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MGP004795

UniProt Annotations

Entry Information
Gene Namedihydroxyacetone kinase 2 homolog (S. cerevisiae)
Protein EntryDHAK_HUMAN
UniProt IDQ3LXA3
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q3LXA3-1; Sequence=Displayed; Name=2; IsoId=Q3LXA3-2; Sequence=VSP_057181; Note=Inactive as DHA kinase and FMN cyclase.;
Biophysicochemical PropertiesKinetic parameters: KM=0.5 uM for dihydroxyacetone {ECO:0000269|PubMed:4688871}; KM=11 uM for glyceraldehyde {ECO:0000269|PubMed:4688871}; pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:4688871};
Catalytic ActivityATP + D-glyceraldehyde = ADP + D- glyceraldehyde 3-phosphate. {ECO:0000269|PubMed:4688871}.
Catalytic ActivityATP + glycerone = ADP + glycerone phosphate. {ECO:0000269|PubMed:4688871}.
Catalytic ActivityFAD = AMP + riboflavin cyclic-4',5'-phosphate. {ECO:0000269|PubMed:4688871}.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Manganese or cobalt are requested for FAD-AMP lyase activity. {ECO:0000250};
Enzyme RegulationEach activity is inhibited by the substrate(s) of the other.
FunctionCatalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. {ECO:0000269|PubMed:16289032, ECO:0000269|PubMed:4688871}.
SimilarityBelongs to the dihydroxyacetone kinase (DAK) family. {ECO:0000305}.
SimilarityContains 1 DhaK domain. {ECO:0000255|PROSITE- ProRule:PRU00814}.
SimilarityContains 1 DhaL domain. {ECO:0000255|PROSITE- ProRule:PRU00813}.
SubunitHomodimer. {ECO:0000250}.
Tissue SpecificityDetected in erythrocytes (at protein level). {ECO:0000269|PubMed:4688871}.
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