Reviewed, UniProtKB/Swiss-Prot Q4KLZ6 (DHAK_RAT)

Names and origin

Protein names

Recommended name:
    Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
Including the following 2 domains:
    1- Recommended name:
            ATP-dependent dihydroxyacetone kinase
                Short name=DHA kinase
              EC=2.7.1.29
        Alternative name(s):
            Glycerone kinase
    2- Recommended name:
            FAD-AMP lyase (cyclizing)
              EC=4.6.1.15
        Alternative name(s):
            FAD-AMP lyase (cyclic FMN forming)
            FMN cyclase

Gene names

Name:

Dak

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	578 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes both the phosphorylation of dihydroxyacetone and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Ref.2
Catalytic activity	ATP + glycerone = ADP + glycerone phosphate. FAD = AMP + riboflavin cyclic-4',5'-phosphate.
Cofactor	Magnesium By similarity. Manganese or cobalt; for FAD-AMP lyase activity. Ref.3
Enzyme regulation	Each activity is inhibited by the substrate(s) of the other.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the dihydroxyacetone kinase (DAK) family. Contains 1 DAK1 (dihydroxyacetone kinase subunit 1) domain. Contains 1 DAK2 (dihydroxyacetone kinase subunit 2) domain.
Biophysicochemical properties	Kinetic parameters: KM=8.8 µM for FAD with manganese KM=12.5 µM for ADP-glucose with manganese KM=652 µM for UDP-glucose with manganese KM=606 µM for UDP-galactose with manganese KM=714 µM for UDP-xylose with manganese KM=107 µM for UDP-glucuronate with manganese KM=108 µM for UDP-galacturonate with manganese KM=416 µM for CDP-glucose with manganese KM=795 µM for CDP-glycerol with manganese KM=784 µM for GDP-glucose with manganese KM=343 µM for GDP-alpha-L-fucose with manganese KM=114 µM for FAD with cobalt KM=120 µM for ADP-glucose with cobalt KM=2550 µM for UDP-glucose with cobalt KM=3661 µM for UDP-galactose with cobalt KM=2354 µM for UDP-xylose with cobalt KM=539 µM for UDP-glucuronate with cobalt KM=759 µM for UDP-galacturonate with cobalt KM=3703 µM for CDP-glucose with cobalt KM=2031 µM for CDP-glycerol with cobalt KM=2246 µM for GDP-glucose with cobalt KM=991 µM for GDP-alpha-L-fucose with cobalt

Ontologies

Keywords
Ligand	ATP-binding Cobalt FAD Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Lyase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	glycerol metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FAD-AMP lyase (cyclizing) activity Inferred from electronic annotation. Source: EC cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW glycerone kinase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 578	578	Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)		PRO_0000121527
Regions
	Domain	18 – 340	323	DAK1
	Domain	398 – 571	174	DAK2
	Nucleotide binding	403 – 407	5	ATP By similarity
	Nucleotide binding	446 – 494	49	ATP By similarity
Sites
	Active site	221	1	Tele-hemiaminal-histidine intermediate By similarity
	Metal binding	396	1	Magnesium 2 By similarity
	Metal binding	401	1	Magnesium 1 By similarity
	Metal binding	401	1	Magnesium 2 By similarity
	Metal binding	403	1	Magnesium 1 By similarity
	Metal binding	403	1	Magnesium 2 By similarity
	Metal binding	404	1	Magnesium 2 By similarity
	Binding site	59	1	Dihydroxyacetone By similarity
	Binding site	114	1	Dihydroxyacetone By similarity
	Binding site	556	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4KLZ6-1 [UniParc]. Last modified August 2, 2005. Version 1. Checksum: C343482447F9770B	FASTA	578	59,444
	10 20 30 40 50 60 MSSKKMVNSV EGCAGDALAG FVACNPDLQL LQGYRVALRS DLDSLKGRVA LLSGGGSGHE 70 80 90 100 110 120 PAHAGFIGKG MLTGVIAGAV FASPAVGSIL AAIRAVAQAG TAGTLLIVKN YTGDRLNFGL 130 140 150 160 170 180 AMEQAKAEGI SVEMVVIEDD SAFTVLKKAG RRGLCGTILI HKVAGALAEE GMGLEEITKK 190 200 210 220 230 240 VSVIAKAIGT LGVSLSPCSV PGTKPTFELA ADEMELGLGI HGEAGVRRIK LVPVDQIVTL 250 260 270 280 290 300 MLDHMTDTSN ISHVPVKSGS SVVLMVNNLG GLSFLELGII ADAAIRLLEG RGVKVARALV 310 320 330 340 350 360 GTFMSALEMR GVSLTLMLVD EPLLKLIDAE TNAKAWPHMS KVSVTGRNRI RAAPTEPAEA 370 380 390 400 410 420 PEATAAGGVA SKQMTLVLDR ISTTLIGLEE HLNALDRAAG DGDCGSTHSR AAKAIQGWLK 430 440 450 460 470 480 EGPTPASPAQ VLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKANTDLPA WSAAMDAGLK 490 500 510 520 530 540 AMQKYGKAAP GDRTMLDSLW AAAQELQAWK SPGASLLPVL TKAVKSAEAA AEATKNMEAG 550 560 570 AGRASYISSA QLDQPDPGAV AAAAIFRAIL EVLQTKAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Brown Norway. Tissue: Testis.
[2]	"Identification of human and rat FAD-AMP lyase (cyclic FMN forming) as ATP-dependent dihydroxyacetone kinases." Cabezas A., Costas M.J., Pinto R.M., Couto A., Cameselle J.C. Biochem. Biophys. Res. Commun. 338:1682-1689(2005) [PubMed: 16289032] [Abstract] Cited for: FUNCTION, FAD-AMP LYASE ACTIVITY.
[3]	"Purification, characterization, and substrate and inhibitor structure-activity studies of rat liver FAD-AMP lyase (cyclizing): preference for FAD and specificity for splitting ribonucleoside diphosphate-X into ribonucleotide and a five-atom cyclic phosphodiester of X, either a monocyclic compound or a cis-bicyclic phosphodiester-pyranose fusion." Cabezas A., Pinto R.M., Fraiz F., Canales J., Gonzalez-Santiago S., Cameselle J.C. Biochemistry 40:13710-13722(2001) [PubMed: 11695920] [Abstract] Cited for: COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC098925 mRNA. Translation: AAH98925.1.
IPI	IPI00372498.
RefSeq	NP_001034120.1.
UniGene	Rn.55630
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q4KLZ6.
Genome annotation databases
Ensembl	ENSRNOG00000020704. Rattus norvegicus. [Contig view]
GeneID	361730.
KEGG	rno:361730.
NMPDR	fig|10116.3.peg.3721.
Organism-specific databases
RGD	1311026. Dak.
Phylogenomic databases
HOVERGEN	Q4KLZ6.
Enzyme and pathway databases
BRENDA	2.7.1.29. 248.
Gene expression databases
ArrayExpress	Q4KLZ6.
GermOnline	ENSRNOG00000020704. Rattus norvegicus.
Family and domain databases
InterPro	IPR004006. Dak1. IPR004007. Dak2. IPR012734. DhaK_ATP. [Graphical view]
Pfam	PF02733. Dak1. 1 hit. PF02734. Dak2. 1 hit. [Graphical view]
TIGRFAMs	TIGR02361. dak_ATP. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	677430.

Entry information

Entry name

DHAK_RAT

Accession

Primary (citable) accession number: Q4KLZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	August 2, 2005
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)