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Protein

PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK

Gene

dhaK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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). 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).2 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.By similarity

Enzyme regulationi

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

Kineticsi

Kcat is 290 min(-1) for dihydroxyacetone. Kcat is 12.5 min(-1) for D,L-glyceraldehyde.1 Publication
  1. KM=6 µM for dihydroxyacetone1 Publication
  2. 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: InterPro
    • phosphoenolpyruvate-glycerone phosphotransferase activity Source: EcoCyc

    GO - Biological processi

    • cellular response to DNA damage stimulus Source: EcoliWiki
    • glycerol catabolic process Source: UniProtKB-UniPathway
    • glycerol to glycerone phosphate metabolic process Source: EcoCyc
    • ketone catabolic process Source: EcoCyc
    • monosaccharide catabolic process Source: EcoCyc

    Keywordsi

    Molecular functionKinase, Transferase
    Biological processGlycerol metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:G6627-MONOMER.
    MetaCyc:G6627-MONOMER.
    BRENDAi2.7.1.29. 2026.
    UniPathwayiUPA00616.

    Protein family/group databases

    MoonProtiP76015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK1 Publication (EC:2.7.1.121By similarity)
    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: UniProtKB

    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

    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

    Protein-protein interaction databases

    BioGridi4260718. 8 interactors.
    DIPiDIP-11563N.
    IntActiP76015. 6 interactors.
    STRINGi316385.ECDH10B_1253.

    Structurei

    Secondary structure

    1356
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi8 – 10Combined sources3
    Helixi11 – 22Combined sources12
    Beta strandi26 – 29Combined sources4
    Turni30 – 33Combined sources4
    Beta strandi34 – 37Combined sources4
    Beta strandi47 – 56Combined sources10
    Turni57 – 60Combined sources4
    Helixi61 – 63Combined sources3
    Beta strandi64 – 66Combined sources3
    Beta strandi68 – 77Combined sources10
    Helixi83 – 93Combined sources11
    Beta strandi99 – 106Combined sources8
    Helixi107 – 122Combined sources16
    Beta strandi127 – 132Combined sources6
    Beta strandi140 – 142Combined sources3
    Beta strandi145 – 147Combined sources3
    Helixi152 – 166Combined sources15
    Helixi170 – 181Combined sources12
    Beta strandi184 – 192Combined sources9
    Turni197 – 199Combined sources3
    Beta strandi201 – 203Combined sources3
    Beta strandi210 – 213Combined sources4
    Beta strandi217 – 219Combined sources3
    Beta strandi223 – 227Combined sources5
    Helixi231 – 244Combined sources14
    Beta strandi248 – 256Combined sources9
    Turni257 – 260Combined sources4
    Beta strandi261 – 269Combined sources9
    Beta strandi277 – 284Combined sources8
    Beta strandi286 – 288Combined sources3
    Helixi290 – 307Combined sources18
    Beta strandi310 – 317Combined sources8
    Beta strandi325 – 335Combined sources11
    Helixi337 – 344Combined sources8
    Beta strandi347 – 351Combined sources5

    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...

    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

    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: August 30, 2017
    This is version 141 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references