LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the Fe(2) 2-oxoglutarate dioxygenase domain found in isopenicillin N synthase PcbC from fungi and related proteins such as procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2) from humans and 1-aminocyclopropane-1-carboxylate oxidase 1 from plants.The iron 2OG dioxygenase domain has a conserved β-barrel structure [ ], which forms a double-stranded β-helix core fold that forms the predominant class of the cupin superfamily ('cupa' means a small barrel in Latin) []. Two histidines and an aspartate residue catalytically bind a metal ion, in general iron but in some cases another metal, directly involved in catalysis. A conserved arginine or lysine residue further near the C-terminal part acts as the basic residue that interacts with the acidic substrate.Isopenicillin N synthase (IPNS) catalyses conversion of the linear tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV) to isopenicillin N (IPN), the central step in biosynthesis of the beta-lactam antibiotics [ ]. IPNS is a nonhaem-Fe2+-dependent enzyme. It belongs to a class of nonhaem Fe2+-containing enzymes which includes 2-oxoglutarate-dependent dioxygenases, 2-oxoglutarate-dependent hydroxy- lases, and enzymes involved in ethylene formation and anthocyaninidin biosynthesis.The IPNS structure shows that the active site is buried within the hydrophobic pocket of an eight-stranded jelly roll barrel [ , ]. |
| Short Name | IPNS-like_FE2OG_OXY |
