Reviewed, UniProtKB/Swiss-Prot P37529 (DCK_BACSU)

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

Name:	dck
Synonyms:	dak, yaaF
Ordered Locus Names:	BSU00140

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 activity Inferred from electronic annotation. Source: EC deoxycytidine kinase activity Inferred from electronic annotation. Source: EC phosphotransferase activity, alcohol group as acceptor Inferred 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

	Sequence		Length	Mass (Da)
	P37529-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: B02CDBAA1C518305	FASTA	217	25,444
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 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
EMBLGenBankDDBJ	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

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 24, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)