| Description | The ACT domain is found in a variety of contexts and is proposed to be a conserved regulatory binding fold. ACT domains, named after the proteins Aspartate kinase, Chorismate mutase and TyrA (prephenate dehydrogenase), are important for the allosteric regulation of many enzymes, including a wide range of metabolic enzymes.The archetypical ACT domain is the C-terminal regulatory domain of 3-phosphoglycerate dehydrogenase (3PGDH), which folds with a ferredoxin-like topology. A pair of ACT domains form an eight-stranded antiparallel sheet with two molecules of allosteric inhibitor serine bound in the interface. Biochemical exploration of a few other proteins containing ACT domains supports the suggestions that these domains contain the archetypical ACT structure [ , , ].This entry represents the ACT-like domain found in diverse proteins from bacteria, eukaryotes and archaea. | Name | ACT-like domain |
| Short Name | ACT-like_dom_sf | Type | Homologous_superfamily |
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