| Type: | Domain | Name: | Pyruvoyl-dependent histidine/arginine decarboxylase |
| Description: | This entry represents a structural domain found in pyruvoyl-dependent histidine decarboxylase () and arginine decarboxylase (). This domain consists of a duplication of a beta-alpha-beta(2) motif that forms a 4-layer alpha/beta/beta/alpha topology, which contains a silk-like beta-sandwich. This domain contains two chains resulting from self-processing of a single-chain precursor. These proteins form heterohexamers [, ].Histidine decarboxylase catalyses the formation of histamine from histidine. It requires a pyruvoyl group for its activity. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta) 6 by nonhydrolytic self-catalysis.Arginine decarboxylase catalyses the interconversion of arginine and agmatine plus carbon dioxide. It requires a pyruvoyl group for its activity. Archaeoglobus fulgiduscontains three copies of this 80-residue domain, all of which are very closely related. | Short Name: | Pyr-dep_his/arg-deCO2ase |
