bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing); includes: ATP-dependent dihydroxyacetone kinase; DHA kinase; glycerone kinase; FAD-AMP lyase (cyclizing); FAD-AMP lyase (cyclic FMN forming); FMN cyclase (DAK)

Function: - catalyzes both the phosphorylation of dihydroxyacetone & splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate - each activity is inhibited by the substrate(s) of the other ATP + glycerone = ADP + glycerone phosphate FAD = AMP + riboflavin cyclic-4',5'-phosphate Cofactor: - Mg⁺² (putative) - Mn+2 or cobalt; for FAD-AMP lyase activity Structure: - homodimer (putative) - belongs to the dihydroxyacetone kinase (DAK) family - contains 1 DhaK domain - contains 1 DhaL domain

Properties

SIZE: entity length = 575 aa MW = 59 kD MOTIF: DhaK {9-336} MOTIF: Dihydroxyacetone binding {56-59} binding site SITE: 109-109 FOR-BINDING-OF: Dihydroxyacetone binding site SITE: 114-114 FOR-BINDING-OF: Dihydroxyacetone histidine residue {H221} kinase domain MOTIF: ATP-binding site NAME: ATP-binding site DhaL {372-571} MOTIF: ATP-binding site NAME: ATP-binding site SITE: 401-404 ATP-binding site NAME: ATP-binding site SITE: 446-447 ATP-binding site NAME: ATP-binding site SITE: 486-486 ATP-binding site NAME: ATP-binding site SITE: 494-495 ATP-binding site NAME: ATP-binding site SITE: 556-558

Database Correlations

UniProt Q3LXA3 PFAM correlations Entrez Gene 26007 Kegg hsa:26007 ENZYME correlations

References

UniProt :accession Q3LXA3