|PROSITE documentation PDOC51671 [for PROSITE entry PS51671]|
The ACT domain is a 90 amino acid long domain, which has been named after three of the allosterically regulated enzymes in which it is found: aspartate kinase, chorismate mutase and TyrA (prephenate dehydrogenase) . The ACT domain is found in a variety of contexts and is proposed to be a structurally conserved regulatory domain involved in the binding of small ligands, such as amino acids. Most of the proteins in which it is found are involved in amino acid and purine metabolism:
Threonine dehydratases (TDs) contain an ACT-like regulatory domain that possesses structural, rather than sequence, homology to the ACT domain .
The profile we developed cover the entire ACT and ACT-like domains.Last update:
April 2013 / First entry.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Aravind L. Koonin E.V.|
|Title||Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches.|
|Source||J. Mol. Biol. 287:1023-1040(1999).|
|2||Authors||Hsieh M.-H. Goodman H.M.|
|Title||Molecular characterization of a novel gene family encoding ACT domain repeat proteins in Arabidopsis.|
|Source||Plant Physiol. 130:1797-1806(2002).|
|3||Authors||Chipman D.M. Shaanan B.|
|Title||The ACT domain family.|
|Source||Curr. Opin. Struct. Biol. 11:694-700(2001).|