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Q3LXA3

- DHAK_HUMAN

UniProt

Q3LXA3 - DHAK_HUMAN

Protein

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

Gene

DAK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate.2 Publications

    Catalytic activityi

    ATP + glycerone = ADP + glycerone phosphate.1 Publication
    ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate.1 Publication
    FAD = AMP + riboflavin cyclic-4',5'-phosphate.1 Publication

    Cofactori

    Magnesium.By similarity
    Manganese or cobalt; for FAD-AMP lyase activity.By similarity

    Enzyme regulationi

    Each activity is inhibited by the substrate(s) of the other.

    Kineticsi

    1. KM=0.5 µM for dihydroxyacetone1 Publication
    2. KM=11 µM for glyceraldehyde1 Publication

    pH dependencei

    Optimum pH is 6.6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091DihydroxyacetonePROSITE-ProRule annotation
    Binding sitei114 – 1141DihydroxyacetonePROSITE-ProRule annotation
    Active sitei221 – 2211Tele-hemiaminal-histidine intermediatePROSITE-ProRule annotation
    Binding sitei486 – 4861ATP; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi401 – 4044ATPBy similarity
    Nucleotide bindingi446 – 4472ATPBy similarity
    Nucleotide bindingi494 – 4952ATPBy similarity
    Nucleotide bindingi556 – 5583ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. FAD-AMP lyase (cyclizing) activity Source: UniProt
    3. glycerone kinase activity Source: UniProt
    4. metal ion binding Source: UniProtKB-KW
    5. triokinase activity Source: UniProt

    GO - Biological processi

    1. carbohydrate phosphorylation Source: UniProt
    2. cellular carbohydrate metabolic process Source: UniProt
    3. glycerol metabolic process Source: InterPro
    4. innate immune response Source: Reactome
    5. regulation of innate immune response Source: UniProt

    Keywords - Molecular functioni

    Kinase, Lyase, Transferase

    Keywords - Ligandi

    ATP-binding, Cobalt, FAD, Flavoprotein, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.29. 2681.
    ReactomeiREACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)
    Including the following 2 domains:
    ATP-dependent dihydroxyacetone kinase (EC:2.7.1.28, EC:2.7.1.29)
    Short name:
    DHA kinase
    Alternative name(s):
    Glycerone kinase
    Triokinase
    Triose kinase
    FAD-AMP lyase (cyclizing) (EC:4.6.1.15)
    Alternative name(s):
    FAD-AMP lyase (cyclic FMN forming)
    FMN cyclase
    Gene namesi
    Name:DAK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:24552. DAK.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142672014.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 575575Bifunctional ATP-dependent dihydroxyacetone kinase/FAD-AMP lyase (cyclizing)PRO_0000121525Add
    BLAST

    Proteomic databases

    MaxQBiQ3LXA3.
    PaxDbiQ3LXA3.
    PRIDEiQ3LXA3.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00551024.

    PTM databases

    PhosphoSiteiQ3LXA3.

    Miscellaneous databases

    PMAP-CutDBQ3LXA3.

    Expressioni

    Tissue specificityi

    Detected in erythrocytes (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ3LXA3.
    BgeeiQ3LXA3.
    CleanExiHS_DAK.
    GenevestigatoriQ3LXA3.

    Organism-specific databases

    HPAiHPA039486.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi117481. 18 interactions.
    DIPiDIP-60967N.
    MINTiMINT-5001370.
    STRINGi9606.ENSP00000310493.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3LXA3.
    SMRiQ3LXA3. Positions 3-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 336328DhaKPROSITE-ProRule annotationAdd
    BLAST
    Domaini372 – 571200DhaLPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni56 – 594Dihydroxyacetone bindingBy similarity

    Sequence similaritiesi

    Contains 1 DhaK domain.PROSITE-ProRule annotation
    Contains 1 DhaL domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2376.
    HOGENOMiHOG000234158.
    HOVERGENiHBG079502.
    InParanoidiQ3LXA3.
    KOiK00863.
    OMAiDHMTDPS.
    OrthoDBiEOG71K630.
    PhylomeDBiQ3LXA3.
    TreeFamiTF313821.

    Family and domain databases

    InterProiIPR004006. Dak1.
    IPR012734. DhaK_ATP.
    IPR004007. DhaL_dom.
    [Graphical view]
    PfamiPF02733. Dak1. 1 hit.
    PF02734. Dak2. 1 hit.
    [Graphical view]
    SUPFAMiSSF101473. SSF101473. 1 hit.
    TIGRFAMsiTIGR02361. dak_ATP. 1 hit.
    PROSITEiPS51481. DHAK. 1 hit.
    PS51480. DHAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q3LXA3-1 [UniParc]FASTAAdd to Basket

