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Protein

Dihydroxyacetone kinase

Gene

dhaK

Organism
Citrobacter freundii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of dihydroxyacetone.

Catalytic activityi

ATP + glycerone = ADP + glycerone phosphate.2 Publications

Cofactori

Mg2+1 Publication, Ca2+1 PublicationNote: Divalent metal cations, Mg2+ or Ca2+.1 Publication

Kineticsi

  1. KM=30 µM for dihydroxyacetone1 Publication
  2. KM=70 µM for ATP1 Publication

    Pathwayi: glycerol fermentation

    This protein is involved in step 2 of the subpathway that synthesizes glycerone phosphate from glycerol (oxidative route).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glycerol dehydrogenase (dhaD)
    2. Dihydroxyacetone kinase (dhaK)
    This subpathway is part of the pathway glycerol fermentation, which is itself part of Polyol metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from glycerol (oxidative route), the pathway glycerol fermentation and in Polyol metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei109Substrate1
    Binding sitei114Substrate1
    Active sitei220Tele-hemiaminal-histidine intermediatePROSITE-ProRule annotation1 Publication1
    Binding sitei468ATP; via carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi385 – 388ATP1 Publication4
    Nucleotide bindingi431 – 432ATP1 Publication2
    Nucleotide bindingi476 – 477ATP1 Publication2
    Nucleotide bindingi533 – 535ATP1 Publication3

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycerol metabolism

    Keywords - Ligandi

    ATP-binding, Calcium, Lipid-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-4504.
    BRENDAi2.7.1.29. 1398.
    SABIO-RKP45510.
    UniPathwayiUPA00617; UER00669.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydroxyacetone kinase (EC:2.7.1.29)
    Short name:
    DHA kinase
    Alternative name(s):
    Glycerone kinase
    Gene namesi
    Name:dhaK
    OrganismiCitrobacter freundii
    Taxonomic identifieri546 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi380D → A: Loss of kinase activity. 1 Publication1
    Mutagenesisi385D → A: Loss of kinase activity. 1 Publication1
    Mutagenesisi387D → A: Loss of kinase activity. 1 Publication1
    Mutagenesisi388T → H: Reduced kinase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001215282 – 552Dihydroxyacetone kinaseAdd BLAST551

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1552
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 11Combined sources3
    Helixi12 – 22Combined sources11
    Beta strandi29 – 32Combined sources4
    Beta strandi40 – 44Combined sources5
    Beta strandi52 – 61Combined sources10
    Turni62 – 65Combined sources4
    Helixi66 – 68Combined sources3
    Beta strandi73 – 82Combined sources10
    Helixi88 – 98Combined sources11
    Beta strandi104 – 110Combined sources7
    Helixi112 – 127Combined sources16
    Beta strandi132 – 137Combined sources6
    Beta strandi146 – 148Combined sources3
    Helixi155 – 167Combined sources13
    Helixi172 – 184Combined sources13
    Beta strandi186 – 194Combined sources9
    Beta strandi203 – 205Combined sources3
    Beta strandi213 – 215Combined sources3
    Beta strandi225 – 229Combined sources5
    Helixi233 – 247Combined sources15
    Beta strandi254 – 260Combined sources7
    Helixi266 – 277Combined sources12
    Helixi282 – 284Combined sources3
    Beta strandi285 – 292Combined sources8
    Beta strandi300 – 309Combined sources10
    Helixi314 – 319Combined sources6
    Helixi356 – 371Combined sources16
    Helixi373 – 381Combined sources9
    Beta strandi384 – 386Combined sources3
    Helixi388 – 404Combined sources17
    Helixi413 – 427Combined sources15
    Helixi430 – 448Combined sources19
    Helixi453 – 468Combined sources16
    Beta strandi474 – 476Combined sources3
    Helixi478 – 490Combined sources13
    Helixi495 – 511Combined sources17
    Helixi529 – 531Combined sources3
    Helixi534 – 547Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1UN8X-ray2.50A/B1-552[»]
    1UN9X-ray3.10A/B2-552[»]
    ProteinModelPortaliP45510.
    SMRiP45510.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45510.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini8 – 327DhaKPROSITE-ProRule annotationAdd BLAST320
    Domaini356 – 548DhaLPROSITE-ProRule annotationAdd BLAST193

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni58 – 61Substrate binding4

    Domaini

    The C-terminal domain consists of a eight-helix alpha barrel. The eight helices form a pocket that includes a tightly bound phospholipid. The cellular function of this lipid is unknown; it has no significant effect on enzyme activity.

