{"metadata":{"accession":"PF06491","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR009474","hierarchy":null,"name":{"name":"Disulphide isomerase","short":"Disulph_isomer"},"description":[{"text":"<p>This family of proteins has disulphide isomerase activity, [ec:5.3.4.1]. It has a similar fold to thioredoxin, with an alpha-beta-alpha-beta-alpha-beta-beta-alpha topology. It has a conserved CGC motif in the loop immediately downstream of the first beta strand. This motif is essential for activity [[cite:PUB00052908]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00052908":{"PMID":19653655,"ISBN":null,"volume":"48","issue":"36","year":2009,"title":"Structure and function of Bacillus subtilis YphP, a prokaryotic disulfide isomerase with a CXC catalytic motif .","URL":null,"raw_pages":"8664-71","medline_journal":"Biochemistry","ISO_journal":"Biochemistry","authors":["Derewenda U","Boczek T","Gorres KL","Yu M","Hung LW","Cooper D","Joachimiak A","Raines RT","Derewenda ZS."],"DOI_URL":"http://dx.doi.org/10.1021/bi900437z"}},"set_info":{"accession":"CL0172","name":"Thioredoxin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":3890,"pathways":0,"proteins":3890,"proteomes":3148,"sets":1,"structural_models":{"alphafold":2471},"structures":2,"taxa":4075},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":59,"alignment:full":1740},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"7rzb","name":"BrxA from Staphylococcus aureus with bacillithiol mixed disulfide"}}}