{"metadata":{"accession":"PF11852","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR024561","hierarchy":null,"name":{"name":"Alpha-1,6-glucosidases, pullulanase-type, C-terminal","short":"Pullul_strch_C"},"description":[{"text":"<p>This entry represents the uncharacterised C-terminal domain of secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants [[cite:PUB00097791]]. Both enzymes hydrolyse alpha-1,6 glycosidic linkages. 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.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00097791":{"PMID":18815382,"ISBN":null,"volume":"148","issue":"3","year":2008,"title":"Further evidence for the mandatory nature of polysaccharide debranching for the aggregation of semicrystalline starch and for overlapping functions of debranching enzymes in Arabidopsis leaves.","URL":null,"raw_pages":"1309-23","medline_journal":"Plant Physiol","ISO_journal":"Plant Physiol","authors":["Wattebled F","Planchot V","Dong Y","Szydlowski N","Pontoire B","Devin A","Ball S","D'Hulst C."],"DOI_URL":null}},"set_info":{"accession":"CL0369","name":"GHD"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":143,"interactions":0,"matches":3256,"pathways":0,"proteins":3239,"proteomes":2756,"sets":1,"structural_models":{"alphafold":1099},"structures":28,"taxa":4152},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":60,"alignment:full":1572},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}