LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | The ATP-grasp fold is one of several distinct ATP-binding folds, and is found in enzymes that catalyse the formation of amide bonds, catalysing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule [ ]. This fold is found in many different enzyme families, including various peptide synthetases, biotin carboxylase, synapsin, succinyl-CoA synthetase, pyruvate phosphate dikinase, and glutathione synthetase, glutathionylspermidine synthase, amongst others []. These enzymes contribute predominantly to macromolecular synthesis, using ATP-hydrolysis to activate their substrates. This superfamily represents the pre-ATP-grasp structural domain, which precedes the ATP-grasp domain in all superfamily members, and which usually occurs at the N terminus of the protein. The structure of the pre-ATP-grasp domain consists of α/β/α in three layers, and is possibly a rudiment form of the Rossmann-fold. |
| Short Name | PreATP-grasp_dom_sf |
