{"metadata":{"accession":"PF02952","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR015888","hierarchy":null,"name":{"name":"L-fucose isomerase, C-terminal domain","short":"Fucose_iso_C"},"description":[{"text":"

L-fucose isomerase (5.3.1.25) converts the aldose L-fucose into the corresponding ketose L-fuculose during the first step in fucose metabolism using Mn2+ as a cofactor. The enzyme is a hexamer, forming the largest structurally known ketol isomerase, and each protomer consists of three domains. This entry represents the C-terminal domain.

","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"L-fucose_isomerase","extract":"

In enzymology, a L-fucose isomerase is an enzyme that catalyzes the chemical reaction

L-fucose L-fuculose
","thumbnail":null}],"literature":{"PUB00007428":{"PMID":9367760,"ISBN":null,"volume":"273","issue":"1","year":1997,"title":"Structure and mechanism of L-fucose isomerase from Escherichia coli.","URL":null,"raw_pages":"256-68","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["Seemann JE","Schulz GE."],"DOI_URL":"http://dx.doi.org/10.1006/jmbi.1997.1280"}},"set_info":{"accession":"CL0866","name":"ALR_C-like"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":11,"interactions":0,"matches":5174,"pathways":0,"proteins":5174,"proteomes":2183,"sets":1,"structural_models":{"alphafold":4303,"bfvd":0},"structures":9,"taxa":4717},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":19,"alignment:full":1739},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}