| Accession | TIGR02715 |
| Name | amido_AtzE |
| Function | amidohydrolase, AtzE family |
| Trusted Cutoff | 425.75 |
| Domain Trusted Cutoff | 425.75 |
| Noise Cutoff | 371.70 |
| Domain Noise Cutoff | 371.70 |
| Isology Type | subfamily |
| EC Number | 3.-.-.- |
| HMM Length | 452 |
| Mainrole Category | Unknown function |
| Subrole Category | Enzymes of unknown specificity |
| Gene Ontology Term | GO:0016811: hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides molecular_function |
| Author | Haft DH |
| Entry Date | Dec 1 2005 4:34PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Members of this protein family are aminohydrolases related to, but distinct from, glutamyl-tRNA(Gln) amidotransferase subunit A. The best characterized member is the biuret hydrolase of Pseudomonas sp. ADP, which hydrolyzes ammonia from the three-nitrogen compound biuret to yield allophanate. Allophanate is also an intermediate in urea degradation by the urea carboxylase/allophanate hydrolase pathway, an alternative to urease. |
| References | RN [1]
RM 16085834
RT Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism.
RA Cheng G, Shapir N, Sadowsky MJ, Wackett LP.
RL Appl Environ Microbiol. 2005 Aug;71(8):4437-45. |
