InterPro domain: IPR007085

This entry represents the C-terminal domain found in DNA/pantothenate metabolism flavoproteins, which affects synthesis of DNA and pantothenate metabolism. These proteins contain ATP, phosphopantothenate, and cysteine binding sites. The structure of this domain has been determined in human phosphopantothenoylcysteine (PPC) synthetase [ 1 ] and as the PPC synthase domain (CoaB) from the Escherichia coli coenzyme A bifunctional protein CoaBC [ 2 ]. This domain adopts a 3-layer alpha/beta/alpha fold with mixed beta-sheets, which topologically resembles a combination of Rossmann-like and ribokinase-like folds. The structure of these proteins predicts a ping pong mechanism with initial formation of an acyladenylate intermediate, followed by release of pyrophosphate and attack by cysteine to form the final products PPC and AMP.

1. Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution. Structure 11, 927-36
2. Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase. Structure 12, 1977-88