InterPro domain: IPR016181

General Information

  • Identifier IPR016181
  • Description Acyl-CoA N-acyltransferase
  • Number of genes 6061
  • Gene duplication stats Loading...

Abstract

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 [ 1 ], the histone acetyltransferase domain of P300/CBP associating factor PCAF [ 2 ], the catalytic domain of GCN5 histone acetyltransferase [ 3 ], and diamine acetyltransferase 1 [ 4 ].
  • Autoinducer synthetases, such as protein LasI [ 5 ] and acyl-homoserinelactone synthase EsaI [ 6 ].
  • 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 [ 7 ].
  • 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) [ 8 ].
  • FemXAB nonribosomal peptidyltransferases, including methicillin-resistance protein FemA (transfer glycyl residue from tRNA-Gly) [ 9 ] and peptidyltransferase FemX [ 10 ].
  • Hypothetical protein cg14615-pa from Drosophila melanogaster (Fruit fly).


1. X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members. Protein Sci. 12, 426-37
2. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18, 3521-32
3. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proc. Natl. Acad. Sci. U.S.A. 96, 8931-6
4. Structures of wild-type and mutant human spermidine/spermine N1-acetyltransferase, a potential therapeutic drug target. Proc. Natl. Acad. Sci. U.S.A. 103, 2063-8
5. Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI. Mol. Microbiol. 53, 1135-46
6. Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing. Mol. Cell 9, 685-94
7. The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli. Protein Sci. 16, 528-34
8. Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis. Biochemistry 40, 6335-43
9. X-ray crystal structure of Staphylococcus aureus FemA. Structure 10, 1107-15
10. Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition. Structure 12, 257-67

Species distribution

Gene table

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