The N-acetyltransferases (NAT) ([ec:2.3.1.-]) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodelling. The Gcn5-related N-acetyltransferases (GNAT) catalyse the transfer of the acetyl from the CoA donor to a primary amine of the acceptor. The GNAT proteins share a domain composed of four conserved sequence motifs A-D [[cite:PUB00005463], [cite:PUB00033792]]. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of N-terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalysing the acetylation of amino groups in aminoglycoside antibiotics [[cite:PUB00027579]]. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [[cite:PUB00005463], [cite:PUB00033792], [cite:PUB00027579], [cite:PUB00025257], [cite:PUB00033793]].
\n\nThe acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 β-strands (B) and 4 helices (H) in the topology B1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be from the same monomer or contributed by another [[cite:PUB00033792], [cite:PUB00033793]]. Motifs D (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core [[cite:PUB00033792], [cite:PUB00025257], [cite:PUB00033793]], while the N-terminal motif C (B1-H1) is less conserved.
\n\nSome proteins known to contain a GNAT domain:
\n\nThis entry represents the entire GNAT domain.
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00005463":{"PMID":9175471,"ISBN":null,"volume":"22","issue":"5","year":1997,"title":"GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein.","URL":null,"raw_pages":"154-5","medline_journal":"Trends Biochem Sci","ISO_journal":"Trends Biochem. Sci.","authors":["Neuwald AF","Landsman D."],"DOI_URL":"http://dx.doi.org/10.1016/S0968-0004(97)01034-7"},"PUB00025257":{"PMID":12527305,"ISBN":null,"volume":"325","issue":"5","year":2003,"title":"Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation.","URL":null,"raw_pages":"1019-30","medline_journal":"J Mol Biol","ISO_journal":"J. Mol. Biol.","authors":["He H","Ding Y","Bartlam M","Sun F","Le Y","Qin X","Tang H","Zhang R","Joachimiak A","Liu J","Zhao N","Rao Z."],"DOI_URL":"http://dx.doi.org/10.1016/S0022-2836(02)01284-6"},"PUB00033793":{"PMID":15581578,"ISBN":null,"volume":"433","issue":"1","year":2005,"title":"Structure and functions of the GNAT superfamily of acetyltransferases.","URL":null,"raw_pages":"212-26","medline_journal":"Arch Biochem Biophys","ISO_journal":"Arch. Biochem. Biophys.","authors":["Vetting MW","S de Carvalho LP","Yu M","Hegde SS","Magnet S","Roderick SL","Blanchard JS."],"DOI_URL":"http://dx.doi.org/10.1016/j.abb.2004.09.003"},"PUB00033792":{"PMID":10940244,"ISBN":null,"volume":"29","issue":null,"year":2000,"title":"GCN5-related N-acetyltransferases: a structural overview.","URL":null,"raw_pages":"81-103","medline_journal":"Annu Rev Biophys Biomol Struct","ISO_journal":null,"authors":["Dyda F","Klein DC","Hickman AB."],"DOI_URL":"http://dx.doi.org/10.1146/annurev.biophys.29.1.81"},"PUB00027579":{"PMID":12592013,"ISBN":null,"volume":"12","issue":"3","year":2003,"title":"X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members.","URL":null,"raw_pages":"426-37","medline_journal":"Protein Sci","ISO_journal":"Protein Sci.","authors":["Burk DL","Ghuman N","Wybenga-Groot LE","Berghuis AM."],"DOI_URL":"http://dx.doi.org/10.1110/ps.0233503"}},"set_info":null,"overlaps_with":[{"accession":"IPR016181","name":"Acyl-CoA N-acyltransferase","type":"homologous_superfamily"},{"accession":"IPR027455","name":"Spermine/spermidine acetyltransferase, N-terminal","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":4868,"interactions":4,"matches":1187630,"pathways":334,"proteins":1162535,"proteomes":12522,"sets":0,"structural_models":{"alphafold":859379},"structures":654,"taxa":51946},"entry_annotations":{"alignment:seed":35,"alignment:full":4174},"cross_references":{"prositedoc":{"displayName":"PROSITE Doc","description":"PROSITE is a database of protein families and domains.","rank":18,"accessions":[{"accession":"PDOC51186","url":"http://prosite.expasy.org/PDOC51186"}]},"gp":{"displayName":"Genome Properties","description":"Genome properties