Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009033 | molecular_function | trimethylamine-N-oxide reductase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009061 | biological_process | anaerobic respiration |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030151 | molecular_function | molybdenum ion binding |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050626 | molecular_function | trimethylamine-N-oxide reductase (cytochrome c) activity |
Functional Information from PROSITE/UniProt
| site_id | PS00490 |
| Number of Residues | 18 |
| Details | MOLYBDOPTERIN_PROK_2 Prokaryotic molybdopterin oxidoreductases signature 2. TaTArhADIVLPaTTsyE |
| Chain | Residue | Details |
| A | THR463-GLU480 | |
| site_id | PS00932 |
| Number of Residues | 28 |
| Details | MOLYBDOPTERIN_PROK_3 Prokaryotic molybdopterin oxidoreductases signature 3. AaarGIaDgDvLrVfNdrGqilvgAkVS |
| Chain | Residue | Details |
| A | ALA676-SER703 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 17 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TRP116 | |
| A | GLN458 | |
| A | ARG481 | |
| A | ASP511 | |
| A | ALA641 | |
| A | ARG647 | |
| A | HIS649 | |
| A | ASN737 | |
| A | GLY754 | |
| A | SER147 | |
| A | LYS190 | |
| A | ILE220 | |
| A | GLN241 | |
| A | TRP322 | |
| A | ARG326 | |
| A | ASN434 | |
| A | HIS438 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 8658134 |
| Chain | Residue | Details |
| A | TYR114 | |
| A | TRP116 | |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 701 |
| Chain | Residue | Details |
| A | TYR114 | electrostatic stabiliser |
| A | TRP116 | steric role |
