ID   DGK1_LACAC              Reviewed;         215 AA.
AC   P0C1F9; Q59483; Q5FHT0;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Deoxyadenosine kinase;
DE            Short=DADO kinase;
DE            Short=DAK;
DE            EC=2.7.1.76;
DE   AltName: Full=Deoxynucleoside kinase complex I S-component;
GN   OrderedLocusNames=LBA1949;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC   -!- FUNCTION: DGK/DAK plays an essential role in generating the
CC       deoxyribonucleotide precursors, dGTP and dATP, for DNA metabolism.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Heterodimer of a deoxyadenosine (DAK) and a deoxyguanosine
CC       kinase (DGK). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR   EMBL; CP000033; AAV43744.1; -; Genomic_DNA.
DR   RefSeq; WP_003549467.1; NC_006814.3.
DR   RefSeq; YP_194775.1; NC_006814.3.
DR   AlphaFoldDB; P0C1F9; -.
DR   SMR; P0C1F9; -.
DR   STRING; 272621.LBA1949; -.
DR   GeneID; 56943496; -.
DR   KEGG; lac:LBA1949; -.
DR   PATRIC; fig|272621.13.peg.1853; -.
DR   eggNOG; COG1428; Bacteria.
DR   HOGENOM; CLU_030466_2_1_9; -.
DR   OrthoDB; 9776634at2; -.
DR   BioCyc; LACI272621:G1G49-1900-MONOMER; -.
DR   BRENDA; 2.7.1.76; 2846.
DR   Proteomes; UP000006381; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..215
FT                   /note="Deoxyadenosine kinase"
FT                   /id="PRO_0000175095"
FT   ACT_SITE        79
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         9..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  24780 MW;  D809444D93676648 CRC64;
     MIQVIVLSGP IGAGKSSLTS ILAEHLGTQA FYEGVDSNPV LPLYYKDMKR YTFLLNTYLL
     NHRLAQINQA IQEKNSVSDR SIYEDALFFK MNADSSVADP TEFKIYNDLL ENMMEDTPGN
     PSKKPDLLIY IHVSLDTMLK RIKKRGRSFE QISTDPSLKD YYARLLKYYE PWYENYNASP
     KIMINGDKLD FVTNMNAQKE VLKEIDEKLR EIGNL
//