Reviewed,
UniProtKB/Swiss-Prot P37529 (DCK_BACSU)
Last modified
November 24, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Deoxyadenosine/deoxycytidine kinase Short name=dAK/dCK EC=2.7.1.76 EC=2.7.1.74 | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 217 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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) 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. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW deoxyadenosine kinase activityInferred from electronic annotation. Source: EC deoxycytidine kinase activityInferred from electronic annotation. Source: EC phosphotransferase activity, alcohol group as acceptorInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 217 | 217 | Deoxyadenosine/deoxycytidine kinase | PRO_0000049430 | |||
Sequences
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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: 7584024] [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. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [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: 6251049] [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: 11078735] [Abstract] Cited for: NOMENCLATURE, SUBUNIT. |
Cross-references
Sequence databases | |
|---|---|
| D26185 Genomic DNA. Translation: BAA05250.1. AL009126 Genomic DNA. Translation: CAB11790.1. | |
| PIR | S66044. |
| RefSeq | NP_387895.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 936793. |
| GenomeReviews | Gene locus BSU00140 in contig AL009126_GR. |
| KEGG | bsu:BSU00140. |
| NMPDR | fig|224308.1.peg.14. |
Organism-specific databases | |
| SubtiList | BG10078. dck. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P37529. |
| OMA | FFLNKRF |
Family and domain databases | |
| InterPro | IPR002624. Deoxynucleoside_kinase. [Graphical view] |
| PANTHER | PTHR10513. dNK. 1 hit. |
| Pfam | PF01712. dNK. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DCK_BACSU | ||||||||
| Accession | Primary (citable) accession number: P37529 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with


