CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

2.6.1.52
Phosphoserine transaminase.
based on mapping to UniProt Q9Y617
(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)

Q9Y617
SERC_HUMAN
Homo sapiens
Phosphoserine aminotransferase

PDB Structure

PDB 3E77
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Human phosphoserine aminotransferase in complex with PLP
Lehtio, L., Karlberg, T., Andersson, J., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Kotenyova, T., Moche, M., Nilsson, M.E., Nordlund, P., Nyman, T., Olesen, K., Persson, C., Sagemark, J., Thorsell, S.G., Tresaugues, L., Van Den Berg, S., Welin, M., Wikstrom, M., Wisniewska, M., Weigelt, J., Schueler, H., Structural Genomics Consortium (SGC)
TO BE PUBLISHED