H
IPR013815

ATP-grasp fold, subdomain 1

InterPro entry
Short nameATP_grasp_subdomain_1
Overlapping entries
 

Description

This entry represents subdomain 1 found at the N-terminal end of the ATP-grasp domain.

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
[1]
. 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
[2]
. These enzymes contribute predominantly to macromolecular synthesis, using ATP-hydrolysis to activate their substrates.

References

1.A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Galperin MY, Koonin EV. Protein Sci. 6, 2639-43, (1997). View articlePMID: 9416615

2.Mutational analysis of ATP-grasp residues in the two ATP sites of Saccharomyces cerevisiae carbamoyl phosphate synthetase. Eroglu B, Powers-Lee SG. Arch. Biochem. Biophys. 407, 1-9, (2002). View articlePMID: 12392708

Further reading

3. A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:d-alanine ligase of Escherichia coli. Fan C, Moews PC, Shi Y, Walsh CT, Knox JR. Proc. Natl. Acad. Sci. U.S.A. 92, 1172-6, (1995). View articlePMID: 7862655

GO terms

biological process

  • None

molecular function

cellular component

  • None

Cross References

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