CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1300 | Amidase signature (AS) enzymes |
|
3.90.1300.10 | Amidase signature (AS) domain |
Domain Context
CATH Clusters
| Superfamily | Amidase signature (AS) domain |
| Functional Family |
Enzyme Information
| 3.5.1.54 |
Allophanate hydrolase.
based on mapping to UniProt Q936X2
Urea-1-carboxylate + H(2)O = 2 CO(2) + 2 NH(3).
-!- Along with EC 3.5.2.15 and EC 3.5.1.84, forms part of the cyanuric- acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine (2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5- triazine), in bacteria. -!- The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 6.3.4.6, thus bringing about the hydrolysis of urea to CO(2) and NH(3) in the presence of ATP and bicarbonate. -!- The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate.
|
UniProtKB Entries (1)
| Q936X2 |
ATZF_PSESD
Pseudomonas sp. ADP
Allophanate hydrolase
|
PDB Structure
| PDB | 4CP8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
X-Ray Structure of the Amidase Domain of Atzf, the Allophanate Hydrolase from the Cyanuric Acid-Mineralizing Multienzyme Complex.
Appl.Environ.Microbiol.
|
