CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.260 | ACT domain |
Domain Context
CATH Clusters
| Superfamily | 3.30.70.260 |
| Functional Family | D-3-phosphoglycerate dehydrogenase |
Enzyme Information
| 1.1.1.399 |
2-oxoglutarate reductase.
based on mapping to UniProt P9WNX3
(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 P9WNX3
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)
| P9WNX3 |
SERA_MYCTU
Mycobacterium tuberculosis H37Rv
D-3-phosphoglycerate dehydrogenase
|
PDB Structure
| PDB | 1YGY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase: EXTREME ASYMMETRY IN A TETRAMER OF IDENTICAL SUBUNITS
J.Biol.Chem.
|
