InterPro domain: IPR020459

A number of prokaryotic and eukaryotic enzymes, which appear to act via an ATP-dependent covalent binding of AMP to their substrate, share a region of sequence similarity [ 1 , 2 , 3 ]. This region is a Ser/Thr/Gly-rich domain that is further characterised by a conserved Pro-Lys-Gly triplet. The family of enzymes includes luciferase, long chain fatty acid Co-A ligase, acetyl-CoA synthetase and various other closely-related synthetases [ 4 , 5 ].

1. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J. 9, 2743-50
2. Protein sequence homology between plant 4-coumarate:CoA ligase and firefly luciferase. Nucleic Acids Res. 17, 460
3. Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 172, 7011-9
4. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-98
5. Structural Insights into Anthranilate Priming during Type II Polyketide Biosynthesis. ACS Chem. Biol. 11, 95-103