Expasy logo

ENZYME

ENZYME entry: EC 1.1.98.7

Accepted Name
serine-type anaerobic sulfatase-maturating enzyme
Reaction catalysed
L-seryl-[sulfatase] + S-adenosyl-L-methionine <=> 3-oxo-L-alanyl-[sulfatase] + 5'-deoxyadenosine + H(+) + L-methionine
Comment(s)
  • 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 3.1.6.1) 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 1.8.98.7.
Cross-references
BRENDA1.1.98.7
EC2PDB1.1.98.7
ExplorEnz1.1.98.7
PRIAM enzyme-specific profiles1.1.98.7
KEGG Ligand Database for Enzyme Nomenclature1.1.98.7
IUBMB Enzyme Nomenclature1.1.98.7
IntEnz1.1.98.7
MEDLINEFind literature relating to 1.1.98.7
MetaCyc1.1.98.7
Rhea expert-curated reactions1.1.98.7
UniProtKB/Swiss-Prot
Q02550, ANSME_BACTNP20714, ANSME_KLEAEQ9X758, ANSME_KLEPN

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.98.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-