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P37529

- DCK_BACSU

UniProt

P37529 - DCK_BACSU

Protein

Deoxyadenosine/deoxycytidine kinase

Gene

dck

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Plays an essential role in generating the deoxyribonucleotide precursors dATP AND dCTP for DNA metabolism. The phosphate acceptor specificity is strict toward deoxyadenosine (dAdo) and deoxycytidine (dCyd). The specificity toward the sugar moiety of the nucleoside is less strict. Both 2-deoxyribose, ribose, and arabinose nucleosides are phosphorylated, although the 2-deoxyribonucleosides are preferred. The phosphate donor specificity is dependent on the deoxyribonucleoside substrate, but GTP is efficient with both deoxycytidine and deoxyadenosine. Only nucleoside triphosphates can act as phosphate donors.1 Publication

    Catalytic activityi

    ATP + deoxyadenosine = ADP + dAMP.
    NTP + deoxycytidine = NDP + dCMP.

    Enzyme regulationi

    Deoxyadenosine inhibits deoxycytidine phosphorylation and deoxycytidine inhibits deoxyadenosine phosphorylation. Deoxyadenosine/deoxycytidine kinase is inhibited by both dATP and dCTP.1 Publication

    Kineticsi

    1. KM=5 µM for deoxyadenosine (with GTP at pH 8.5 and at 37 degrees Celsius)1 Publication
    2. KM=5 µM for deoxycytidine (with GTP at pH 8.5 and at 37 degrees Celsius)1 Publication
    3. KM=65 µM for GTP (with deoxyadenosine or deoxycytidine at pH 7.8 and at 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is around pH 8.6. At pH 8.0-9.6 more than 90% of maximal activity is still observed.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401SubstrateBy similarity
    Binding sitei52 – 521SubstrateBy similarity
    Binding sitei63 – 631SubstrateBy similarity
    Active sitei87 – 871Proton acceptorSequence Analysis
    Binding sitei88 – 881SubstrateBy similarity
    Binding sitei93 – 931SubstrateBy similarity
    Binding sitei156 – 1561SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 249ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. deoxyadenosine kinase activity Source: UniProtKB-EC
    3. deoxycytidine kinase activity Source: UniProtKB-EC
    4. phosphotransferase activity, alcohol group as acceptor Source: InterPro

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU00140-MONOMER.
    MetaCyc:BSU00140-MONOMER.
    SABIO-RKP37529.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyadenosine/deoxycytidine kinase (EC:2.7.1.74, EC:2.7.1.76)
    Short name:
    dAK/dCK
    Gene namesi
    Name:dck
    Synonyms:dak, yaaF
    Ordered Locus Names:BSU00140
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU00140. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217Deoxyadenosine/deoxycytidine kinasePRO_0000049430Add
    BLAST

    Proteomic databases

    PaxDbiP37529.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU00140.

    Structurei

    3D structure databases

    ProteinModelPortaliP37529.
    SMRiP37529. Positions 6-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DCK/DGK family.Curated

    Phylogenomic databases

    eggNOGiCOG1428.
    HOGENOMiHOG000030092.
    KOiK15519.
    OMAiIYGDVIF.
    OrthoDBiEOG628F9B.
    PhylomeDBiP37529.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR002624. DNK.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10513. PTHR10513. 1 hit.
    PfamiPF01712. dNK. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000705. DNK. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37529-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKEHHIPKNS IITVAGTVGV GKSTLTKTLA KRLGFKTSLE EVDHNPYLEK    50
    FYHDFERWSF HLQIYFLAER FKEQKTIFEA GGGFVQDRSI YEDTGIFAKM 100
    HADKGTMSKV DYKTYTSLFE AMVMTPYFPH PDVLIYLEGD LENILNRIEQ 150
    RGREMELQTS RSYWEEMHTR YENWISGFNA CPVLKLRIED YDLLNDENSI 200
    ENIVDQIASV IHDNQKK 217
    Length:217
    Mass (Da):25,444
    Last modified:October 1, 1994 - v1
    Checksum:iB02CDBAA1C518305
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26185 Genomic DNA. Translation: BAA05250.1.
    AL009126 Genomic DNA. Translation: CAB11790.1.
    PIRiS66044.
    RefSeqiNP_387895.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB11790; CAB11790; BSU00140.
    GeneIDi936793.
    KEGGibsu:BSU00140.
    PATRICi18971489. VBIBacSub10457_0015.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26185 Genomic DNA. Translation: BAA05250.1 .
    AL009126 Genomic DNA. Translation: CAB11790.1 .
    PIRi S66044.
    RefSeqi NP_387895.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P37529.
    SMRi P37529. Positions 6-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU00140.

    Proteomic databases

    PaxDbi P37529.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11790 ; CAB11790 ; BSU00140 .
    GeneIDi 936793.
    KEGGi bsu:BSU00140.
    PATRICi 18971489. VBIBacSub10457_0015.

    Organism-specific databases

    GenoListi BSU00140. [Micado ]

    Phylogenomic databases

    eggNOGi COG1428.
    HOGENOMi HOG000030092.
    KOi K15519.
    OMAi IYGDVIF.
    OrthoDBi EOG628F9B.
    PhylomeDBi P37529.

    Enzyme and pathway databases

    BioCyci BSUB:BSU00140-MONOMER.
    MetaCyc:BSU00140-MONOMER.
    SABIO-RK P37529.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR002624. DNK.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10513. PTHR10513. 1 hit.
    Pfami PF01712. dNK. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000705. DNK. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
      Ogasawara N., Nakai S., Yoshikawa H.
      DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "Deoxyadenosine/deoxycytidine kinase from Bacillus subtilis. Purification, characterization, and physiological function."
      Moellgaard H.
      J. Biol. Chem. 255:8216-8220(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
    4. "Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus subtilis. Substrate specificity and kinetic analysis of deoxyguanosine kinase with UTP as the preferred phosphate donor."
      Andersen R.B., Neuhard J.
      J. Biol. Chem. 276:5518-5524(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE, SUBUNIT.

    Entry informationi

    Entry nameiDCK_BACSU
    AccessioniPrimary (citable) accession number: P37529
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3