EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.1.3.37 | additional information | construction of a variety of truncated forms of isoform AlgE1. An A module alone is sufficient for epimerization and module A1 catalyzes the formation of contiguous stretches of G residues in the polymer, while module A2 introduces single G residues. The epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally | Azotobacter vinelandii |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
5.1.3.37 | extracellular | - |
Azotobacter vinelandii | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.1.3.37 | Ca2+ | the epimerization reaction is Ca2+ dependent, and both the A and R modules bind this cation. The R modules appear to reduce the Ca2+ concentration needed for full activity and also stimulate the reaction rate when positioned both N- and C-terminally | Azotobacter vinelandii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.3.37 | Azotobacter vinelandii | Q44494 | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.1.3.37 | More | enzyme is composed of repeats of two protein modules designated A (385 amino acids) and R (153 amino acids). The modular structure of isoform AlgE1 is A1R1R2R3A2R4. AlgE1 has two catalytic sites for epimerization, each site introducing a different G distribution pattern | Azotobacter vinelandii |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
5.1.3.37 | AlgE1 | - |
Azotobacter vinelandii |