CATH Classification

Domain Context

CATH Clusters

Superfamily HAD superfamily/HAD-like
Functional Family Pyridoxal phosphate phosphatase

Enzyme Information

3.1.3.3
Phosphoserine phosphatase.
based on mapping to UniProt Q96GD0
O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate.
3.1.3.74
Pyridoxal phosphatase.
based on mapping to UniProt Q96GD0
Pyridoxal 5'-phosphate + H(2)O = pyridoxal + phosphate.
-!- Specific for phosphorylated vitamin B(6) compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. -!- This reaction can also be carried out by EC 3.1.3.1 and EC 3.1.3.2, but these enzymes have very broad substrate specificities.

UniProtKB Entries (1)

Q96GD0
PLPP_HUMAN
Homo sapiens
Pyridoxal phosphate phosphatase

PDB Structure

PDB 2P27
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural genomics of protein phosphatases.
Almo, S.C., Bonanno, J.B., Sauder, J.M., Emtage, S., Dilorenzo, T.P., Malashkevich, V., Wasserman, S.R., Swaminathan, S., Eswaramoorthy, S., Agarwal, R., Kumaran, D., Madegowda, M., Ragumani, S., Patskovsky, Y., Alvarado, J., Ramagopal, U.A., Faber-Barata, J., Chance, M.R., Sali, A., Fiser, A., Zhang, Z.Y., Lawrence, D.S., Burley, S.K.
J.Struct.Funct.Genom.