CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1120 | Arylsulfatase, C-terminal domain |
|
3.30.1120.10 |
Domain Context
CATH Clusters
| Superfamily | 3.30.1120.10 |
| Functional Family | Arylsulfatase A |
Enzyme Information
| 3.1.6.1 |
Arylsulfatase (type I).
based on mapping to UniProt P51691
A phenol sulfate + H(2)O = a phenol + sulfate.
-!- Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-beta-lactamase fold and binds two zinc ions as cofactors. -!- Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. -!- The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. -!- This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC 1.8.3.7, EC 1.1.98.-, serine-type anaerobic sulfatase-maturating enzyme, or EC 1.8.98.-, cysteine-type anaerobic sulfatase-maturating enzyme.
|
UniProtKB Entries (1)
| P51691 |
ARS_PSEAE
Pseudomonas aeruginosa PAO1
Arylsulfatase
|
PDB Structure
| PDB | 4CXK |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Evolutionary repurposing of a sulfatase: A new Michaelis complex leads to efficient transition state charge offset.
Proc. Natl. Acad. Sci. U.S.A.
|
