Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components. 2-oxoglutarate + D-alanine = D-glutamate + pyruvate Holoenzyme exhibits additional strong peaks at 333 nm and 415 nm. Addition of D-alanine causes a decrease in absorbance at 419 nm and an increase at 335 nm. Optimum pH is 8.3. Optimum temperature is 60 degrees Celsius. Homodimer. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.