D-glucans.
          • Acts on lutean, pustulan and 1,6-oligo-beta-D-glucosides.
          		 6 E0IBL6 E0IBL6 E6TQX1 E6TQX1 E8U461 E8U461
          Glycoprotein endo-alpha-1,2-mannosidase. [EC: 3.2.1.130]
          Hydrolysis of the terminal alpha-D-glucosyl-(1,3)-D-mannosyl unit from the GlcMan(9)(GlcNAc)(2) oligosaccharide component of the glycoprotein produced in the Golgi membrane.
          • Involved in the synthesis of glycoproteins.
          		 4 G0PU30 G0PU30 K4QVU5 K4QVU5
          Glucosylceramidase. [EC: 3.2.1.45]
          D-glucosyl-N-acylsphingosine + H(2)O = D-glucose + N-acylsphingosine.
          • Also acts on glucosylsphingosine (cf. EC 3.2.1.62).
          		 4 G8SK34 G8SK34 I0K2D7 I0K2D7
          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.
          		 4 B3PEI0 B3PEI0 B3PEI5 B3PEI5
          Glucan 1,3-beta-glucosidase. [EC: 3.2.1.58]
          Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.
          • Acts on oligosaccharides, but very slowly on laminaribiose.
          		 4 B3PEK3 B3PEK3 I3IDC0 I3IDC0
          Exo-alpha-sialidase. [EC: 3.2.1.18]
          Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
          • The enzyme does not act on 4-O-acetylated sialic acids.
          • An endo-alpha-sialidase activity is listed as EC 3.2.1.129.
          • See also EC 4.2.2.15.
          		 4 A0A1B1QMT8 A0A1B1QMT8 A0A1B1QMT8 A0A1B1QMT8
          Arabinan endo-1,5-alpha-L-arabinosidase. [EC: 3.2.1.99]
          Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)- arabinans.
          • Acts best on linear 1,5-alpha-L-arabinan.
          • Also acts on branched arabinan, but more slowly.
          		 2 A0A1E3L931 A0A1E3L931
          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.
          		 2 F1TBY8 F1TBY8
          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.
          		 2 C9RIW3 C9RIW3
          Glucan 1,6-alpha-isomaltosidase. [EC: 3.2.1.94]
          Hydrolysis of (1->6)-alpha-D-glucosidic linkages in polysaccharides, to remove successive isomaltose units from the non-reducing ends of the chains.
          • Optimum activity is on those 1,6-alpha-D-glucans containing 6, 7 and 8 glucose units; those containing 3, 4 and 5 glucose units are hydrolyzed at slower rates.
          		 2 Q44052 Q44052
          Quinoprotein glucose dehydrogenase (PQQ, quinone). [EC: 1.1.5.2]
          D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol.
          • Integral membrane protein containing PQQ as prosthetic group.
          • It also contains bound ubiquinone and Mg(2+) or Ca(2+).
          • Electron acceptor is membrane ubiquinone but usually assayed with phenazine methosulfate.
          • Like in all other quinoprotein alcohol dehydrogenases the catalytic domain has an 8-bladed 'propeller' structure.
          • It occurs in a wide range of bacteria.
          • Catalyzes a direct oxidation of the pyranose form of D-glucose to the lactone and thence to D-gluconate in the periplasm.
          • Oxidizes other monosaccharides including the pyranose forms of pentoses.
          • Formerly EC 1.1.99.17.
          		 2 A0A178X7K7 A0A178X7K7
          Peptidyl-Asp metalloendopeptidase. [EC: 3.4.24.33]
          Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds.
          • A metalloenzyme isolated from Pseudomonas fragi.
          • Useful in protein sequencing applications because of its limited specificity.
          • Belongs to peptidase family M72.
          		 2 Q21DP7 Q21DP7
          Hyaluronoglucosaminidase. [EC: 3.2.1.35]
          Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
          • Also hydrolyzes 1,4-beta-D-glycosidic linkages between N-acetyl- galactosamine or N-acetylgalactosamine sulfate and glucuronic acid in chondroitin, chondroitin 4- and 6-sulfates, and dermatan.
          • Formerly EC 3.2.1.34.
          		 2 A0A1C5SLB9 A0A1C5SLB9
          Rhamnogalacturonan endolyase. [EC: 4.2.2.23]
          Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D- galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non- reducing end.
          • The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168 and Aspergillus aculeatus.
          		 2 A0A085FTD3 A0A085FTD3
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