1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR020622 | Binding_site | Alanine racemase, pyridoxal-phosphate attachment site |
| Type: | Domain | Name: | Alanine racemase, N-terminal |
| Description: | Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine.The molecular structure of alanine racemase from Bacillus stearothermophiluswas 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 beta-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 beta-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. | Short Name: | Ala_racemase_N |
| DB identifier | Type | Name |
|---|---|---|
| IPR020622 | Binding_site | Alanine racemase, pyridoxal-phosphate attachment site |
