{"metadata":{"accession":"PF04768","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR006855","hierarchy":null,"name":{"name":"NAT, N-acetyltransferase, of N-acetylglutamate synthase","short":"NAT"},"description":[{"text":"<p>This is the C-terminal NAT or N-acetyltransferase domain of bifunctional N-acetylglutamate synthase/kinases. It catalyzes the first two steps in arginine biosynthesis. This domain contains the putative NAGS - N-acetylglutamate synthase - active site. It is found at the C-terminus of Neurospora crassa acetylglutamate synthase - amino-acid acetyltransferase, EC: 2.3.1.1. It is also found C-terminal to the amino acid kinase region ([pfam:PF00696]) in some fungal acetylglutamate kinase enzymes [[cite:PUB00110296]]. it stabilises the yeast NAGK, N-acetyl-L-glutamate kinase, slows catalysis and modulates feed-back inhibition by arginine [[cite:PUB00059379]]. This domain is found to be the N-acetyltransferase (NAT) domain, and it has a typical GCN5-related NAT fold and a site that catalyzes NAG synthesis which is located >25 Angstrom away from the L-arginine binding site in the N-terminal domain [pfam:PF00696] [[cite:PUB00074836]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00110296":{"PMID":22174908,"ISBN":null,"volume":"6","issue":"12","year":2011,"title":"A novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris.","URL":null,"raw_pages":"e28825","medline_journal":"PLoS One","ISO_journal":"PLoS One","authors":["Shi D","Li Y","Cabrera-Luque J","Jin Z","Yu X","Zhao G","Haskins N","Allewell NM","Tuchman M."],"DOI_URL":null},"PUB00059379":{"PMID":22529931,"ISBN":null,"volume":"7","issue":"4","year":2012,"title":"Insight on an arginine synthesis metabolon from the tetrameric structure of yeast acetylglutamate kinase.","URL":null,"raw_pages":"e34734","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["de Cima S","Gil-Ortiz F","Crabeel M","Fita I","Rubio V."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0034734"},"PUB00074836":{"PMID":23894642,"ISBN":null,"volume":"8","issue":"7","year":2013,"title":"Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms.","URL":null,"raw_pages":"e70369","medline_journal":"PLoS One","ISO_journal":"PLoS ONE","authors":["Zhao G","Jin Z","Allewell NM","Tuchman M","Shi D."],"DOI_URL":"http://dx.doi.org/10.1371/journal.pone.0070369"}},"set_info":{"accession":"CL0257","name":"Acetyltrans"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":68,"interactions":0,"matches":4354,"pathways":0,"proteins":4045,"proteomes":2336,"sets":1,"structural_models":{"alphafold":3250},"structures":10,"taxa":5183},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":25,"alignment:full":3279},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4nf1","name":"Structure of N-acetyltransferase domain of X. fastidiosa NAGS/K without his-tag"}}}