| Description | The ACT domain is found in a variety of contexts and is proposed to be a conserved regulatory binding fold. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. 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 [ ].Most of the proteins in which it is found are involved in amino acid and purine metabolism:aspartokinaseschorismate mutasesprephenate dehydrogenases (TyrA)prephenate dehydrataseshomoserine dehydrogenasesmalate dehydrogenasesphosphoglycerate dehydrogenasesphenylalanine and tryptophan-4-monooxygenasesphosphoribosylformylglycinamidine synthase (PurQ)uridylyl transferase and removing enzyme (GlnD)GTP pyrophosphokinase/phosphohydrolase (SpoT/RelA)tyrosine and phenol metabolism operon regulators (TyrR)several uncharacterised proteins from archaea, bacteria and plants that contain from one to four copies of this domain [ ]. | Name | ACT domain |
| Short Name | ACT_dom | Type | Domain |
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