| Primary Identifier | IPR002986 | Type | Family |
| Short Name | DAP_deCOOHase_LysA |
| description | Pyridoxal-dependent decarboxylases that act on ornithine-, lysine-, arginine- and related substrates can be classified into different familieson the basis of sequence similarity [, ]. One of these families includesornithine decarboxylase (ODC), which catalyses the transformationof ornithine into putrescine; prokaryotic diaminopimelate decarboxylase, which catalyses the conversion of diaminopimelate into lysine; Pseudomonas syringae pv. tabaciprotein, tabA, which is probably involved in tabtoxin biosynthesis andis similar to diaminopimelate decarboxylase; and bacterial and plant biosynthetic argininedecarboxylase, which catalyses the transformation of arginine into agmatine, the first step in putrescine synthesis from arginine.Although these proteins, which are known collectively as group IVdecarboxylases [], probably share a common evolutionary origin, theirlevels of sequence similarity are low, being confined to a few shortconserved regions. These conserved motifs suggest a common structuralarrangement for positioning of substrate and the cofactor pyridoxal5'-phosphate among bacterial diaminopimelate ddecarboxylases, eukaryotic ornithinedecarboxylases and arginine decarboxylases [].This entry represents the diaminopimelate decarboxylase LysA, which converts meso-diaminopimelate into lysine and is the last step of the DAP lysine biosynthetic pathway. The structure of bacterial diaminopimelate decarboxylase has been determined []. |
