| Type: | Domain | Name: | Pullulanase, extracellular |
| Description: | Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterised members of this family include a surface-located pullulanase from Streptococcus pneumoniae[] and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity []. | Short Name: | Pullulan_Gpos |
| DB identifier | Type | Name |
|---|---|---|
| IPR006047 | Domain | Glycosyl hydrolase, family 13, catalytic domain |
| IPR004193 | Domain | Glycoside hydrolase, family 13, N-terminal |
| IPR013783 | Domain | Immunoglobulin-like fold |
| IPR019931 | Domain | LPXTG cell wall anchor domain |
| IPR005323 | Domain | Bacterial pullanase-associated domain |
| IPR019948 | Domain | Gram-positive anchor |
