CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1100 |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.1100 |
| Functional Family |
Enzyme Information
| 4.2.1.22 |
Cystathionine beta-synthase.
based on mapping to UniProt Q9YBL2
L-serine + L-homocysteine = L-cystathionine + H(2)O.
-!- A multifunctional enzyme: catalyzes beta-replacement reaction between L-serine, L-cysteine, cysteine thioethers or some other beta- substituted alpha-L-amino acids and a variety of mercaptans. -!- Formerly EC 4.2.1.21.
|
| 2.5.1.47 |
Cysteine synthase.
based on mapping to UniProt Q9YBL2
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.
-!- Some alkyl thiols, cyanide, pyrazole and some other heterocyclic compounds can act as acceptors. -!- Not identical with EC 2.5.1.51, EC 2.5.1.52 and EC 2.5.1.53. -!- Formerly EC 4.2.99.8.
|
| 2.5.1.65 |
O-phosphoserine sulfhydrylase.
based on mapping to UniProt Q9YBL2
O-phospho-L-serine + hydrogen sulfide = L-cysteine + phosphate.
-!- The enzyme from Aeropyrum pernix acts on both O-phospho-L-serine and O(3)-acetyl-L-serine, in contrast with EC 2.5.1.47, which acts only on O(3)-acetyl-L-serine.
|
UniProtKB Entries (1)
| Q9YBL2 |
CYSO_AERPE
Aeropyrum pernix K1
Protein CysO
|
PDB Structure
| PDB | 1WKV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Three-dimensional Structure of a New Enzyme, O-Phosphoserine Sulfhydrylase, involved in l-Cysteine Biosynthesis by a Hyperthermophilic Archaeon, Aeropyrum pernix K1, at 2.0A Resolution
J.Mol.Biol.
|
