Reviewed,
UniProtKB/Swiss-Prot P37530 (DGK_BACSU)
Last modified
December 15, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Deoxyguanosine kinase Short name=DGUO kinase Short name=dGK EC=2.7.1.113 | ||||||
| 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 | 207 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 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. Ref.3 |
| Catalytic activity | ATP + deoxyguanosine = ADP + dGMP. |
| Enzyme regulation | Inhibited by deoxyguanosine at concentrations above 30 µM only with UTP as phosphate donor. dGTP is a potent competitive inhibitor. Ref.3 |
| Subunit structure | Homodimer. Ref.3 |
| Miscellaneous | Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism. |
| Sequence similarities | Belongs to the DCK/DGK family. |
| Biophysicochemical properties | Kinetic parameters: KM=0.6 µM for deoxyguanosine (with UTP at pH 7.8 and at 37 degrees Celsius) KM=1.7 µM for deoxyguanosine (with CTP at pH 7.8 and at 37 degrees Celsius) KM=6.5 µM for deoxyguanosine (with ATP at pH 7.8 and at 37 degrees Celsius) KM=10.4 µM for deoxyguanosine (with GTP at pH 7.8 and at 37 degrees Celsius) KM=6 µM for UTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) KM=35 µM for CTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) KM=36 µM for ATP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) KM=46 µM for GTP (with deoxyguanosine at pH 7.8 and at 37 degrees Celsius) Vmax=8.1 µmol/min/mg enzyme toward deoxyguanosine (with 0.5 mM UTP at pH 7.8 and at 37 degrees Celsius) pH dependence: 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. |
| Mass spectrometry | Molecular mass is 24147 Da from positions 1 - 207. Determined by ESI. Ref.3 |
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 deoxyguanosine kinase activityInferred from electronic annotation. Source: EC phosphotransferase activity, alcohol group as acceptorInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
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] | "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: FUNCTION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION, NOMENCLATURE, SUBUNIT. |
Cross-references
Sequence databases | |
|---|---|
| D26185 Genomic DNA. Translation: BAA05251.1. AL009126 Genomic DNA. Translation: CAB11791.1. | |
| PIR | S66045. |
| RefSeq | NP_387896.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 937037. |
| GenomeReviews | Gene locus BSU00150 in contig AL009126_GR. |
| KEGG | bsu:BSU00150. |
| NMPDR | fig|224308.1.peg.15. |
Organism-specific databases | |
| SubtiList | BG10079. dgk. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG725501. |
| OMA | NPFLEKF. |
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 | DGK_BACSU | ||||||||
| Accession | Primary (citable) accession number: P37530 | ||||||||
| 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 |

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