CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
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 2PA3
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The Effect of Hinge Mutations on Effector Binding and Domain Rotation in Escherichia coli D-3-Phosphoglycerate Dehydrogenase.
Dey, S., Hu, Z., Xu, X.L., Sacchettini, J.C., Grant, G.A.
J.Biol.Chem.
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