Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Streptomyces viridochromogenes |
Crystallization (Comment) | Organism |
---|---|
to 1.8 A resolution. The overall structure consists of imperfect tandem repeats of a bi-domain architecture. Each of the repeats is composed of an all-alpha-helical domain linked to a beta-barrel fold characteristic of the cupin superfamily. A Cd(II) ion is situated at the base of the active site and is coordinated by residues His 129, Glu 176 and His 182 | Streptomyces viridochromogenes |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | mononuclear non-haem iron(II)-dependent enzyme | Streptomyces viridochromogenes |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces viridochromogenes | Q5IW40 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | all four electrons required for reduction of O2 are provided by the substrate. Occurence of an intermediate species in which oxygen derived from O2 exchanges with water | ? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no cofactors required | Streptomyces viridochromogenes |