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    MTSKKLVNSV AGCADDALAG LVACNPNLQL LQGHRVALRS DLDSLKGRVA    50
    LLSGGGSGHE PAHAGFIGKG MLTGVIAGAV FTSPAVGSIL AAIRAVAQAG 100
    TVGTLLIVKN YTGDRLNFGL AREQARAEGI PVEMVVIGDD SAFTVLKKAG 150
    RRGLCGTVLI HKVAGALAEA GVGLEEIAKQ VNVVAKAMGT LGVSLSSCSV 200
    PGSKPTFELS ADEVELGLGI HGEAGVRRIK MATADEIVKL MLDHMTNTTN 250
    ASHVPVQPGS SVVMMVNNLG GLSFLELGII ADATVRSLEG RGVKIARALV 300
    GTFMSALEMP GISLTLLLVD EPLLKLIDAE TTAAAWPNVA AVSITGRKRS 350
    RVAPAEPQEA PDSTAAGGSA SKRMALVLER VCSTLLGLEE HLNALDRAAG 400
    DGDCGTTHSR AARAIQEWLK EGPPPASPAQ LLSKLSVLLL EKMGGSSGAL 450
    YGLFLTAAAQ PLKAKTSLPA WSAAMDAGLE AMQKYGKAAP GDRTMLDSLW 500
    AAGQELQAWK SPGADLLQVL TKAVKSAEAA AEATKNMEAG AGRASYISSA 550
    RLEQPDPGAV AAAAILRAIL EVLQS 575
    Length:575
    Mass (Da):58,947
    Last modified:November 2, 2010 - v2
    Checksum:i4DB8C5326F65122C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71V → A in BAB14722. (PubMed:14702039)Curated
    Sequence conflicti19 – 191A → S in BAD97300. 1 PublicationCurated
    Sequence conflicti75 – 751V → A in BAB14722. (PubMed:14702039)Curated
    Sequence conflicti376 – 3761L → P in BAB14722. (PubMed:14702039)Curated
    Sequence conflicti497 – 4971D → G in BAB14722. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti185 – 1851A → T.3 Publications
    Corresponds to variant rs2260655 [ dbSNP | Ensembl ].
    VAR_028108
    Natural varianti334 – 3341A → G.
    Corresponds to variant rs35723406 [ dbSNP | Ensembl ].
    VAR_054780

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS8003.1.
    RefSeqiNP_056348.2. NM_015533.3.
    XP_006718559.1. XM_006718496.1.
    UniGeneiHs.6278.

    Genome annotation databases

    EnsembliENST00000394900; ENSP00000378360; ENSG00000149476.
    GeneIDi26007.
    KEGGihsa:26007.
    UCSCiuc001nre.3. human.

    Polymorphism databases

    DMDMi311033370.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS8003.1.
    RefSeqi NP_056348.2. NM_015533.3.
    XP_006718559.1. XM_006718496.1.
    UniGenei Hs.6278.

    3D structure databases

    ProteinModelPortali Q3LXA3.
    SMRi Q3LXA3. Positions 3-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117481. 18 interactions.
    DIPi DIP-60967N.
    MINTi MINT-5001370.
    STRINGi 9606.ENSP00000310493.

    PTM databases

    PhosphoSitei Q3LXA3.

    Polymorphism databases

    DMDMi 311033370.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00551024.

    Proteomic databases

    MaxQBi Q3LXA3.
    PaxDbi Q3LXA3.
    PRIDEi Q3LXA3.

    Protocols and materials databases

    DNASUi 26007.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394900 ; ENSP00000378360 ; ENSG00000149476 .
    GeneIDi 26007.
    KEGGi hsa:26007.
    UCSCi uc001nre.3. human.

    Organism-specific databases

    CTDi 26007.
    GeneCardsi GC11P061100.
    HGNCi HGNC:24552. DAK.
    HPAi HPA039486.
    MIMi 615844. gene.
    neXtProti NX_Q3LXA3.
    PharmGKBi PA142672014.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2376.
    HOGENOMi HOG000234158.
    HOVERGENi HBG079502.
    InParanoidi Q3LXA3.
    KOi K00863.
    OMAi DHMTDPS.
    OrthoDBi EOG71K630.
    PhylomeDBi Q3LXA3.
    TreeFami TF313821.

    Enzyme and pathway databases

    BRENDAi 2.7.1.29. 2681.
    Reactomei REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

    Miscellaneous databases

    ChiTaRSi DAK. human.
    GeneWikii DAK_(gene).
    GenomeRNAii 26007.
    NextBioi 47741.
    PMAP-CutDB Q3LXA3.
    PROi Q3LXA3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q3LXA3.
    Bgeei Q3LXA3.
    CleanExi HS_DAK.
    Genevestigatori Q3LXA3.

    Family and domain databases

    InterProi IPR004006. Dak1.
    IPR012734. DhaK_ATP.
    IPR004007. DhaL_dom.
    [Graphical view ]
    Pfami PF02733. Dak1. 1 hit.
    PF02734. Dak2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101473. SSF101473. 1 hit.
    TIGRFAMsi TIGR02361. dak_ATP. 1 hit.
    PROSITEi PS51481. DHAK. 1 hit.
    PS51480. DHAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDHAK_HUMAN
    AccessioniPrimary (citable) accession number: Q3LXA3
    Secondary accession number(s): Q53EQ9, Q9BVA7, Q9H895
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3