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"metadata": {
"accession": "PS51186",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR000182",
"hierarchy": null,
"name": {
"name": "Gcn5-related N-acetyltransferase (GNAT) domain profile",
"short": "GNAT"
},
"description": [
{
"text": "<p>The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetyl\ncoenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction\nimplicated in various functions from bacterial antibiotic resistance to\nmammalian circadian rhythm and chromatin remodeling. The Gcn5-related\nN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoA\ndonor to a primary amine of the acceptor. The GNAT proteins share a domain\ncomposed of four conserved sequence motifs A-D [[cite:PUB00005463]][[cite:PUB00033792]]. This GNAT domain is\nnamed after yeast GCN5 (from General Control Nonrepressed) and related histone\nacetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues\nof amino terminal histone tails, resulting in transcription activation.\nAnother category of GNAT, the aminoglycoside N-acetyltransferases, confer\nantibiotic resistance by catalyzing the acetylation of amino groups in\naminoglycoside antibiotics [[cite:PUB00027579]]. GNAT proteins can also have anabolic and\ncatabolic 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\n7 beta strands (B) and 4 helices (H) in the topology\nB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be\nfrom the same monomer or contributed by another [[cite:PUB00033792]][[cite:PUB00033793]]. Motifs\nD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core\n[[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\n - Yeast GCN5 and Hat1, which are histone acetyltransferases (EC 2.3.1.48).\n - Human PCAF, a histone acetyltransferase.\n - Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT\n (AANAT), which acetylates serotonin into a circadian neurohormone that may\n participate in light-dark rhythms, and human mood and behavior.\n - Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4).\n - Escherichia coli rimI and rimJ, which acetylate the N-terminal alanine of\n ribosomal proteins S18 and S5, respectively (EC 2.3.1.128).\n - Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (aac),\n which acetylates the 2' hydroxyl or amino group of a broad spectrum of\n aminoglycoside antibiotics.\n - Bacillus subtilis bltD and paiA, which acetylate spermine and spermidine.\n - Escherichia coli uncharacterized protein YjdJ [[cite:PUB00046616]].\n - Animal N-acetyltransferase domain-containing protein 1 (NATD1 or GTLF3B)\n [[cite:PUB00046616]].\n - Arabidopsis thaliana minimal acetyltransferase At1g77540 [[cite:PUB00046616]].\n - Animal alpha-tubulin N-acetyltransferases (TATs), acetylate Lys-40 of\n alpha-tubulin in most eukaryotes. TATs show preference for tubulin already\n incorporated in microtubules, and acetylation is associated predominantly\n with stable microtubules such as those found in cilia and axons. TATs show\n high sequence conservation from flagellates to humans [[cite:PUB00074837]].\n - Vertebrate-like N-acetyl-L-gluatamate synthase (NAGS, EC 2.3.1.1), catalyze\n the conversion of AcCoA and L-glutamate to CoA and N-acetyl-L-glutamate\n (NAG). They include not only vertebrate NAGS, but also fungal NAGS and\n NAGK, and bacterial bifunctional NAGS/K [[cite:PUB00074836]].\n - Bacteria-like NAGS, includes most bacterial and plant NAGS.\n\nAs the GNAT domain has largely diverged we developed several profiles. The\nfirst one is general and detects several subfamilies of GNAT domains. The\nsecond is specific for the YjtD-type subfamily [[cite:PUB00046616]] and the third for the ATAT-\ntype subfamily [[cite:PUB00074837]]. The fourth profile is directed against the vertebrate-like\nNAGS-type GNAT domain [[cite:PUB00074836]]. All the profiles we developed cover the entire GNAT\ndomain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"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"
},
"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"
},
"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"
},
"PUB00074837": {
"PMID": 23105108,
"ISBN": null,
"volume": "287",
"issue": "50",
"year": 2012,
"title": "Crystal structures of tubulin acetyltransferase reveal a conserved catalytic core and the plasticity of the essential N terminus.",
"URL": null,
"raw_pages": "41569-75",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Kormendi V",
"Szyk A",
"Piszczek G",
"Roll-Mecak A."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.C112.421222"
},
"PUB00046616": {
"PMID": 18709443,
"ISBN": null,
"volume": "9",
"issue": "1-4",
"year": 2008,
"title": "Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.",
"URL": null,
"raw_pages": "7-20",
"medline_journal": "J Struct Funct Genomics",
"ISO_journal": "J. Struct. Funct. Genomics",
"authors": [
"Cort JR",
"Ramelot TA",
"Murray D",
"Acton TB",
"Ma LC",
"Xiao R",
"Montelione GT",
"Kennedy MA."
],
"DOI_URL": "http://dx.doi.org/10.1007/s10969-008-9041-z"
},
"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"
},
"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"
},
"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": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 882304,
"pathways": 0,
"proteins": 864222,
"proteomes": 21449,
"sets": 0,
"structural_models": {
"alphafold": 641738,
"bfvd": 109
},
"structures": 641,
"taxa": 42872
},
"entry_annotations": {},
"cross_references": {},
"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"
}
}
}
