ATP-grasp fold, succinyl-CoA synthetase-type (IPR013650)

Short name: ATP-grasp_succ-CoA_synth-type

Overlapping homologous superfamilies


Domain relationships

  • ATP-grasp fold (IPR011761)
    • ATP-grasp fold, succinyl-CoA synthetase-type (IPR013650)


The ATP-grasp superfamily currently includes 17 groups of enzymes, catalyzing ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule [PMID: 9416615]. They contribute predominantly to macromolecular synthesis. ATP-hydrolysis is used to activate a substrate. For example, DD-ligase transfers phosphate from ATP to D-alanine on the first step of catalysis. On the second step the resulting acylphosphate is attacked by a second D-alanine to produce a DD dipeptide following phosphate elimination [PMID: 7939684].

The ATP-grasp domain contains three conserved motifs, corresponding to the phosphate binding loop and the Mg(2+) binding site [PMID: 8804825]. The fold is characterised by two alpha-beta subdomains that grasp the ATP molecule between them. Each subdomain provides a variable loop that forms a part of the active site, completed by region of other domains not conserved between the various ATP-grasp enzymes [PMID: 7862655].

The ATP-grasp domain represented by this entry is found primarily in succinyl-CoA synthetases (EC:

Contributing signatures

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