CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.2300 | Response regulator |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.2300 |
| Functional Family |
Enzyme Information
| 1.20.4.1 |
Arsenate reductase (glutaredoxin).
based on mapping to UniProt P74313
Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H(2)O.
-!- A molybdoenzyme. -!- The enzyme is part of a system for detoxifying arsenate. -!- Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 7.3.2.7; in other organisms, arsenite can be methylated by EC 2.1.1.137 in a pathway that produces non-toxic organoarsenical compounds (cf. EC 1.20.4.4). -!- Formerly EC 1.97.1.5.
|
| 3.1.3.48 |
Protein-tyrosine-phosphatase.
based on mapping to UniProt P74313
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
-!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.
|
UniProtKB Entries (1)
| P74313 |
ARSC_SYNY3
Synechocystis sp. PCC 6803 substr. Kazusa
Glutaredoxin arsenate reductase
|
PDB Structure
| PDB | 2MYT |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.
J.Biol.Chem.
|