| Type: | Family | Name: | Decarboxylase UbiX/Pad1 |
| Description: | In Escherichia coli, the protein UbiX (3-octaprenyl-4-hydroxybenzoate carboxy-lyase) has been shown to be involved in the third step of ubiquinone biosynthesis. It catalyses the reaction [3-octaprenyl-4-hydroxybenzoate = 2-octaprenylphenol + CO2] []. The knockout of the homologous protein in yeast (Pad1) confers sensitivity to phenylacrylic acid, showing that this enzyme functions as a phenylacrylic acid decarboxylase [, ].E. coli strains also contain, in addition to UbiX, a second paralogue named Pad1. Its amino acid sequence shows 52% identity to UbiX and slightly higher sequence identity to Saccharomyces cerevisiae phenylacrylic acid decarboxylase Pad1. Despite its higher sequence similarity with yeast Pad1, E. coli Pad1 does not seem to have phenylacrylic acid decarboxylase activity. Its function is unknown, Pad1 may remove the carboxylate group from derivatives of benzoic acid but not from substituted phenolic acids []. | Short Name: | UbiX_Pad1 |
