{"metadata":{"accession":"PF00668","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR001242","hierarchy":null,"name":{"name":"Condensation domain","short":"Condensation"},"description":[{"text":"<p>This domain is found in many multi-domain enzymes which synthesise peptide antibiotics. This domain catalyses a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain ([pfam:PF00550]). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site [[cite:PUB00007135]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Condensation_domain","extract":"<p>In molecular biology, the <b>condensation domain</b> is a protein domain found in many multi-domain enzymes which synthesise peptide antibiotics. This domain catalyses a condensation reaction to form peptide bonds in non-ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pp-binding). It has been shown that mutations in the HHXXXDG sequence motif in this domain abolish activity suggesting this is part of the active site.</p>","thumbnail":null}],"literature":{"PUB00007135":{"PMID":9712910,"ISBN":null,"volume":"273","issue":"35","year":1998,"title":"Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain.","URL":null,"raw_pages":"22773-81","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Stachelhaus T","Mootz HD","Bergendahl V","Marahiel MA."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.273.35.22773"}},"set_info":{"accession":"CL0149","name":"CoA-acyltrans"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":7481,"interactions":0,"matches":149357,"pathways":0,"proteins":68562,"proteomes":8647,"sets":1,"structural_models":{"alphafold":14105},"structures":107,"taxa":14069},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":21,"alignment:full":72612},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7c1u","name":"Crystal structure of the starter condensation domain of rhizomide synthetase RzmA mutant H140V/R148A in a \"product-released\" conformation"}}}