| Type: | Domain | Name: | Pre-ATP-grasp domain |
| 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 entry 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 alpha/beta/alpha in three layers, and is possibly a rudiment form of the Rossmann-fold. | Short Name: | PreATP-grasp_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR005481 | Domain | Biotin carboxylase-like, N-terminal domain |
| IPR020562 | Domain | Phosphoribosylglycinamide synthetase, N-terminal |
| IPR004887 | Domain | Glutathione synthase, substrate-binding, eukaryotic |
| IPR005494 | Domain | Glutathionylspermidine synthase, pre-ATP-grasp-like domain |
| IPR020897 | Domain | Synapsin, pre-ATP-grasp domain |
