Homologous Superfamily

ATP-grasp fold, subdomain 1 (IPR013815)

Short name: ATP_grasp_subdomain_1

Overlapping entries


The ATP-grasp fold is one of several distinct ATP-binding folds, and is found in enzymes that catalyze the formation of amide bonds, catalyzing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule [PMID: 9416615]. 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, amongst others [PMID: 12392708]. These enzymes contribute predominantly to macromolecular synthesis, using ATP-hydrolysis to activate their substrates.

The ATP-grasp fold shares functional and structural similarities with the PIPK (phosphatidylinositol phosphate kinase) and protein kinase superfamilies. The ATP-grasp domain consists of two subdomains with different alpha+beta folds, which grasp the ATP molecule between them. Each subdomain provides a variable loop that forms part of the active site, with regions from other domains also contributing to the active site, even though these other domains are not conserved between the various ATP-grasp enzymes [PMID: 7862655]. This entry represents subdomain 1 found at the N-terminal end of the ATP-grasp domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005524 ATP binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.