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
//
