| Primary Identifier | IPR001608 | Type | Domain |
| Short Name | Ala_racemase_N |
| description | Alanine racemase plays a role in providing the D-alanine required for cell wallbiosynthesis by isomerising L-alanine to D-alanine.The molecular structure of alanine racemase from Bacillus stearothermophilus was determined by X-ray crystallography to a resolution of 1.9 A []. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N terminus, and a C-terminal domain essentially composed of β-strands. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the alpha/beta barrel and is covalently linked via an aldimine linkage to a lysine residue, which is at the C terminus of the first β-strand of the alpha/beta barrel.This N-terminal domain is also found in the PROSC (proline synthetase co-transcribed bacterial homologue) family of proteins, which are not known to have alanine racemase activity. |
