Hydrolyase LeuD/HacB/DmdB (IPR011827)

Short name: LeuD_type2/HacB/DmdB

Overlapping homologous superfamilies

Family relationships


This entry is most closely related to the 3-isopropylmalate dehydratase IPR004431. It includes methanogen homoaconitase small subunit HacB from Methanocaldococcus jannaschii [PMID: 18765671, PMID: 20170198], 3-isopropylmalate dehydratase small subunit LeuD from Salmonella typhimurium [PMID: 2993799] and 2,3-dimethylmalate dehydratase small subunit DmdB from Eubacterium barkeri [PMID: 6489933].

The structure of the Pyrococcus horikoshii small subunit (O59393) has recently been determined [PMID: 15522288]. 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.

GO terms

Biological Process

GO:0008152 metabolic process

Molecular Function

GO:0016836 hydro-lyase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.