{"metadata":{"accession":"PF09318","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR015397","hierarchy":null,"name":{"name":"Glycosyl transferase 1 domain A","short":"Glyco_trans_A_1"},"description":[{"text":"<p>Glyco_trans_A_1 is family of found predominantly at the N-terminus of various prokaryotic alpha-glucosyltransferases. According to whether the domain exists as a whole molecule or as a half molecule determines the number of sugar residues that the molecule transfers. Two-domain proteins are processive in that they transfer more than one sugar residue, processively; single domain proteins transfer just one sugar moiety [[cite:PUB00075675],[cite:PUB00064844]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00075675":{"PMID":7883697,"ISBN":null,"volume":"177","issue":"6","year":1995,"title":"Multidomain architecture of beta-glycosyl transferases: implications for mechanism of action.","URL":null,"raw_pages":"1419-24","medline_journal":"J Bacteriol","ISO_journal":"J. Bacteriol.","authors":["Saxena IM","Brown RM Jr","Fevre M","Geremia RA","Henrissat B."],"DOI_URL":null},"PUB00064844":{"PMID":21862581,"ISBN":null,"volume":"286","issue":"40","year":2011,"title":"A molecular chaperone mediates a two-protein enzyme complex and glycosylation of serine-rich streptococcal adhesins.","URL":null,"raw_pages":"34923-31","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Wu R","Wu H."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M111.239350"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":4,"interactions":0,"matches":67,"pathways":0,"proteins":67,"proteomes":64,"sets":0,"structural_models":{"alphafold":39},"structures":0,"taxa":123},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":1,"alignment:full":24},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}