1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR000573 | Domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain |
| Type: | Family | Name: | Hydrolyase LeuD/DmdB, bacterial |
| Description: | This entry includes 3-isopropylmalate dehydratase small subunit LeuD from Heliobacterium modesticaldum and 2,3-dimethylmalate dehydratase small subunit DmdB from Eubacterium barkeri []. The structure of the Pyrococcus horikoshiismall subunit () has recently been determined []. As expected the structure of this polypeptide is similar to that of aconitase domain 4, though one alpha helix is replaced by a short loop with relatively high temperature factor values. This loop region is thought to be important for substrate recognition. Unlike other aconitase family proteins, this subunit formed a tetramer through disulphide linkages, though it is not expected to interfere with its interaction with the large subunit. These disulphide linkages would be expected to confer thermostability on the enzyme, reflecting the thermophilic lifestyle of the organism.Homoaconitase, aconitase, and 3-isopropylmalate dehydratase have similar overall structures. All are dehydratases and bind a [4Fe-4S]-cluster. 3-isopropylmalate dehydratase is split into large (leuC) and small (leuD) chains in eubacteria. Several pairs of archaeal proteins resemble the leuC and leuD pair in length and sequence but even more closely resemble the respective domains of homoaconitase, and their identity is uncertain. | Short Name: | LeuD/DmdB_bac |
| DB identifier | Type | Name |
|---|---|---|
| IPR000573 | Domain | Aconitase A/isopropylmalate dehydratase small subunit, swivel domain |
