Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P37530

- DGK_BACSU

UniProt

P37530 - DGK_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Deoxyguanosine kinase

Gene

dgk

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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.
InParanoidiP37530.
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

        10         20         30         40         50
MNTAPFIAIE GPIGAGKTTL ATMLSQKFGF PMINEIVEDN PYLDKFYDNI
60 70 80 90 100
KEWSFQLEMF FLCHRYKQLE DTSDHFLKKG QPVIADYHIY KNVIFAERTL
110 120 130 140 150
SPHQLEKYKK IYHLLTDDLP KPNFIIYIKA SLPTLLHRIE KRGRPFEKKI
160 170 180 190 200
ETSYLEQLIS DYEVAIKQLQ EADPELTVLT VDGDSKDFVL NKSDFERIAA

HVKELIV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P37530.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 96 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