CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate Aminotransferase, domain 1
Functional Family Phosphoserine aminotransferase

Enzyme Information

2.6.1.52
Phosphoserine transaminase.
based on mapping to UniProt Q9RME2
(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 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5 (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)

Q9RME2
SERC_BACAO
Bacillus alcalophilus
Phosphoserine aminotransferase

PDB Structure

PDB 2BIE
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Strain Relief at the Active Site of Phosphoserine Aminotransferase Induced by Radiation Damage.
Dubnovitsky, A.P., Ravelli, R.B.G., Popov, A.N., Papageorgiou, A.C.
Protein Sci.