IPR026260
Threonine synthase, bacterial/archaeal
InterPro entry
Short name | Thr_Synthase_bac/arc |
Overlapping homologous superfamilies | |
family relationships |
Description
Threonine synthase (
4.2.3.1) catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate, using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes
[1].
This entry represents the a group of threonine synthases from bacteria and archaea.
References
1.Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase. Parsot C. EMBO J. 5, 3013-9, (1986). View articlePMID: 3098560
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Contributing Member Database Entry
- PIRSF:PIRSF038945
Representative structure
2zsj: Crystal structure of threonine synthase from Aquifex aeolicus VF5