CATH Domain 3e77C02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.1150	Aspartate Aminotransferase, domain 1
	3.90.1150.10	Aspartate Aminotransferase, domain 1

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 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	PDBSum Proteopedia
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