CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.70.260
Functional Family D-3-phosphoglycerate dehydrogenase

Enzyme Information

1.1.1.95
Phosphoglycerate dehydrogenase.
based on mapping to UniProt P0A9T0
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.
1.1.1.399
2-oxoglutarate reductase.
based on mapping to UniProt P0A9T0
(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.

UniProtKB Entries (1)

P0A9T0
SERA_ECOLI
Escherichia coli K-12
D-3-phosphoglycerate dehydrogenase

PDB Structure

PDB 1YBA
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Vmax Regulation through Domain and Subunit Changes. The Active Form of Phosphoglycerate Dehydrogenase
Thompson, J.R., Bell, J.K., Bratt, J., Grant, G.A., Banaszak, L.J.
Biochemistry