Protein Variants | Comment | Organism |
---|---|---|
additional information | mutation of Glu 333 present in domain II leads to a reduction in the activity of the enzyme | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | the enzyme has two domains, each containing a Mn(II) ion coordinated with three histidine residues, binding structure in domain I, overview | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
oxalate + H+ | Bacillus subtilis | - |
formate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
oxalate + H+ | - |
Bacillus subtilis | formate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
OXDC | - |
Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
O2 | required | Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
additional information | analysis of transport of the product, i.e., CO2, from the reaction center to the surface of the enzyme using atomistic molecular dynamics simulations. Structure-function analysis using protein crystal structure, PDB ID 1L3J, simulations, overview. Domain I is the active site domain, while domain II is nonreceptive to hosting the formate and is incapable of releasing the CO2 molecule | Bacillus subtilis |