Mannitol dehydrogenase, C-terminal (IPR013118)

Short name: Mannitol_DH_C

Overlapping homologous superfamilies

Domain relationships



Long-chain mannitol dehydrogenases are a group of secondary alcohol dehydrogenases that differ from other alcohol or polyol dehydrogenases in that they do not utilise Zn(2+) or other metal cofactors and do not contain a conserved catalytic tyrosine residue. The proteins in this family that have been studied are monomeric enzymes of ~54 kDa and include:

These enzymes are mostly found in bacteria, though they are also present in some fungal species.

This entry represents the C-terminal substrate-binding domain of long-chain mannitol dehydrogenases. This domain is primarily alpha-helical in nature, being composed of eleven helices and a small beta hairpin [PMID: 12196534]. Most of the residues implicated in substrate binding are located within this region, and a conserved lysine residue is thought to act as a proton acceptor during catalysis.

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0050662 coenzyme binding
GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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