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

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

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.1
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 By similarity.
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.

Hide | Top

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Cobalt FAD Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Lyase Transferase
Technical term	Complete proteome 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...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 575

575

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

PRO_0000121525

Regions

Domain

18 – 340

323

DAK1

Domain

398 – 516

119

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

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

Natural variations

Natural variant

185

1

T → A: dbSNP rs2260655. Ref.4

VAR_028108

Natural variant

334

1

A → G: dbSNP rs35723406.

VAR_054780

Experimental info

Sequence conflict

7

1

V → A in BAB14722. Ref.2

Sequence conflict

19

1

A → S in BAD97300. Ref.3

Sequence conflict

75

1

V → A in BAB14722. Ref.2

Sequence conflict

376

1

L → P in BAB14722. Ref.2

Sequence conflict

497

1

D → G in BAB14722. Ref.2

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q3LXA3-1 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: D8C871622535E40D
Show »

FASTA

575

58,977

        10         20         30         40         50         60 
MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA LLSGGGSGHE 

        70         80         90        100        110        120 
PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG TVGTLLIVKN YTGDRLNFGL 

       130        140        150        160        170        180 
AREQARAEGI PVEMVVIGDD SAFTVLKKAG RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ 

       190        200        210        220        230        240 
VNVVTKAMGT LGVSLSSCSV PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL 

       250        260        270        280        290        300 
MLDHMTNTTN ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV 

       310        320        330        340        350        360 
GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS RVAPAEPQEA 

       370        380        390        400        410        420 
PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG DGDCGTTHSR AARAIQEWLK 

       430        440        450        460        470        480 
EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE 

       490        500        510        520        530        540 
AMQKYGKAAP GDRTMLDSLW AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG 

       550        560        570 
AGRASYISSA RLEQPDPGAV AAAAILRAIL EVLQS

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FAD-AMP LYASE ACTIVITY. Tissue: Brain.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thyroid.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[4]	"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], VARIANT ALA-185. Tissue: Cervix.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ138290 mRNA. Translation: ABA10576.1. AK023915 mRNA. Translation: BAB14722.1. AK223580 mRNA. Translation: BAD97300.1. BC001341 mRNA. Translation: AAH01341.1.
IPI	IPI00551024.
RefSeq	NP_056348.2.
UniGene	Hs.6278
3D structure databases
SMR	Q3LXA3. Positions 3-571.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3LXA3.
PTM databases
PhosphoSite	Q3LXA3.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00551024.
Proteomic databases
PRIDE	Q3LXA3.
Genome annotation databases
Ensembl	ENST00000311463; ENSP00000310493; ENSG00000149476; Homo sapiens. [Genome view] ENST00000394900; ENSP00000378360; ENSG00000149476; Homo sapiens. [Genome view]
GeneID	26007.
KEGG	hsa:26007.
UCSC	uc001nre.1. human.
Organism-specific databases
CTD	26007.
GeneCards	GC11P060858.
HGNC	HGNC:24552. DAK.
PharmGKB	PA142672014.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG473357.
HOVERGEN	Q3LXA3.
InParanoid	Q3LXA3.
PhylomeDB	Q3LXA3.
Enzyme and pathway databases
BRENDA	2.7.1.29. 247. 4.6.1.15. 247.
Gene expression databases
ArrayExpress	Q3LXA3.
Bgee	Q3LXA3.
CleanEx	HS_DAK.
Genevestigator	Q3LXA3.
GermOnline	ENSG00000149476. Homo sapiens.
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	47741.
PMAP-CutDB	Q3LXA3.

Hide | Top

Entry information

Entry name

DHAK_HUMAN

Accession

Primary (citable) accession number: Q3LXA3
Secondary accession number(s): Q53EQ9, Q9BVA7, Q9H895

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	October 25, 2005
Last modified:	February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Hide | Top

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents