ID   DCK_BACSU               Reviewed;         217 AA.
AC   P37529;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Deoxyadenosine/deoxycytidine kinase;
DE            Short=dAK/dCK;
DE            EC=2.7.1.74;
DE            EC=2.7.1.76;
GN   Name=dck; Synonyms=dak, yaaF; OrderedLocusNames=BSU00140;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND
RP   ACTIVITY REGULATION.
RX   PubMed=6251049; DOI=10.1016/s0021-9258(19)70633-4;
RA   Moellgaard H.;
RT   "Deoxyadenosine/deoxycytidine kinase from Bacillus subtilis. Purification,
RT   characterization, and physiological function.";
RL   J. Biol. Chem. 255:8216-8220(1980).
RN   [4]
RP   NOMENCLATURE, AND SUBUNIT.
RX   PubMed=11078735; DOI=10.1074/jbc.m007918200;
RA   Andersen R.B., Neuhard J.;
RT   "Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus
RT   subtilis. Substrate specificity and kinetic analysis of deoxyguanosine
RT   kinase with UTP as the preferred phosphate donor.";
RL   J. Biol. Chem. 276:5518-5524(2001).
CC   -!- FUNCTION: Plays an essential role in generating the deoxyribonucleotide
CC       precursors dATP and dCTP for DNA metabolism. The phosphate acceptor
CC       specificity is strict toward deoxyadenosine (dAdo) and deoxycytidine
CC       (dCyd). The specificity toward the sugar moiety of the nucleoside is
CC       less strict. Both 2-deoxyribose, ribose, and arabinose nucleosides are
CC       phosphorylated, although the 2-deoxyribonucleosides are preferred. The
CC       phosphate donor specificity is dependent on the deoxyribonucleoside
CC       substrate, but GTP is efficient with both deoxycytidine and
CC       deoxyadenosine. Only nucleoside triphosphates can act as phosphate
CC       donors. {ECO:0000269|PubMed:6251049}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC         Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC         EC=2.7.1.76;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC         ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC   -!- ACTIVITY REGULATION: Deoxyadenosine inhibits deoxycytidine
CC       phosphorylation and deoxycytidine inhibits deoxyadenosine
CC       phosphorylation. Deoxyadenosine/deoxycytidine kinase is inhibited by
CC       both dATP and dCTP. {ECO:0000269|PubMed:6251049}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for deoxyadenosine (with GTP at pH 8.5 and at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:6251049};
CC         KM=5 uM for deoxycytidine (with GTP at pH 8.5 and at 37 degrees
CC         Celsius) {ECO:0000269|PubMed:6251049};
CC         KM=65 uM for GTP (with deoxyadenosine or deoxycytidine at pH 7.8 and
CC         at 37 degrees Celsius) {ECO:0000269|PubMed:6251049};
CC       pH dependence:
CC         Optimum pH is around pH 8.6. At pH 8.0-9.6 more than 90% of maximal
CC         activity is still observed. {ECO:0000269|PubMed:6251049};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11078735}.
CC   -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR   EMBL; D26185; BAA05250.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11790.1; -; Genomic_DNA.
DR   PIR; S66044; S66044.
DR   RefSeq; NP_387895.1; NC_000964.3.
DR   RefSeq; WP_003226792.1; NZ_JNCM01000024.1.
DR   AlphaFoldDB; P37529; -.
DR   SMR; P37529; -.
DR   STRING; 224308.BSU00140; -.
DR   PaxDb; 224308-BSU00140; -.
DR   EnsemblBacteria; CAB11790; CAB11790; BSU_00140.
DR   GeneID; 83883219; -.
DR   GeneID; 936793; -.
DR   KEGG; bsu:BSU00140; -.
DR   PATRIC; fig|224308.179.peg.14; -.
DR   eggNOG; COG1428; Bacteria.
DR   InParanoid; P37529; -.
DR   OrthoDB; 9776634at2; -.
DR   PhylomeDB; P37529; -.
DR   BioCyc; BSUB:BSU00140-MONOMER; -.
DR   BioCyc; MetaCyc:BSU00140-MONOMER; -.
DR   SABIO-RK; P37529; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004137; F:deoxycytidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd01673; dNK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002624; DCK/DGK.
DR   InterPro; IPR031314; DNK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR   PANTHER; PTHR10513:SF15; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 10, MITOCHONDRIAL; 1.
DR   Pfam; PF01712; dNK; 1.
DR   PIRSF; PIRSF000705; DNK; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..217
FT                   /note="Deoxyadenosine/deoxycytidine kinase"
FT                   /id="PRO_0000049430"
FT   ACT_SITE        87
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         16..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  25444 MW;  B02CDBAA1C518305 CRC64;
     MKEHHIPKNS IITVAGTVGV GKSTLTKTLA KRLGFKTSLE EVDHNPYLEK FYHDFERWSF
     HLQIYFLAER FKEQKTIFEA GGGFVQDRSI YEDTGIFAKM HADKGTMSKV DYKTYTSLFE
     AMVMTPYFPH PDVLIYLEGD LENILNRIEQ RGREMELQTS RSYWEEMHTR YENWISGFNA
     CPVLKLRIED YDLLNDENSI ENIVDQIASV IHDNQKK
//