EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.2.1.25 | the active site contains a catalytically important [2Fe-2S] cluster and Mg2+ ion and is buried between two domains, and at the dimer interface. The active site Lys129 is carbamylated. Ser480 and Thr482 are essential residues for catalysis, and the S480A mutant structure shows an open conformation in which the active site is more accessible for the substrate. The alkoxide ion form of the Ser480 side chain may function as a base and the [2Fe-2S] cluster may function as a Lewis acid in the elimination reaction | Rhizobium leguminosarum bv. trifolii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.1.25 | S480A | completely inactive. Upon cocrystallization with calcium arabinonate, a partially bound substrate is observed in the pocket | Rhizobium leguminosarum bv. trifolii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.25 | Rhizobium leguminosarum bv. trifolii | I9XDU6 | - |
- |
4.2.1.25 | Rhizobium leguminosarum bv. trifolii WSM597 | I9XDU6 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.25 | Rleg9DRAFT_6269 | - |
Rhizobium leguminosarum bv. trifolii |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.25 | [2Fe-2S]-center | presence of a planar [2Fe-2S] cluster in the N-terminal domain, where Fe1 is tetrahedrally coordinated by two bridging sulfide ions and two cysteines and Fe2 is three-coordinated by two bridging sulfides and one cysteine (Cys200) | Rhizobium leguminosarum bv. trifolii |