EC - Serine-type anaerobic sulfatase-maturating enzyme

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
serine-type anaerobic sulfatase-maturating enzyme
Systematic name:
[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)



A bacterial radical S-adenosyl-L-methionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC by converting a conserved L-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Szameit, C., Miech, C., Balleininger, M., Schmidt, B., von Figura, K., Dierks, T.
    The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.
    J. Biol. Chem. 274 : 15375-15381 (1999). [PMID: 10336424]
  2. Fang, Q., Peng, J., Dierks, T.
    Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB.
    J. Biol. Chem. 279 : 14570-14578 (2004). [PMID: 14749327]
  3. Grove, T. L., Lee, K. H., St Clair, J., Krebs, C., Booker, S. J.
    In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.
    Biochemistry 47 : 7523-7538 (2008). [PMID: 18558715]

[EC created 2020]