CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Phosphoserine aminotransferase

Enzyme Information
Phosphoserine transaminase.
based on mapping to UniProt Q96255
(1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + L-glutamate.
-!- Catalyzes the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli. -!- Also catalyzes the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E.coli (using reaction 2 above). -!- In E.coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC, EC, EC, EC, EC and EC (with pyridoxine 5'-phosphate as substrate). -!- Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis. -!- Non-phosphorylated forms of serine and threonine are not substrates.

UniProtKB Entries (1)

Arabidopsis thaliana
Phosphoserine aminotransferase 1, chloroplastic

PDB Structure

External Links
Primary Citation
Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) FromArabidopsis thaliana- the Enzyme Involved in the Phosphorylated Pathway of Serine Biosynthesis.
Sekula, B., Ruszkowski, M., Dauter, Z.
Front Plant Sci