Pathways & interactions
Acyl-CoA N-acyltransferase (IPR016181)
Short name: Acyl_CoA_acyltransferase
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:
- N-acetyl transferase (NAT) family members, including aminoglycoside N-acetyltransferases [PMID: 12592013], the histone acetyltransferase domain of P300/CBP associating factor PCAF [PMID: 10393169], the catalytic domain of GCN5 histone acetyltransferase [PMID: 10430873], and diamine acetyltransferase 1 [PMID: 16455797].
- Autoinducer synthetases, such as protein LasI [PMID: 15306017] and acyl-homoserinelactone synthase EsaI [PMID: 11931774].
- 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 [PMID: 17242373].
- 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.
- 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).
Several proteins carry a duplication of this domain, which consists of two NAT-like domains swapped with the C-terminal strands, including:
- N-myristoyl transferase (NMT) [PMID: 11371195].
- FemXAB nonribosomal peptidyltransferases, including methicillin-resistance protein FemA (transfer glycyl residue from tRNA-Gly) [PMID: 12176388] and peptidyltransferase FemX [PMID: 14962386].
- Hypothetical protein cg14615-pa from Drosophila melanogaster (Fruit fly).