CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate Aminotransferase, domain 1
Functional Family Phosphoserine aminotransferase 2, chloroplastic

Enzyme Information
Phosphoserine transaminase.
based on mapping to UniProt Q9PIH3
(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)

Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
Phosphoserine aminotransferase

PDB Structure

External Links
Primary Citation
Crystal Structure of Phosphoserine Aminotransferase from Campylobacter jejuni
Kim, Y., Gu, M., Papazisi, L., Anderson, W.F., Joachimiak, A.
To be Published