| Primary Identifier | IPR044505 | Type | Domain |
| Short Name | GlgX_Isoamylase_N_E_set |
| description | This entry represents the N-terminal Early set domain found in bacterial glycogen debranching enzymes and isoamylases from bacteria and plants. Glycogen debranching enzymes have 4-alpha-glucanotransferase activity, that transfers a segment of the 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan, and amylo-1,6-glucosidase activity, which catalyses the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues []. Isoamylase is one of the starch-debranching enzymes that catalyse the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen [, ].This E or "early"set domains are associated with the catalytic domain of glycogen branching enzymes at the N-terminal end. The N-terminal domain of the 1,4 alpha glucan branching enzyme may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions []. |
