IPR038110
Threonine dehydratase, ACT-like domain superfamily
InterPro entry
Short name | TD_ACT-like_sf |
Overlapping entries |
Description
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
[2].
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)
[1]. 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
[3].
References
1.Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. Aravind L, Koonin EV. J. Mol. Biol. 287, 1023-40, (1999). View articlePMID: 10222208
2.Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, Chinchilla D, Eisenstein E. Structure 6, 465-75, (1998). View articlePMID: 9562556
3.The ACT domain family. Chipman DM, Shaanan B. Curr. Opin. Struct. Biol. 11, 694-700, (2001). View articlePMID: 11751050
Cross References
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:3.40.1020.10