CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.270 | Urate Oxidase |
|
3.10.270.10 | Urate Oxidase; |
Domain Context
CATH Clusters
| Superfamily | Urate Oxidase; |
| Functional Family |
Enzyme Information
| 4.1.1.97 |
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase.
based on mapping to UniProt Q45697
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)- allantoin + CO(2).
-!- This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans). -!- Formerly EC 4.1.1.n1.
|
| 1.7.3.3 |
Factor independent urate hydroxylase.
based on mapping to UniProt Q45697
Urate + O(2) + H(2)O = 5-hydroxyisourate + H(2)O(2).
-!- Was previously thought to be a copper protein, but it is now known that the enzymes from soybean (Glycine max), the mold Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. -!- The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO(2), although there is an enzyme-catalyzed pathway in which EC 3.5.2.17 catalyzes the first step. -!- The enzyme is different from EC 1.14.13.113.
|
UniProtKB Entries (1)
| Q45697 |
PUCL_BACSB
Bacillus sp. TB-90
Uric acid degradation bifunctional protein
|
PDB Structure
| PDB | 1J2G |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of urate oxidase from Bacillus SP.
To be Published
|
