<p>This entry represents a structural domain found in several acyl-CoA acyltransferase enzymes. This domain has a 3-layer alpha/beta/alpha structure that contains mixed beta-sheets, and can be found in the following proteins:</p><p> <ul><li> N-acetyl transferase (NAT) family members, including aminoglycoside N-acetyltransferases [<cite idref="PUB00027579"/>], the histone acetyltransferase domain of P300/CBP associating factor PCAF [<cite idref="PUB00023984"/>], the catalytic domain of GCN5 histone acetyltransferase [<cite idref="PUB00006453"/>], and diamine acetyltransferase 1 [<cite idref="PUB00039506"/>].</li><li> Autoinducer synthetases, such as protein LasI [<cite idref="PUB00030742"/>] and acyl-homoserinelactone synthase EsaI [<cite idref="PUB00026875"/>].</li><li>Leucyl/phenylalanyl-tRNA-protein transferase (LFTR), a close relative of the non-ribosomal peptidyltransferases; there is a deletion of the N-terminal half of the N-terminal NAT-like domain after the domain duplication/swapping events [<cite idref="PUB00040115"/>].</li><li>Ornithine decarboxylase antizyme, which may have evolved a different function for this domain, although the putative active site maps to the same location in the common fold.</li><li>Arginine N-succinyltransferase, alpha chain, AstA, which contains an extra C-terminal domain that is similar to the double psi beta-barrel fold domain (missing one strand and untangled psi-loops).</li></ul> </p><p>Several proteins carry a duplication of this domain, which consists of two NAT-like domains swapped with the C-terminal strands, including:</p><p> <ul><li> N-myristoyl transferase (NMT) [<cite idref="PUB00026039"/>].</li><li> FemXAB nonribosomal peptidyltransferases, including methicillin-resistance protein FemA (transfer glycyl residue from tRNA-Gly) [<cite idref="PUB00014008"/>] and peptidyltransferase FemX [<cite idref="PUB00029031"/>].</li><li> Hypothetical protein cg14615-pa from <taxon tax_id="7227">Drosophila melanogaster</taxon> (Fruit fly).</li></ul> </p> Acyl-CoA N-acyltransferase