CATH Classification

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
Oda, Y., Mino, K., Ishikawa, K., Ataka, M.
J.Mol.Biol.