{"metadata":{"accession":"PF13427","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR025184","hierarchy":null,"name":{"name":"Aminoglycoside adenylyltransferase, C-terminal domain","short":"AadA_C"},"description":[{"text":"<p>This domain is found at the C-terminal end of Aminoglycoside adenylyltransferase from Salmonella typhimurium (AadA) and other proteins associated with methicillin-resistant bacteria. AadA adenylates the 3''-hydroxyl group of the streptomycin glucosamine ring and the 9-hydroxyl group of the spectinomycin actinamine ring, mediating bacterial resistance to these antibiotics. This enzyme is organised into two domains: a N-terminal domain with a nucleotidyltransferase fold ([pfam:PF01909]) and a C-terminal domain (this entry) which consists of five alpha-helices forming an up-and-down alpha-helical bundle. This domain undergoes small conformational changes upon binding of ATP and magnesium that play a key role in the binding of the antibiotic compounds [[cite:PUB00091136],[cite:PUB00100854]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00100854":{"PMID":29871922,"ISBN":null,"volume":"293","issue":"29","year":2018,"title":"Structural mechanism of AadA, a dual-specificity aminoglycoside adenylyltransferase from <i>Salmonella enterica</i>.","URL":null,"raw_pages":"11481-11490","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Stern AL","Van der Verren SE","Kanchugal P S","Nasvall J","Gutierrez-de-Teran H","Selmer M."],"DOI_URL":null},"PUB00091136":{"PMID":26527143,"ISBN":null,"volume":"71","issue":"Pt 11","year":2015,"title":"Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3'')(9) adenyltransferase.","URL":null,"raw_pages":"2267-77","medline_journal":"Acta Crystallogr D Biol Crystallogr","ISO_journal":"Acta Crystallogr. D Biol. Crystallogr.","authors":["Chen Y","Nasvall J","Wu S","Andersson DI","Selmer M."],"DOI_URL":"https://doi.org/10.1107/S1399004715016429"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":27,"interactions":0,"matches":2850,"pathways":0,"proteins":2850,"proteomes":1991,"sets":0,"structural_models":{"alphafold":1883},"structures":9,"taxa":3364},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":26,"alignment:full":1101},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}