{"metadata":{"accession":"IPR040042","entry_id":null,"type":"family","go_terms":[{"identifier":"GO:0003844","name":"1,4-alpha-glucan branching enzyme activity","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0030979","name":"alpha-glucan biosynthetic process","category":{"code":"P","name":"biological_process"}}],"source_database":"interpro","member_databases":{"panther":{"PTHR41695":"1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED"}},"integrated":null,"hierarchy":{"accession":"IPR040042","name":"1,4-alpha-glucan branching enzyme MT3115-like","type":"Family","children":[{"accession":"IPR048145","name":"1,4-alpha-glucan branching enzyme TTHA1902","type":"Family","children":[]}]},"name":{"name":"1,4-alpha-glucan branching enzyme MT3115-like","short":"Branching_enz_MT3115-like"},"description":[{"text":"<p>This entry consists of 1,4-alpha-glucan branching enzymes. Branching enzymes (BEs) generally belong to glycoside hydrolase family 13 (GH13); however this group belongs to the GH57 family. This enzyme catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position [[cite:PUB00090452], [cite:PUB00090453]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00090452":{"PMID":21097495,"ISBN":null,"volume":"286","issue":"5","year":2011,"title":"Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed.","URL":null,"raw_pages":"3520-30","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Palomo M","Pijning T","Booiman T","Dobruchowska JM","van der Vlist J","Kralj S","Planas A","Loos K","Kamerling JP","Dijkstra BW","van der Maarel MJ","Dijkhuizen L","Leemhuis H."],"DOI_URL":"https://doi.org/10.1074/jbc.M110.179515"},"PUB00090453":{"PMID":16885460,"ISBN":null,"volume":"188","issue":"16","year":2006,"title":"A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.","URL":null,"raw_pages":"5915-24","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Murakami T","Kanai T","Takata H","Kuriki T","Imanaka T."],"DOI_URL":"https://doi.org/10.1128/JB.00390-06"}},"set_info":null,"overlaps_with":[{"accession":"IPR027291","name":"Glycoside hydrolase 38, N-terminal domain superfamily","type":"homologous_superfamily"},{"accession":"IPR011330","name":"Glycoside hydrolase/deacetylase, beta/alpha-barrel","type":"homologous_superfamily"},{"accession":"IPR037090","name":"Glycoside hydrolase families 57, central domain","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":2698,"pathways":3,"proteins":2698,"proteomes":1759,"sets":0,"structural_models":{"alphafold":2124,"bfvd":0},"structures":7,"taxa":3714},"entry_annotations":{},"cross_references":{"ec":{"displayName":"ENZYME","description":"ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.","rank":19,"accessions":[{"accession":"2.4.1.18","url":"https://enzyme.expasy.org/EC/2.4.1.18"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"3n98","name":"Crystal structure of TK1436, a GH57 branching enzyme from hyperthermophilic archaeon Thermococcus kodakaraensis, in complex with glucose and additives"}}}