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P37529 (DCK_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Deoxyadenosine/deoxycytidine kinase
Short name=dAK/dCK
EC=2.7.1.74
EC=2.7.1.76
Gene names
Name:dck
Synonyms:dak, yaaF
Ordered Locus Names:BSU00140
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

ATP + deoxyadenosine = ADP + dAMP.

NTP + deoxycytidine = NDP + dCMP.

Enzyme regulation

Deoxyadenosine inhibits deoxycytidine phosphorylation and deoxycytidine inhibits deoxyadenosine phosphorylation. Deoxyadenosine/deoxycytidine kinase is inhibited by both dATP and dCTP. Ref.3

Subunit structure

Homodimer. Ref.4

Sequence similarities

Belongs to the DCK/DGK family.

Biophysicochemical properties

Kinetic parameters:

KM=5 µM for deoxyadenosine (with GTP at pH 8.5 and at 37 degrees Celsius) Ref.3

KM=5 µM for deoxycytidine (with GTP at pH 8.5 and at 37 degrees Celsius)

KM=65 µM for GTP (with deoxyadenosine or deoxycytidine at pH 7.8 and at 37 degrees Celsius)

pH dependence:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Deoxyadenosine/deoxycytidine kinase
PRO_0000049430

Regions

Nucleotide binding16 – 249ATP By similarity

Sites

Active site871Proton acceptor Potential
Binding site401Substrate By similarity
Binding site521Substrate By similarity
Binding site631Substrate By similarity
Binding site881Substrate By similarity
Binding site931Substrate By similarity
Binding site1561Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P37529 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: B02CDBAA1C518305

FASTA21725,444
        10         20         30         40         50         60 
MKEHHIPKNS IITVAGTVGV GKSTLTKTLA KRLGFKTSLE EVDHNPYLEK FYHDFERWSF 

        70         80         90        100        110        120 
HLQIYFLAER FKEQKTIFEA GGGFVQDRSI YEDTGIFAKM HADKGTMSKV DYKTYTSLFE 

       130        140        150        160        170        180 
AMVMTPYFPH PDVLIYLEGD LENILNRIEQ RGREMELQTS RSYWEEMHTR YENWISGFNA 

       190        200        210 
CPVLKLRIED YDLLNDENSI ENIVDQIASV IHDNQKK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D26185 Genomic DNA. Translation: BAA05250.1.
AL009126 Genomic DNA. Translation: CAB11790.1.
PIRS66044.
RefSeqNP_387895.1. NC_000964.3.

3D structure databases

ProteinModelPortalP37529.
SMRP37529. Positions 6-212.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU00140.

Proteomic databases

PaxDbP37529.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11790; CAB11790; BSU00140.
GeneID936793.
KEGGbsu:BSU00140.
PATRIC18971489. VBIBacSub10457_0015.

Organism-specific databases

GenoListBSU00140. [Micado]

Phylogenomic databases

eggNOGCOG1428.
HOGENOMHOG000030092.
KOK15519.
OMAFVDNPED.
ProtClustDBCLSK884721.

Enzyme and pathway databases

BioCycBSUB:BSU00140-MONOMER.
SABIO-RKP37529.

Family and domain databases

InterProIPR002624. Deoxynucleoside_kinase.
[Graphical view]
PANTHERPTHR10513. PTHR10513. 1 hit.
PfamPF01712. dNK. 1 hit.
[Graphical view]
PIRSFPIRSF000705. DNK. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCK_BACSU
AccessionPrimary (citable) accession number: P37529
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents