Description

IPR000182 is a GNAT domain.

<p>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]].</p> <p>The 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.</p> <p>Some proteins known to contain a GNAT domain:</p> <ul> <li>Actinobacterial mycothiol acetyltransferase (MshD), which catalyses the transfer of acetyl from acetyl-CoA to desacetylmycothiol to form mycothiol.</li> <li>Yeast GCN5 and Hat1, which are histone acetyltransferases (EC 2.3.1.48).</li> <li>Human PCAF, a histone acetyltransferase.</li> <li>Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT (AANAT), which acetylates serotonin into a circadian neurohormone that may participate in light-dark rhythms, and human mood and behaviour.</li> <li>Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4).</li> <li>Escherichia coli RimI and RimJ, which acetylate the N-terminal alanine of ribosomal proteins S18 and S5, respectively (EC 2.3.1.128).</li> <li>Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (Aac), which acetylates the 2' hydroxyl or amino group of a broad spectrum of aminoglycoside antibiotics.</li> <li>Bacillus subtilis BltD and PaiA, which acetylate spermine and spermidine.</li></ul> <p>This entry represents the entire GNAT domain.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 112

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: