Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues, multifrequency EPR studies on the Mn2+ centers of oxalate decarboxylase, overview | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Oxalate | Bacillus subtilis | - |
Formate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
oxalate = formate + CO2 | catalytic mechanism | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Oxalate | - |
Bacillus subtilis | Formate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme is composed of two cupin domains, each of which contains a Mn2+ ion coordinated by four identical conserved residues | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
OXDC | - |
Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4 | - |
- |
Bacillus subtilis |