{"metadata":{"accession":"PF06230","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010415","hierarchy":null,"name":{"name":"LpxI C-terminal domain","short":"LpxI_C"},"description":[{"text":"<p>This entry represents the catalytic C-terminal domain of the LpxI enzyme that is involved in biosynthesis of lipid A. Specifically it carried out the hydrolysis of UDP-2,3-diacyl- glucosamine. This step is either carried out by LpxI or LpxH [[cite:PUB00091500]]. This domain comprises a five-stranded mixed beta-sheet bracketed by one alpha-helix on one side and three on the other. This domain is structurally related to a superfamily that includes cytosine deaminase [[cite:PUB00091500]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00091500":{"PMID":23042606,"ISBN":null,"volume":"19","issue":"11","year":2012,"title":"LpxI structures reveal how a lipid A precursor is synthesized.","URL":null,"raw_pages":"1132-8","medline_journal":"Nat Struct Mol Biol","ISO_journal":"Nat. Struct. Mol. Biol.","authors":["Metzger LE 4th","Lee JK","Finer-Moore JS","Raetz CR","Stroud RM."],"DOI_URL":"https://doi.org/10.1038/nsmb.2393"}},"set_info":{"accession":"CL0109","name":"CDA"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":7,"interactions":0,"matches":2774,"pathways":0,"proteins":2749,"proteomes":2742,"sets":1,"structural_models":{"alphafold":1935},"structures":2,"taxa":4373},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":119,"alignment:full":1622},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}