CATH Classification

Domain Context

CATH Clusters

Superfamily paralog of FGE (formylglycine-generating enzyme)
Functional Family Sulfatase modifying factor 1

Enzyme Information

1.8.3.7
Formylglycine-generating enzyme.
based on mapping to UniProt Q8NBK3
A [sulfatase]-L-cysteine + O(2) + 2 a thiol = a [sulfatase]-3-oxo-L- alanine + hydrogen sulfide + a disulfide + H(2)O.
-!- The enzyme, which is found in both prokaryotes and eukaryotes, catalyzes a modification of a conserved L-cysteine residue in the active site of sulfatases, generating a unique 3-oxo-L-alanine residue that is essential for sulfatase activity. -!- The exact nature of the thiol involved is still not clear - dithiothreitol and cysteamine are the most efficiently used thiols in vitro. -!- Glutathione alo acts in vitro, but it is not known whether it is used in vivo.

UniProtKB Entries (1)

Q8NBK3
SUMF1_HUMAN
Homo sapiens
Formylglycine-generating enzyme

PDB Structure

PDB 2HIB
External Links
Method X-RAY DIFFRACTION
Organism Homo
Primary Citation
Probing the oxygen-binding site of the human formylglycine-generating enzyme using halide ions.
Roeser, D., Schmidt, B., Preusser-Kunze, A., Rudolph, M.G.
Acta Crystallogr.,Sect.D