Description

IPR006047 is a Glycosyl hydrolase family 13, catalytic domain.

<p>Enzymes containing this domain, such as alpha-amylase, belong to family 13 ([cazy:GH13]) of the glycosyl hydrolases. The maltogenic alpha-amylase is an enzyme that catalyses the 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 in the conversion of starch to maltose. Other enzymes include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins.</p> <p>This entry represents the catalytic domain found in several protein members of this family. It has a structure consisting of an 8-stranded α/β barrel that contains the active site, interrupted by a ~70 amino acid calcium-binding domain protruding between β-strand 3 and α-helix 3, and a carboxyl-terminal β-barrel domain [[cite:PUB00027665]].</p> <p>Family GH13 is the major glycoside hydrolase family acting on substrates containing α-glucoside linkages. GH13 contains hydrolases, transglycosidases, and isomerases [[cite:PUB00047252]]; noticeably, animal amino acid transporters [[cite:PUB00060751]], which have no glycosidase activity [[cite:PUB00128908]], are also GH13 members. The enzymes are found in a very wide range of organisms from all kingdoms. The GH13 enzymes have a wide range of different preferred substrates and products. For example, the α-amylases prefer polysaccharides of the α-1,4-glucan type, such as amylose and amylopectin, but are also able to attack the supramolecular structures represented by starch granules and glycogen particles. Among thousands of sequences and ~30 different enzyme specificities [[cite:PUB00080589]] many are closely related to each other; GH13 therefore has officially been subdivided into almost 40 subfamilies [[cite:PUB00119822]]. In general, the GH13 members are multidomain proteins with catalytic (β/α)8-barrel (i.e. TIM-barrel) domain (called domain A) having a small domain B (usually varying in length and of irregular structure) [[cite:PUB00047252]]. Some of these enzymes include:</p> <ul><li>α-amylase [ec:3.2.1.1]</li> <li>oligo-1,6-glucosidase [ec:3.2.1.10]</li> <li>α-glucosidase [ec:3.2.1.20]</li> <li>pullulanase [ec:3.2.1.4]</li> <li>cyclomaltodextrinase [ec:3.2.1.54]</li> <li>maltotetraose-forming α-amylase [ec:3.2.1.60]</li> <li>isoamylase [ec:3.2.1.68]</li> <li>dextran glucosidase [ec:3.2.1.70]</li> <li>trehalose-6-phosphate hydrolase [ec:3.2.1.93]</li> <li>maltohexaose-forming α-amylase [ec:3.2.1.9])</li> <li>maltotriose-forming α-amylase [ec:3.2.1.116]</li> <li>maltogenic amylase [ec:3.2.1.133]</li> <li>neopullulanase [ec:3.2.1.135]</li> <li>malto-oligosyltrehalose trehalohydrolase [ec:3.2.1.141]</li> <li>limit dextrinase [ec:3.2.1.142]</li> <li>amylosucrase [ec:2.4.1.4]</li> <li>sucrose phosphorylase [ec:2.4.1.7]</li> <li>cyclomaltodextrin glucanotransferase (CGTase) [ec:2.4.1.19]</li> <li>4-α-glucanotransferase [ec:2.4.1.25]</li> <li>isomaltulose synthase [ec:5.4.99.11]</li> <li>trehalose synthase [ec:5.4.99.16]</li></ul> <p>O-Glycosyl hydrolases ([ec:3.2.1.]) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [[cite:PUB00004870], [cite:PUB00005266]]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) website.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 45

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: