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Protein

PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK

Gene

dhaK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP (PubMed:15476397, PubMed:11350937). Binds covalently dihydroxyacetone in hemiaminal linkage (PubMed:15476397). DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:24440518). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:24440518). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:24440518).3 Publications

Miscellaneous

Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity.1 Publication

Catalytic activityi

Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate.1 Publication

Activity regulationi

Inhibited by chloro-3-hydroxyacetone and D,L-glyceraldehyde.1 Publication

Kineticsi

kcat is 2.8 sec(-1) with dihydroxyacetone as substrate. Values measured with the DhaKLM complex (PubMed:11350937). kcat is 290 min(-1) with dihydroxyacetone as substrate. kcat is 12.5 min(-1) with D,L-glyceraldehyde as substrate (PubMed:15476397).2 Publications
  1. KM=45 µM for dihydroxyacetone1 Publication
  2. KM=6 µM for dihydroxyacetone1 Publication
  3. KM=110 µM for D,L-glyceraldehyde1 Publication

    Pathwayi: glycerol degradation

    This protein is involved in the pathway glycerol degradation, which is part of Polyol metabolism.Curated
    View all proteins of this organism that are known to be involved in the pathway glycerol degradation and in Polyol metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei56Proton acceptor1 Publication1
    Binding sitei104DihydroxyacetoneCombined sources2 Publications1
    Binding sitei109DihydroxyacetoneCombined sources3 Publications1
    Active sitei218Tele-hemiaminal-histidine intermediatePROSITE-ProRule annotationCombined sources3 Publications1

    GO - Molecular functioni

    • glycerone kinase activity Source: GO_Central
    • identical protein binding Source: IntAct
    • phosphoenolpyruvate-glycerone phosphotransferase activity Source: EcoCyc

    GO - Biological processi

    Keywordsi

    Molecular functionKinase, Transferase
    Biological processGlycerol metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:G6627-MONOMER
    MetaCyc:G6627-MONOMER
    BRENDAi2.7.1.29 2026
    UniPathwayi
    UPA00616

    Protein family/group databases

    MoonProtiP76015

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK1 Publication (EC:2.7.1.1211 Publication)
    Gene namesi
    Name:dhaK1 Publication
    Synonyms:ycgT
    Ordered Locus Names:b1200, JW5187
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13901 dhaK

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi56H → A or N: Shows a moderate decrease in the catalytic efficiency but at least a 40-to 300-fold increase in affinity for dihydroxyacetone. 1 Publication1
    Mutagenesisi109D → A or N: Loss of kinase activity. 1 Publication1
    Mutagenesisi218H → A or K: Loss of kinase activity. 2 Publications1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001215291 – 356PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaKAdd BLAST356

    Proteomic databases

    EPDiP76015
    PaxDbiP76015
    PRIDEiP76015

    Expressioni

    Inductioni

    Activated by DhaR.2 Publications

    Interactioni

    Subunit structurei

    Homodimer (PubMed:12813127, PubMed:15476397, PubMed:24440518). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL (PubMed:12813127, PubMed:15476397). DhaL also forms a complex with DhaR (PubMed:24440518).3 Publications

    Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi4260718, 14 interactors
    ComplexPortaliCPX-2634 Dha Kinase
    DIPiDIP-11563N
    IntActiP76015, 7 interactors
    STRINGi316385.ECDH10B_1253

    Structurei

    Secondary structure

    1356
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP76015
    SMRiP76015
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP76015

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini7 – 352DhaKPROSITE-ProRule annotationAdd BLAST346

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni53 – 56Dihydroxyacetone bindingCombined sources3 Publications4

    Phylogenomic databases

    eggNOGiENOG4105CMT Bacteria
    COG2376 LUCA
    HOGENOMiHOG000226638
    InParanoidiP76015
    KOiK05878
    PhylomeDBiP76015

    Family and domain databases

    InterProiView protein in InterPro
    IPR012736 DhaK_1
    IPR004006 DhaK_dom
    PfamiView protein in Pfam
    PF02733 Dak1, 1 hit
    TIGRFAMsiTIGR02363 dhaK1, 1 hit
    PROSITEiView protein in PROSITE
    PS51481 DHAK, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P76015-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKKLINDVQD VLDEQLAGLA KAHPSLTLHQ DPVYVTRADA PVAGKVALLS
    60 70 80 90 100
    GGGSGHEPMH CGYIGQGMLS GACPGEIFTS PTPDKIFECA MQVDGGEGVL
    110 120 130 140 150
    LIIKNYTGDI LNFETATELL HDSGVKVTTV VIDDDVAVKD SLYTAGRRGV
    160 170 180 190 200
    ANTVLIEKLV GAAAERGDSL DACAELGRKL NNQGHSIGIA LGACTVPAAG
    210 220 230 240 250
    KPSFTLADNE MEFGVGIHGE PGIDRRPFSS LDQTVDEMFD TLLVNGSYHR
    260 270 280 290 300
    TLRFWDYQQG SWQEEQQTKQ PLQSGDRVIA LVNNLGATPL SELYGVYNRL
    310 320 330 340 350
    TTRCQQAGLT IERNLIGAYC TSLDMTGFSI TLLKVDDETL ALWDAPVHTP

    ALNWGK
    Length:356
    Mass (Da):38,215
    Last modified:November 13, 2007 - v2
    Checksum:i510D73BE9685395F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC74284.2
    AP009048 Genomic DNA Translation: BAA36057.2
    PIRiE64866
    RefSeqiNP_415718.6, NC_000913.3
    WP_000733715.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC74284; AAC74284; b1200
    BAA36057; BAA36057; BAA36057
    GeneIDi945747
    KEGGiecj:JW5187
    eco:b1200
    PATRICifig|1411691.4.peg.1085

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC74284.2
    AP009048 Genomic DNA Translation: BAA36057.2
    PIRiE64866
    RefSeqiNP_415718.6, NC_000913.3
    WP_000733715.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1OI2X-ray1.75A/B1-356[»]
    1OI3X-ray2.00A/B1-356[»]
    1UODX-ray1.90A/B1-356[»]
    1UOEX-ray2.00A/B1-356[»]
    3PNKX-ray2.21A/B2-356[»]
    3PNLX-ray2.20A2-356[»]
    3PNMX-ray2.55A/B/C/D2-356[»]
    3PNOX-ray1.97A/B/C/D2-356[»]
    3PNQX-ray2.20A/B/C/D2-356[»]
    4LRXX-ray3.25A/B1-356[»]
    4LRYX-ray2.83A/B1-356[»]
    ProteinModelPortaliP76015
    SMRiP76015
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260718, 14 interactors
    ComplexPortaliCPX-2634 Dha Kinase
    DIPiDIP-11563N
    IntActiP76015, 7 interactors
    STRINGi316385.ECDH10B_1253

    Protein family/group databases

    MoonProtiP76015

    Proteomic databases

    EPDiP76015
    PaxDbiP76015
    PRIDEiP76015

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74284; AAC74284; b1200
    BAA36057; BAA36057; BAA36057
    GeneIDi945747
    KEGGiecj:JW5187
    eco:b1200
    PATRICifig|1411691.4.peg.1085

    Organism-specific databases

    EchoBASEiEB3660
    EcoGeneiEG13901 dhaK

    Phylogenomic databases

    eggNOGiENOG4105CMT Bacteria
    COG2376 LUCA
    HOGENOMiHOG000226638
    InParanoidiP76015
    KOiK05878
    PhylomeDBiP76015

    Enzyme and pathway databases

    UniPathwayi
    UPA00616

    BioCyciEcoCyc:G6627-MONOMER
    MetaCyc:G6627-MONOMER
    BRENDAi2.7.1.29 2026

    Miscellaneous databases

    EvolutionaryTraceiP76015
    PROiPR:P76015

    Family and domain databases

    InterProiView protein in InterPro
    IPR012736 DhaK_1
    IPR004006 DhaK_dom
    PfamiView protein in Pfam
    PF02733 Dak1, 1 hit
    TIGRFAMsiTIGR02363 dhaK1, 1 hit
    PROSITEiView protein in PROSITE
    PS51481 DHAK, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHAK_ECOLI
    AccessioniPrimary (citable) accession number: P76015
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 13, 2007
    Last modified: November 7, 2018
    This is version 149 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
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