is an annotation system whereby functional attributes can be assigned to a genome, based on the presence of a defined set of protein signatures within that genome.","rank":45,"accessions":[{"accession":"GenProp1695","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1695"},{"accession":"GenProp1222","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1222"},{"accession":"GenProp1630","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1630"},{"accession":"GenProp1610","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp1610"},{"accession":"GenProp0232","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0232"},{"accession":"GenProp0796","url":"https://www.ebi.ac.uk/interpro/genomeproperties/genome-property/GenProp0796"}]},"ec":{"displayName":"ENZYME","description":"ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.","rank":19,"accessions":[{"accession":"2.3.1.-","url":"https://enzyme.expasy.org/EC/2.3.1.-"},{"accession":"2.3.1.1","url":"https://enzyme.expasy.org/EC/2.3.1.1"},{"accession":"2.3.1.110","url":"https://enzyme.expasy.org/EC/2.3.1.110"},{"accession":"2.3.1.17","url":"https://enzyme.expasy.org/EC/2.3.1.17"},{"accession":"2.3.1.178","url":"https://enzyme.expasy.org/EC/2.3.1.178"},{"accession":"2.3.1.183","url":"https://enzyme.expasy.org/EC/2.3.1.183"},{"accession":"2.3.1.189","url":"https://enzyme.expasy.org/EC/2.3.1.189"},{"accession":"2.3.1.193","url":"https://enzyme.expasy.org/EC/2.3.1.193"},{"accession":"2.3.1.202","url":"https://enzyme.expasy.org/EC/2.3.1.202"},{"accession":"2.3.1.210","url":"https://enzyme.expasy.org/EC/2.3.1.210"},{"accession":"2.3.1.228","url":"https://enzyme.expasy.org/EC/2.3.1.228"},{"accession":"2.3.1.254","url":"https://enzyme.expasy.org/EC/2.3.1.254"},{"accession":"2.3.1.255","url":"https://enzyme.expasy.org/EC/2.3.1.255"},{"accession":"2.3.1.256","url":"https://enzyme.expasy.org/EC/2.3.1.256"},{"accession":"2.3.1.257","url":"https://enzyme.expasy.org/EC/2.3.1.257"},{"accession":"2.3.1.258","url":"https://enzyme.expasy.org/EC/2.3.1.258"},{"accession":"2.3.1.259","url":"https://enzyme.expasy.org/EC/2.3.1.259"},{"accession":"2.3.1.264","url":"https://enzyme.expasy.org/EC/2.3.1.264"},{"accession":"2.3.1.266","url":"https://enzyme.expasy.org/EC/2.3.1.266"},{"accession":"2.3.1.267","url":"https://enzyme.expasy.org/EC/2.3.1.267"},{"accession":"2.3.1.271","url":"https://enzyme.expasy.org/EC/2.3.1.271"},{"accession":"2.3.1.280","url":"https://enzyme.expasy.org/EC/2.3.1.280"},{"accession":"2.3.1.308","url":"https://enzyme.expasy.org/EC/2.3.1.308"},{"accession":"2.3.1.311","url":"https://enzyme.expasy.org/EC/2.3.1.311"},{"accession":"2.3.1.33","url":"https://enzyme.expasy.org/EC/2.3.1.33"},{"accession":"2.3.1.36","url":"https://enzyme.expasy.org/EC/2.3.1.36"},{"accession":"2.3.1.4","url":"https://enzyme.expasy.org/EC/2.3.1.4"},{"accession":"2.3.1.48","url":"https://enzyme.expasy.org/EC/2.3.1.48"},{"accession":"2.3.1.53","url":"https://enzyme.expasy.org/EC/2.3.1.53"},{"accession":"2.3.1.57","url":"https://enzyme.expasy.org/EC/2.3.1.57"},{"accession":"2.3.1.59","url":"https://enzyme.expasy.org/EC/2.3.1.59"},{"accession":"2.3.1.60","url":"https://enzyme.expasy.org/EC/2.3.1.60"},{"accession":"2.3.1.80","url":"https://enzyme.expasy.org/EC/2.3.1.80"},{"accession":"2.3.1.82","url":"https://enzyme.expasy.org/EC/2.3.1.82"},{"accession":"2.3.1.87","url":"https://enzyme.expasy.org/EC/2.3.1.87"},{"accession":"2.3.2.-","url":"https://enzyme.expasy.org/EC/2.3.2.-"},{"accession":"2.7.1.190","url":"https://enzyme.expasy.org/EC/2.7.1.190"},{"accession":"2.7.11.1","url":"https://enzyme.expasy.org/EC/2.7.11.1"},{"accession":"2.7.2.8","url":"https://enzyme.expasy.org/EC/2.7.2.8"},{"accession":"2.8.1.-","url":"https://enzyme.expasy.org/EC/2.8.1.-"},{"accession":"4.3.2.1","url":"https://enzyme.expasy.org/EC/4.3.2.1"},{"accession":"6.2.1.22","url":"https://enzyme.expasy.org/EC/6.2.1.22"},{"accession":"6.3.5.2","url":"https://enzyme.expasy.org/EC/6.3.5.2"}]}},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"5ls7","name":"Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ"}}}