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P37530

- DGK_BACSU

UniProt

P37530 - DGK_BACSU

Protein

Deoxyguanosine kinase

Gene

dgk

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 95 (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 dGTP for DNA metabolism. Highly specific toward deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity is observed with guanosine. UTP is slightly more efficient as phosphate donor than CTP, ATP and GTP.1 Publication

    Catalytic activityi

    ATP + deoxyguanosine = ADP + dGMP.

    Enzyme regulationi

    Inhibited by deoxyguanosine at concentrations above 30 µM only with UTP as phosphate donor. dGTP is a potent competitive inhibitor.1 Publication

    Kineticsi

    1. KM=0.6 µM for deoxyguanosine (with UTP at pH 7.8 and at 37 degrees Celsius)1 Publication
    2. KM=1.7 µM for deoxyguanosine (with CTP at pH 7.8 and at 37 degrees Celsius)1 Publication
    3. KM=6.5 µM for deoxyguanosine (with ATP at pH 7.8 and at 37 degrees Celsius)1 Publication
    4. KM=10.4 µM for deoxyguanosine (with GTP at pH 7.8 and at 37 degrees Celsius)1 Publication
    5. KM=6 µM for UTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius)1 Publication
    6. KM=35 µM for CTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius)1 Publication
    7. KM=36 µM for ATP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius)1 Publication
    8. KM=46 µM for GTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius)1 Publication

    Vmax=8.1 µmol/min/mg enzyme toward deoxyguanosine (with 0.5 mM UTP at pH 7.8 and at 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is around pH 9 (with saturating concentrations of dGuo and UTP). At pH 7.5 and 11.5 more than 80% of maximal activity is still observed. At pH 6.0, 60% activity remains, whereas the enzyme is completely inactive below pH 5.6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei35 – 351SubstrateBy similarity
    Binding sitei47 – 471SubstrateBy similarity
    Active sitei86 – 861Proton acceptorSequence Analysis
    Binding sitei147 – 1471SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 199ATPBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU00150-MONOMER.
    SABIO-RKP37530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyguanosine kinase (EC:2.7.1.113)
    Short name:
    DGUO kinase
    Short name:
    dGK
    Gene namesi
    Name:dgk
    Synonyms:yaaG
    Ordered Locus Names:BSU00150
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU00150. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 207207Deoxyguanosine kinasePRO_0000049431Add
    BLAST

    Proteomic databases

    PaxDbiP37530.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU00150.

    Structurei

    3D structure databases

    ProteinModelPortaliP37530.
    SMRiP37530. Positions 5-203.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DCK/DGK family.Curated

    Phylogenomic databases

    eggNOGiCOG1428.
    HOGENOMiHOG000030092.
    KOiK15518.
    OMAiVESAMTH.
    OrthoDBiEOG628F9B.
    PhylomeDBiP37530.

    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.

    P37530-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTAPFIAIE GPIGAGKTTL ATMLSQKFGF PMINEIVEDN PYLDKFYDNI    50
    KEWSFQLEMF FLCHRYKQLE DTSDHFLKKG QPVIADYHIY KNVIFAERTL 100
    SPHQLEKYKK IYHLLTDDLP KPNFIIYIKA SLPTLLHRIE KRGRPFEKKI 150
    ETSYLEQLIS DYEVAIKQLQ EADPELTVLT VDGDSKDFVL NKSDFERIAA 200
    HVKELIV 207
    Length:207
    Mass (Da):24,145
    Last modified:October 1, 1994 - v1
    Checksum:i0F77C6B31E9AA331
    GO

    Mass spectrometryi

    Molecular mass is 24147 Da from positions 1 - 207. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26185 Genomic DNA. Translation: BAA05251.1.
    AL009126 Genomic DNA. Translation: CAB11791.1.
    PIRiS66045.
    RefSeqiNP_387896.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB11791; CAB11791; BSU00150.
    GeneIDi937037.
    KEGGibsu:BSU00150.
    PATRICi18971491. VBIBacSub10457_0016.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26185 Genomic DNA. Translation: BAA05251.1 .
    AL009126 Genomic DNA. Translation: CAB11791.1 .
    PIRi S66045.
    RefSeqi NP_387896.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P37530.
    SMRi P37530. Positions 5-203.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU00150.

    Proteomic databases

    PaxDbi P37530.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11791 ; CAB11791 ; BSU00150 .
    GeneIDi 937037.
    KEGGi bsu:BSU00150.
    PATRICi 18971491. VBIBacSub10457_0016.

    Organism-specific databases

    GenoListi BSU00150. [Micado ]

    Phylogenomic databases

    eggNOGi COG1428.
    HOGENOMi HOG000030092.
    KOi K15518.
    OMAi VESAMTH.
    OrthoDBi EOG628F9B.
    PhylomeDBi P37530.

    Enzyme and pathway databases

    BioCyci BSUB:BSU00150-MONOMER.
    SABIO-RK P37530.

    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. "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: FUNCTION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION, NOMENCLATURE, SUBUNIT.

    Entry informationi

    Entry nameiDGK_BACSU
    AccessioniPrimary (citable) accession number: P37530
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.

    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