| Accession | TIGR01747 |
| Name | diampropi_NH3ly |
| Function | diaminopropionate ammonia-lyase family |
| Trusted Cutoff | 274.00 |
| Domain Trusted Cutoff | 274.00 |
| Noise Cutoff | 112.90 |
| Domain Noise Cutoff | 112.90 |
| Isology Type | subfamily |
| EC Number | 4.3.1.15 |
| HMM Length | 376 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Other |
| Gene Ontology Term | GO:0008152: metabolic process biological_process |
| | GO:0008838: diaminopropionate ammonia-lyase activity molecular_function |
| Author | Haft DH |
| Entry Date | Nov 15 2002 4:40PM |
| Last Modified | Dec 12 2011 9:27PM |
| Comment | This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). |
| References | DR EXPERIMENTAL; SP|P40817|DPAL_SALTY;
RM 3275662
RT Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme, and sequence determination of the pyridoxal 5'-phosphate binding peptide.
RA Nagasawa T, Tanizawa K, Satoda T, Yamada H.
RL J Biol Chem 1988 Jan 15;263(2):958-64 |
