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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091Substrate
    Binding sitei114 – 1141Substrate
    Active sitei220 – 2201Tele-hemiaminal-histidine intermediatePROSITE-ProRule annotation1 Publication
    Binding sitei468 – 4681ATP; via carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi385 – 3884ATP1 Publication
    Nucleotide bindingi431 – 4322ATP1 Publication
    Nucleotide bindingi476 – 4772ATP1 Publication
    Nucleotide bindingi533 – 5353ATP1 Publication

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi380 – 3801D → A: Loss of kinase activity. 1 Publication
    Mutagenesisi385 – 3851D → A: Loss of kinase activity. 1 Publication
    Mutagenesisi387 – 3871D → A: Loss of kinase activity. 1 Publication
    Mutagenesisi388 – 3881T → H: Reduced kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 552551Dihydroxyacetone kinasePRO_0000121528Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    552
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 113Combined sources
    Helixi12 – 2211Combined sources
    Beta strandi29 – 324Combined sources
    Beta strandi40 – 445Combined sources
    Beta strandi52 – 6110Combined sources
    Turni62 – 654Combined sources
    Helixi66 – 683Combined sources
    Beta strandi73 – 8210Combined sources
    Helixi88 – 9811Combined sources
    Beta strandi104 – 1107Combined sources
    Helixi112 – 12716Combined sources
    Beta strandi132 – 1376Combined sources
    Beta strandi146 – 1483Combined sources
    Helixi155 – 16713Combined sources
    Helixi172 – 18413Combined sources
    Beta strandi186 – 1949Combined sources
    Beta strandi203 – 2053Combined sources
    Beta strandi213 – 2153Combined sources
    Beta strandi225 – 2295Combined sources
    Helixi233 – 24715Combined sources
    Beta strandi254 – 2607Combined sources
    Helixi266 – 27712Combined sources
    Helixi282 – 2843Combined sources
    Beta strandi285 – 2928Combined sources
    Beta strandi300 – 30910Combined sources
    Helixi314 – 3196Combined sources
    Helixi356 – 37116Combined sources
    Helixi373 – 3819Combined sources
    Beta strandi384 – 3863Combined sources
    Helixi388 – 40417Combined sources
    Helixi413 – 42715Combined sources
    Helixi430 – 44819Combined sources
    Helixi453 – 46816Combined sources
    Beta strandi474 – 4763Combined sources
    Helixi478 – 49013Combined sources
    Helixi495 – 51117Combined sources
    Helixi529 – 5313Combined sources
    Helixi534 – 54714Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UN8X-ray2.50A/B1-552[»]
    1UN9X-ray3.10A/B2-552[»]
    ProteinModelPortaliP45510.
    SMRiP45510. Positions 1-550.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45510.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 327320DhaKPROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 548193DhaLPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 614Substrate binding

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UN8X-ray2.50A/B1-552[»]
    1UN9X-ray3.10A/B2-552[»]
    ProteinModelPortaliP45510.
    SMRiP45510. Positions 1-550.
    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: May 11, 2016
    This is version 77 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.