| Accession | TIGR03860 |
| Name | FMN_nitrolo |
| Function | FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family |
| Trusted Cutoff | 279.70 |
| Domain Trusted Cutoff | 279.70 |
| Noise Cutoff | 262.35 |
| Domain Noise Cutoff | 262.35 |
| Isology Type | subfamily |
| EC Number | 1.-.-.- |
| HMM Length | 422 |
| Mainrole Category | Unknown function |
| Subrole Category | Enzymes of unknown specificity |
| Gene Ontology Term | GO:0008152: metabolic process biological_process |
| | GO:0016491: oxidoreductase activity molecular_function |
| | GO:0050662: coenzyme binding molecular_function |
| Author | Haft DH |
| Entry Date | Oct 12 2009 8:36AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model represents a distinctive clade, in which all characterized members are FMN-binding, within the larger family of luciferase-like monooxygenases (LLM), among which there are both FMN- and F420-binding enzymes. A well-characterized member is nitrilotriacetate monooxygenase from Aminobacter aminovorans (Chelatobacter heintzii), where nitrilotriacetate is a chelating agent used in detergents. |
| References | DR EXPERIMENTAL; SP|P54989; Nitrilotriacetate monooxygenase
RN [1]
RM PMID:9023192
RT Cloning, sequencing, and analysis of a gene cluster from Chelatobacter heintzii ATCC 29600 encoding nitrilotriacetate monooxygenase and NADH:flavin mononucleotide oxidoreductase.
RA Xu Y, Mortimer MW, Fisher TS, Kahn ML, Brockman FJ, Xun L
RL J Bacteriol. 1997 Feb;179(4):1112-6. |
