DhaK domain (IPR004006)

Short name: DhaK_dom

Overlapping homologous superfamilies


Domain relationships


Dihydroxyacetone (Dha) kinases are a family of sequence-conserved enzymes that phosphorylate dihydroxyacetone, glyceraldehyde and other short-chain ketoses and aldoses. They can be divided into two groups according to the source of high-energy phosphate that they utilise, either ATP or phosphoenolpyruvate (PEP). The ATP-dependent forms are the two-domain Dha kinases (DAK), which occur in animals, plants and eubacteria. They consist of a Dha binding (K) and an ATP binding (L) domain. The PEP-dependent forms occur only in eubacteria and a few archaebacteria and consist of three subunits. Two subunits, DhaK and DhaL, are homologous to the K and L domains. Intriguingly, the ADP moiety is not exchanged for ATP but remains permanently bound to the DhaL subunit where it is rephosphorylated in situ by the third subunit, DhaM, which is homologous to the IIA domain of the mannose transporter of the bacterial PEP:sugar phosphotransferase system (PTS) [PMID: 16647083, PMID: 18957416].

The DhaK domain consists of two alpha/beta-folds, each containing a six- stranded mixed beta-sheet surrounded by six and three helices, respectively. Dha is bound in hemiaminal linkage to the imidazole nitrogen of an invariant histidine [PMID: 12966101, PMID: 12813127].

GO terms

Biological Process

GO:0006071 glycerol metabolic process

Molecular Function

GO:0004371 glycerone kinase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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