ACT-like domain

Definition

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 [[cite:PMID:11751050], [cite:PMID:16987805], [cite:PMID:31900369]]. This entry represents the ACT-like domain found in diverse proteins from bacteria, eukaryotes and archaea.

7 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (7 proteins: gene, accession, name)

• CASTOR1
• CASTOR2
• CASTOR3P
• PAH
• TH
• TPH1
• TPH2