CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1090 | Dehydroquinate synthase-like, alpha domain |
|
1.20.1090.10 | Dehydroquinate synthase-like - alpha domain |
Domain Context
CATH Clusters
| Superfamily | Dehydroquinate synthase-like - alpha domain |
| Functional Family |
Enzyme Information
| 1.1.1.261 |
sn-glycerol-1-phosphate dehydrogenase.
based on mapping to UniProt A3MTM6
sn-glycerol 1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H.
-!- Responsible for the formation of archaea-specific sn-glycerol-1- phosphate, the first step in the biosynthesis of polar lipids in archaea. -!- It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. -!- The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP- unsaturated archaeol. -!- The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine. -!- Activity of the enzyme is stimulated by K(+).
|
UniProtKB Entries (1)
| A3MTM6 |
G1PDH_PYRCJ
Pyrobaculum calidifontis JCM 11548
Glycerol-1-phosphate dehydrogenase [NAD(P)+]
|
PDB Structure
| PDB | 5FB3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Unique coenzyme binding mode of hyperthermophilic archaeal sn-glycerol-1-phosphate dehydrogenase from Pyrobaculum calidifontis
Proteins
|
