| Primary Identifier | IPR005308 | Type | Domain |
| Short Name | OKR_de-COase_N |
| description | This domain has a flavodoxin-like fold, and is termed the "wing"domain because of its position in the overall 3D structure. Ornithine decarboxylase from Lactobacillus 30a (L30a OrnDC, ) is representative of the large, pyridoxal-5'-phosphate-dependentdecarboxylases that act on lysine, arginine or ornithine. The crystal structure of the L30a OrnDC has been solved to 3.0 A resolution. Six dimers related by C6 symmetry compose the enzymatically activedodecamer (approximately 106Da). Each monomer of L30a OrnDC can be described in terms of five sequential folding domains.The amino-terminal domain, residues 1 to 107, consists of a five-stranded β-sheet termed the "wing"domain. Two wing domains ofeach dimer project inward towards the centre of the dodecamer and contribute to dodecamer stabilisation [].Proteins containing this domain include the ornithine decarboxylase, the lysine decarboxylase and the biodegradative arginine decarboxylase. |
