Homologous Superfamily

Threonine dehydratase, ACT-like domain superfamily (IPR038110)

Short name: TD_ACT-like_sf

Overlapping entries


Threonine deaminase (threonine dehydratase, TD) is the first enzyme on the pathway for the biosynthesis of isoleucine. TD is organized into two domains. The larger N-terminal domain is considered the catalytic domain as it contains the essential pyridoxal phosphate cofactor. The C-terminal regulatory domain folds as an eight-stranded antiparallel sheet. The holoenzyme is a homotetramer in which the intersubunit contacts lie between pairs of C-terminal regulatory domains and pairs of N-terminal domains [PMID: 9562556].

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) [PMID: 10222208]. 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. There is a close structural and functional relationship between the regulatory domain of TD and the ACT domain [PMID: 11751050].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.