CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.3330 | UraD-like |
|
1.10.3330.10 | Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase |
Domain Context
CATH Clusters
| Superfamily | Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase |
| Functional Family | Uric acid degradation bifunctional protein TTL |
Enzyme Information
| 3.5.2.17 |
Hydroxyisourate hydrolase.
based on mapping to UniProt Q9LVM5
5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro- 1H-imidazole-5-carboxylate.
-!- The reaction is the first stage in the conversion of 5-hydroxyisourate into (S)-allantoin. -!- This reaction will also occur spontaneously, but more slowly.
|
| 4.1.1.97 |
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase.
based on mapping to UniProt Q9LVM5
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.
|
UniProtKB Entries (1)
| Q9LVM5 |
TTHL_ARATH
Arabidopsis thaliana
Uric acid degradation bifunctional protein TTL
|
PDB Structure
| PDB | 2Q37 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and functional basis for (s)-allantoin formation in the ureide pathway.
J.Biol.Chem.
|
