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InterPro: IPR012734 Dihydroxyacetone kinase

Protein matchesHelp
UniProtKB
Matches:
122 proteins
AccessionHelp IPR012734 DhaK_ATP
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR004006 Dak kinase
IPR004007 Dak phosphatase
GO Term annotationHelp
Function GO:0004371 glycerone kinase activity
GO:0005524 ATP binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family consists of examples of the single chain form of dihydroxyacetone kinase (also called glycerone kinase) that uses ATP (EC:2.7.1.29) as the phosphate donor, rather than a phosphoprotein as in Escherichia coli. This form has separable domains homologous to the K and L subunits of the E. coli enzyme, and is found in yeasts and other eukaryotes and in some bacteria, including Citrobacter freundii. The member from tomato has been shown to phosphorylate dihydroxyacetone, 3,4-dihydroxy-2-butanone, and some other aldoses and ketoses [1].

Structural linksHelp
Database linksHelp
Enzyme: EC:2.7.1.29
PRIAM: PRI001940

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012734 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P43550 Dihydroxyacetone kinase 2

P45510 Dihydroxyacetone kinase

Q3LXA3 Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)

Q4KLZ6 Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)

Q8VC30 Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR004006 Dak kinase
IPR004007 Dak phosphatase
IPR012734 Dihydroxyacetone kinase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain

PublicationsHelp
1. Herz S, Kis K, Bacher A, Rohdich F.
A tomato enzyme catalyzing the phosphorylation of 3,4-dihydroxy-2-butanone.
Phytochemistry 60 3-11 2002 [PubMed: 11985845]
http://dx.doi.org/10.1016/S0031-9422(02)00056-0

Additional ReadingHelp
Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B.
Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.
J. Biol. Chem. 278 2003 48236-44 [PubMed: 12966101]
http://dx.doi.org/10.1074/jbc.M305942200
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InterPro 24.0