    Sequence similaritiesi

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

    Family and domain databases

    InterProiIPR012734. DhaK_ATP.
    IPR004006. DhaK_dom.
    IPR004007. DhaL_dom.
    [Graphical view]
    PfamiPF02733. Dak1. 1 hit.
    PF02734. Dak2. 1 hit.
    [Graphical view]
    SMARTiSM01120. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P45510-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSQFFFNQRT HLVSDVIDGA IIASPWNNLA RLESDPAIRI VVRRDLNKNN
    60 70 80 90 100
    VAVISGGGSG HEPAHVGFIG KGMLTAAVCG DVFASPSVDA VLTAIQAVTG
    110 120 130 140 150
    EAGCLLIVKN YTGDRLNFGL AAEKARRLGY NVEMLIVGDD ISLPDNKHPR
    160 170 180 190 200
    GIAGTILVHK IAGYFAERGY NLATVLREAQ YAASNTFSLG VALSSCHLPQ
    210 220 230 240 250
    ETDAAPRHHP GHAELGMGIH GEPGASVIDT QNSAQVVNLM VDKLLAALPE
    260 270 280 290 300
    TGRLAVMINN LGGVSVAEMA IITRELASSP LHSRIDWLIG PASLVTALDM
    310 320 330 340 350
    KGFSLTAIVL EESIEKALLT EVETSNWPTP VPPREITCVV SSHASARVEF
    360 370 380 390 400
    QPSANALVAG IVELVTATLS DLETHLNALD AKVGDGDTGS TFAAAAREIA
    410 420 430 440 450
    SLLHRQQLPL NNLATLFALI GERLTVVMGG SSGVLMSIFF TAAGQKLEQG
    460 470 480 490 500
    ANVVEALNTG LAQMKFYGGA DEGDRTMIDA LQPALTSLLA QPKNLQAAFD
    510 520 530 540 550
    AAQAGAERTC LSSKANAGRA SYLSSESLLG NMDPGAQRLA MVFKALAESE

    LG
    Length:552
    Mass (Da):57,940
    Last modified:January 23, 2007 - v3
    Checksum:i8208307ECF3F79EA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U09771 Genomic DNA. Translation: AAB48843.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U09771 Genomic DNA. Translation: AAB48843.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1UN8X-ray2.50A/B1-552[»]
    1UN9X-ray3.10A/B2-552[»]
    ProteinModelPortaliP45510.
    SMRiP45510.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00617; UER00669.
    BioCyciMetaCyc:MONOMER-4504.
    BRENDAi2.7.1.29. 1398.
    SABIO-RKP45510.

    Miscellaneous databases

    EvolutionaryTraceiP45510.

    Family and domain databases

    InterProiIPR012734. DhaK_ATP.
    IPR004006. DhaK_dom.
    IPR004007. DhaL_dom.
    [Graphical view]
    PfamiPF02733. Dak1. 1 hit.
    PF02734. Dak2. 1 hit.
    [Graphical view]
    SMARTiSM01120. Dak2. 1 hit.
    [Graphical view]
    SUPFAMiSSF101473. SSF101473. 1 hit.
    TIGRFAMsiTIGR02361. dak_ATP. 1 hit.
    PROSITEiPS51481. DHAK. 1 hit.
    PS51480. DHAL. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHAK_CITFR
    AccessioniPrimary (citable) accession number: P45510
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 79 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.