DGK_DICDI
ID DGK_DICDI Reviewed; 285 AA.
AC Q54UT2; Q14EL5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Deoxyguanosine kinase;
DE Short=dGK;
DE EC=2.7.1.113;
DE AltName: Full=DddGK;
GN Name=dgk; ORFNames=DDB_G0280843;
OS Dictyostelium discoideum (Slime mold).
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: Purine-specific deoxyribonucleoside kinase that
CC phosphorylates preferentially deoxyguanosine, as part of the
CC deoxyribonucleotide salvage pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC EC=2.7.1.113; Evidence={ECO:0000269|PubMed:17448496};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for deoxyguanosine {ECO:0000269|PubMed:17448496};
CC KM=206 uM for deoxyadenosine {ECO:0000269|PubMed:17448496};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; AY669384; AAV85947.1; -; mRNA.
DR EMBL; AAFI02000025; EAL67033.2; -; Genomic_DNA.
DR RefSeq; XP_641009.2; XM_635917.2.
DR AlphaFoldDB; Q54UT2; -.
DR SMR; Q54UT2; -.
DR STRING; 44689.DDB0233982; -.
DR PaxDb; Q54UT2; -.
DR EnsemblProtists; EAL67033; EAL67033; DDB_G0280843.
DR GeneID; 8621793; -.
DR KEGG; ddi:DDB_G0280843; -.
DR dictyBase; DDB_G0280843; dgk.
DR eggNOG; KOG3877; Eukaryota.
DR HOGENOM; CLU_050591_0_0_1; -.
DR InParanoid; Q54UT2; -.
DR OMA; KYALIMQ; -.
DR PhylomeDB; Q54UT2; -.
DR BRENDA; 2.7.1.113; 1939.
DR SABIO-RK; Q54UT2; -.
DR PRO; PR:Q54UT2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IDA:dictyBase.
DR GO; GO:0006180; P:deoxyguanosine salvage; IDA:dictyBase.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..285
FT /note="Deoxyguanosine kinase"
FT /id="PRO_0000327522"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 39..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 285 AA; 33193 MW; 1857E13F82E733C5 CRC64;
MFRRSLMFMI SNNKNTNMVS SINTTNKVNN FSKIIILEGN ISAGKTYLSS KLGDLLGYKV
FLEPTATNPY LSLFYKEPSK YALIMQKWLL NQRYNTFLNA LQYSLENEQG VILDRSVYSD
WVFAENCRSE GLISAEGFKE YNSIRDRFLS NIPIPNVTLF LDVDPKQCLQ RIQNRKRDCE
QSIPLSYLSG LDNCYKKFLI EMKSKGSNVI ILDWNNFGDI NLVLNEINND NFNNFNNSNN
SKFNDVNYKK QQLISDIENE KNNLKEMKFF LNENNNNNNQ EKIKS
