PROSITE documentation PDOC51480
DhaL domain profile


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 utilize, 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) (see <PDOC51481>) 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) (see <PDOC00528>) [1,2].

The DhaL domain consists of eight antiparallel α-helices arranged in an up-and-down geometry and aligned on a circle (see <PDB:1UN8>). This results in the formation of a helix barrel enclosing a deep pocket. The helices are amphipathic with the hydrophobic side chains directed into the pocket of the barrel and with the polar residues exposed. The nucleotide is bound on the top of the barrel [1,3].

The DhaL α helix barrel fold appears not only as C-terminal domain in Dha kinases but also as N-terminal domain in a family of two-domain proteins with unknown function. One representative example is YfhG of Lactococcus lactis [3].

The profile we developed covers the entire DhaL domain.

Last update:

February 2010 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

DHAL, PS51480; DhaL domain profile  (MATRIX)


1AuthorsOberholzer A.E. Schneider P. Baumann U. Erni B.
TitleCrystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase.
SourceJ. Mol. Biol. 359:539-545(2006).
PubMed ID16647083

2AuthorsZurbriggen A. Jeckelmann J.-M. Christen S. Bieniossek C. Baumann U. Erni B.
TitleX-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex.
SourceJ. Biol. Chem. 283:35789-35796(2008).
PubMed ID18957416

3AuthorsSiebold C. Arnold I. Garcia-Alles L.F. Baumann U. Erni B.
TitleCrystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.
SourceJ. Biol. Chem. 278:48236-48244(2003).
PubMed ID12966101

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