ID   DAK_DICDI               Reviewed;         245 AA.
AC   Q54YL2; Q49UB1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Deoxyadenosine kinase;
DE            EC=2.7.1.76;
DE   AltName: Full=DddDAK;
DE            Short=DAK;
GN   Name=dak; ORFNames=DDB_G0278191;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=AX4;
RX   PubMed=17448496; DOI=10.1016/j.jmb.2007.03.053;
RA   Sandrini M.P.B., Soederbom F., Mikkelsen N.E., Piskur J.;
RT   "Dictyostelium discoideum salvages purine deoxyribonucleosides by highly
RT   specific bacterial-like deoxyribonucleoside kinases.";
RL   J. Mol. Biol. 369:653-664(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Specific kinase that phosphorylates deoxyadenosine but not
CC       any other deoxyribonucleoside, as part of the deoxyribonucleotide
CC       salvage pathway.
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; Evidence={ECO:0000269|PubMed:17448496};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4 uM for thymidine {ECO:0000269|PubMed:17448496};
CC         KM=22.7 uM for deoxyadenosine {ECO:0000269|PubMed:17448496};
CC         KM=146 uM for fludarabine {ECO:0000269|PubMed:17448496};
CC         Note=Catalytic efficiency is 100-fold higher for deoxyadenosine than
CC         for thymidine.;
CC   -!- MISCELLANEOUS: Can also efficiently phosphorylate medically important
CC       adenosine analogs, such as 9-beta-d-arabinofuranosyl-2-fluoroadenine
CC       (fludarabine).
CC   -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR   EMBL; AY192983; AAO64433.1; -; mRNA.
DR   EMBL; AAFI02000023; EAL68268.1; -; Genomic_DNA.
DR   RefSeq; XP_642190.1; XM_637098.1.
DR   AlphaFoldDB; Q54YL2; -.
DR   SMR; Q54YL2; -.
DR   STRING; 44689.Q54YL2; -.
DR   PaxDb; 44689-DDB0232027; -.
DR   EnsemblProtists; EAL68268; EAL68268; DDB_G0278191.
DR   GeneID; 8621397; -.
DR   KEGG; ddi:DDB_G0278191; -.
DR   dictyBase; DDB_G0278191; dak.
DR   eggNOG; KOG4235; Eukaryota.
DR   HOGENOM; CLU_049131_0_1_1; -.
DR   InParanoid; Q54YL2; -.
DR   OMA; PYLADFY; -.
DR   PhylomeDB; Q54YL2; -.
DR   Reactome; R-DDI-73614; Pyrimidine salvage.
DR   Reactome; R-DDI-74217; Purine salvage.
DR   SABIO-RK; Q54YL2; -.
DR   PRO; PR:Q54YL2; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004136; F:deoxyadenosine kinase activity; IDA:dictyBase.
DR   GO; GO:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IDA:dictyBase.
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; IPR031314; DNK_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10513:SF49; DEOXYADENOSINE KINASE; 1.
DR   PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR   Pfam; PF01712; 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..245
FT                   /note="Deoxyadenosine kinase"
FT                   /id="PRO_0000327714"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         28..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   245 AA;  28416 MW;  ADA9B360DFE66B23 CRC64;
     MTTPILNSSV PGNIQKKSLE GTHIAISGLI GAGKTTLAVA LGKVLNLPTY FEEVIDNLYL
     QDFYKDPKKY GFQLQIYLLN SRFQQQQQII WQARGGVQDR TIYEDSVFAK MLNESGLLDD
     RDYNTYCKLF QNLSNFMRRP DLIIHLDVSP EKSLERIKLR NRDCEKDVSL EYLQNLYNAY
     HEFLQDISRY IPVIRINWSE FVDPEQLAQM IKAEYESMRF MNQINPPTFG NGPTTNKIIS
     TPKDL
//