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InterPro: IPR004006 Dak kinase

Protein matches Help

UniProtKB

Matches:

1185 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR004006 Dak1

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02733	Dak1	1185
Signatures in BioMart

InterPro Relationships Help

Children

IPR012736 Dihydroxyacetone kinase DhaK, subunit 1

Found in

IPR012734 Dihydroxyacetone kinase
IPR012735 Dihydroxyacetone kinase DhaK, subunit 1b

GO Term annotation Help

Process

GO:0006071 glycerol metabolic process

Function

GO:0004371 glycerone kinase activity

InterPro annotation

Entry Details in BioMart

Abstract

Dihydroxyacetone kinase (glycerone kinase) EC:2.7.1.29 catalyses the phosphorylation of glycerone in the presence of ATP to glycerone phosphate in the glycerol utilization pathway. This is the kinase domain of the dihydroxyacetone kinase family.

Structural links Help

PDB - click here

SCOP: c.119.1.2

CATH: 3.30.1180.20 , 3.40.50.10440

Database links Help

Enzyme: EC:2.7.1

PANDIT: PF02733

Blocks: IPB004006

CluSTr: ALLvsALL:39163:45.5

Pfam Clan: CL0245.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004006

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

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

Publications Help

Additional Reading Open in usermanual
	Siebold C, Garcia-Alles LF, Erni B, Baumann U. A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase. Proc. Natl. Acad. Sci. U.S.A. 100 2003 8188-92 [PubMed: 12813127] http://dx.doi.org/10.1073/pnas.0932787100
	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
	Garcia-Alles LF, Siebold C, Nyffeler TL, Flukiger-Bruhwiler K, Schneider P, Burgi HB, Baumann U, Erni B. Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism. Biochemistry 43 2004 13037-45 [PubMed: 15476397] http://dx.doi.org/10.1021/bi048575m

InterPro 24.0