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Q3LXA3 (DHAK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)

Including the following 2 domains:

  1. ATP-dependent dihydroxyacetone kinase
    Short name=DHA kinase
    EC=2.7.1.28
    EC=2.7.1.29
    Alternative name(s):
    Glycerone kinase
    Triokinase
    Triose kinase
  2. FAD-AMP lyase (cyclizing)
    EC=4.6.1.15
    Alternative name(s):
    FAD-AMP lyase (cyclic FMN forming)
    FMN cyclase
Gene names
Name:DAK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Ref.1 Ref.6

Catalytic activity

ATP + glycerone = ADP + glycerone phosphate. Ref.6

ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate. Ref.6

FAD = AMP + riboflavin cyclic-4',5'-phosphate. Ref.6

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.

Tissue specificity

Detected in erythrocytes (at protein level). Ref.6

Sequence similarities

Belongs to the dihydroxyacetone kinase (DAK) family.

Contains 1 DhaK domain.

Contains 1 DhaL domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 µM for dihydroxyacetone Ref.6

KM=11 µM for glyceraldehyde

pH dependence:

Optimum pH is 6.6.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
PRO_0000121525

Regions

Domain9 – 336328DhaK
Domain372 – 571200DhaL
Nucleotide binding401 – 4044ATP By similarity
Nucleotide binding446 – 4472ATP By similarity
Nucleotide binding494 – 4952ATP By similarity
Nucleotide binding556 – 5583ATP By similarity
Region56 – 594Dihydroxyacetone binding By similarity

Sites

Active site2211Tele-hemiaminal-histidine intermediate By similarity
Binding site1091Dihydroxyacetone By similarity
Binding site1141Dihydroxyacetone By similarity
Binding site4861ATP; via carbonyl oxygen By similarity

Natural variations

Natural variant1851A → T. Ref.1 Ref.2 Ref.3
Corresponds to variant rs2260655 [ dbSNP | Ensembl ].
VAR_028108
Natural variant3341A → G.
Corresponds to variant rs35723406 [ dbSNP | Ensembl ].
VAR_054780

Experimental info

Sequence conflict71V → A in BAB14722. Ref.2
Sequence conflict191A → S in BAD97300. Ref.3
Sequence conflict751V → A in BAB14722. Ref.2
Sequence conflict3761L → P in BAB14722. Ref.2
Sequence conflict4971D → G in BAB14722. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3LXA3 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: 4DB8C5326F65122C

FASTA57558,947
        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 
VNVVAKAMGT 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

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, FAD-AMP LYASE ACTIVITY, VARIANT THR-185.
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-185.
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], VARIANT THR-185.
Tissue: Kidney.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix.
[6]"Dihydroxyacetone metabolism by human erythrocytes: demonstration of triokinase activity and its characterization."
Beutler E., Guinto E.
Blood 41:559-568(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, IDENTITY OF TRIOKINASE AND DIHYDROXYACETONE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ138290 mRNA. Translation: ABA10576.1.
AK023915 mRNA. Translation: BAB14722.1.
AK223580 mRNA. Translation: BAD97300.1.
AP003108 Genomic DNA. No translation available.
BC001341 mRNA. Translation: AAH01341.1.
RefSeqNP_056348.2. NM_015533.3.
UniGeneHs.6278.

3D structure databases

ProteinModelPortalQ3LXA3.
SMRQ3LXA3. Positions 3-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117481. 18 interactions.
MINTMINT-5001370.
STRING9606.ENSP00000310493.

PTM databases

PhosphoSiteQ3LXA3.

Polymorphism databases

DMDM311033370.

2D gel databases

REPRODUCTION-2DPAGEIPI00551024.

Proteomic databases

PaxDbQ3LXA3.
PRIDEQ3LXA3.

Protocols and materials databases

DNASU26007.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394900; ENSP00000378360; ENSG00000149476.
GeneID26007.
KEGGhsa:26007.
UCSCuc001nre.3. human.

Organism-specific databases

CTD26007.
GeneCardsGC11P061100.
HGNCHGNC:24552. DAK.
HPAHPA039486.
neXtProtNX_Q3LXA3.
PharmGKBPA142672014.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2376.
HOGENOMHOG000234158.
HOVERGENHBG079502.
InParanoidQ3LXA3.
KOK00863.
OMALNMNGFS.
OrthoDBEOG71K630.
PhylomeDBQ3LXA3.
TreeFamTF313821.

Enzyme and pathway databases

BRENDA2.7.1.29. 2681.
ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ3LXA3.
BgeeQ3LXA3.
CleanExHS_DAK.
GenevestigatorQ3LXA3.

Family and domain databases

InterProIPR004006. Dak1.
IPR012734. DhaK_ATP.
IPR004007. DhaL_dom.
[Graphical view]
PfamPF02733. Dak1. 1 hit.
PF02734. Dak2. 1 hit.
[Graphical view]
SUPFAMSSF101473. SSF101473. 1 hit.
TIGRFAMsTIGR02361. dak_ATP. 1 hit.
PROSITEPS51481. DHAK. 1 hit.
PS51480. DHAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAK. human.
GeneWikiDAK_(gene).
GenomeRNAi26007.
NextBio47741.
PMAP-CutDBQ3LXA3.
PROQ3LXA3.

Entry information

Entry nameDHAK_HUMAN
AccessionPrimary (citable) accession number: Q3LXA3
Secondary accession number(s): Q53EQ9, Q9BVA7, Q9H895
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

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