CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family D-3-phosphoglycerate dehydrogenase

Enzyme Information

1.1.1.37
Malate dehydrogenase.
based on mapping to UniProt O43175
(S)-malate + NAD(+) = oxaloacetate + NADH.
-!- Also oxidizes some other 2-hydroxydicarboxylic acids.
1.1.1.399
2-oxoglutarate reductase.
based on mapping to UniProt O43175
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH.
-!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95.
1.1.1.95
Phosphoglycerate dehydrogenase.
based on mapping to UniProt O43175
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH.
-!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.

UniProtKB Entries (1)

O43175
SERA_HUMAN
Homo sapiens
D-3-phosphoglycerate dehydrogenase

PDB Structure

PDB 5N53
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Validating and enabling phosphoglycerate dehydrogenase (PHGDH) as a target for fragment-based drug discovery in PHGDH-amplified breast cancer.
Unterlass, J.E., Basle, A., Blackburn, T.J., Tucker, J., Cano, C., Noble, M.E.M., Curtin, N.J.
Oncotarget