Aspartate 1-decarboxylase, pyridoxal-dependent (IPR022517)
Short name: Asp_decarboxylase_pyridox
Overlapping homologous superfamilies
- Pyridoxal phosphate-dependent transferase, major domain (IPR015421)
- Pyridoxal phosphate-dependent transferase (IPR015424)
This enzyme is proposed here to be a form of aspartate 1-decarboxylase, pyridoxal-dependent, that represents a non-orthologous displacement to the more widely distributed pyruvoyl-dependent form (TIGR00223). Aspartate 1-decarboxylase makes beta-alanine, used usually in pathothenate biosynthesis, by decarboxylation from asparatate. A number of species with the PanB and PanC enzymes, however, lack PanD. This protein family occurs in a number of Proteobacteria that lack PanD. This enzyme family appears to be a pyridoxal-dependent enzyme (see PF00282). The family was identified by Partial Phylogenetic Profiling; members in Geobacter sulfurreducens, Geobacter metallireducens, and Pseudoalteromonas atlantica are clustered with the genes for PanB and PanC. We suggest the gene symbol panP (panthothenate biosynthesis enzyme, Pyridoxal-dependent).
- TIGR03799 (NOD_PanD_pyr)