InterPro domain: IPR036551

This entry contains a diverse range of flavoprotein enzymes, including Epidermin decarboxylase, EpiD, which has been shown to be a flavoprotein that binds FMN [ 1 ]. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond.

This superfamily also includes the B chain of dipicolinate synthase. Dipicolinate synthase catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid. Dipicolinic acid is a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance [ 2 ]. This superfamily also includes phenolic acid decarboxylase (also known as phenylacrylic acid decarboxylase [intenz:4.1.1.-]) [ 3 ].

1. Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin. J. Bacteriol. 174, 5354-61
2. Cloning, DNA sequence, functional analysis and transcriptional regulation of the genes encoding dipicolinic acid synthetase required for sporulation in Bacillus subtilis. J. Mol. Biol. 232, 468-83
3. PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae. Gene 142, 107-12