CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1580 | paralog of FGE (formylglycine-generating enzyme) |
|
3.90.1580.10 | paralog of FGE (formylglycine-generating enzyme) |
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.
Acta Crystallogr.,Sect.D
|