Function and Biology

Crystal structure of tetra mutant (D67E,A68P,L98I,A301S) of O-acetylserine sulfhydrylase from Salmonella typhimurium in complex with high-affinity inhibitory peptide from serine acetyltransferase of Salmonella typhimurium at 2.8 A

EC 2.5.1.47: Cysteine synthase

Reaction catalysed:
O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate
Systematic name:
O-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
Alternative Name(s):
  • 3-O-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
  • Acetylserine sulfhydrylase
  • Cysteine synthetase
  • O(3)-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide)
  • O(3)-acetyl-L-serine:hydrogen-sulfide 2-amino-2-carboxyethyltransferase
  • O-acetyl-L-serine sulfhydrylase
  • O-acetyl-L-serine sulfohydrolase
  • O-acetylserine (thiol)-lyase
  • O-acetylserine (thiol)-lyase A
  • O-acetylserine sulfhydrylase
  • OAS sulfhydrylase

Sequence family

Pfam Protein family (Pfam)
PF00291
Domain description: Pyridoxal-phosphate dependent enzyme
Occurring in:
  1. Cysteine synthase
The deposited structure of PDB entry 7yom contains 1 copy of Pfam domain PF00291 (Pyridoxal-phosphate dependent enzyme) in Cysteine synthase. Showing 1 copy in chain A.