DGUOK_XENLA
ID DGUOK_XENLA Reviewed; 265 AA.
AC Q6GPW6;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Deoxyguanosine kinase, mitochondrial {ECO:0000305};
DE Short=XldGK {ECO:0000303|PubMed:27906638};
DE EC=2.7.1.113 {ECO:0000269|PubMed:27906638};
DE Flags: Precursor;
GN Name=dguok {ECO:0000312|Xenbase:XB-GENE-1006122};
GN ORFNames=XELAEV_18017396mg {ECO:0000312|EMBL:OCT88768.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH72990.1};
RN [1] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [2] {ECO:0000312|EMBL:AAH72990.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH72990.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27906638; DOI=10.1080/15257770.2016.1143557;
RA Mutahir Z., Christiansen L.S., Clausen A.R., Berchtold M.W., Gojkovic Z.,
RA Munch-Petersen B., Knecht W., Piskur J.;
RT "Gene duplications and losses among vertebrate deoxyribonucleoside kinases
RT of the non-TK1 Family.";
RL Nucleosides Nucleotides Nucleic Acids 35:677-690(2016).
CC -!- FUNCTION: Phosphorylates deoxyguanosine in the mitochondrial matrix
CC with high efficiency but shows very low activity against other
CC deoxynucleosides. {ECO:0000269|PubMed:27906638}.
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:27906638};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for deoxyguanosine {ECO:0000269|PubMed:27906638};
CC KM=2689 uM for deoxyadenosine {ECO:0000269|PubMed:27906638};
CC KM=4424 uM for deoxycytidine {ECO:0000269|PubMed:27906638};
CC KM=10624 uM for deoxyuridine {ECO:0000269|PubMed:27906638};
CC KM=201859 uM for deoxythymidine {ECO:0000269|PubMed:27906638};
CC Vmax=0.2 umol/min/mg enzyme toward deoxyguanosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.6 umol/min/mg enzyme toward deoxyadenosine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=1 umol/min/mg enzyme toward deoxycytidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.1 umol/min/mg enzyme toward deoxythymidine
CC {ECO:0000269|PubMed:27906638};
CC Vmax=0.04 umol/min/mg enzyme toward deoxyuridine
CC {ECO:0000269|PubMed:27906638};
CC Note=kcat is 0.11 sec(-1) with deoxyguanosine as substrate. kcat is
CC 0.30 sec(-1) with deoxyadenosine as substrate. kcat is 0.51 sec(-1)
CC with deoxycytidine as substrate. kcat is 0.02 sec(-1) with
CC deoxyuridine as substrate. kcat is 0.07 sec(-1) with deoxythymidine
CC as substrate. {ECO:0000269|PubMed:27906638};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16854}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9QX60}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; CM004470; OCT88768.1; -; Genomic_DNA.
DR EMBL; BC072990; AAH72990.1; -; mRNA.
DR RefSeq; NP_001085591.1; NM_001092122.1.
DR RefSeq; XP_018106416.1; XM_018250927.1.
DR AlphaFoldDB; Q6GPW6; -.
DR SMR; Q6GPW6; -.
DR STRING; 8355.Q6GPW6; -.
DR DNASU; 444017; -.
DR GeneID; 444017; -.
DR KEGG; xla:444017; -.
DR CTD; 444017; -.
DR Xenbase; XB-GENE-1006122; dguok.L.
DR OMA; LMIYLRC; -.
DR OrthoDB; 1505356at2759; -.
DR BRENDA; 2.7.1.113; 6725.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 444017; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IDA:UniProtKB.
DR GO; GO:0009157; P:deoxyribonucleoside monophosphate biosynthetic process; IDA:UniProtKB.
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; Kinase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..265
FT /note="Deoxyguanosine kinase, mitochondrial"
FT /id="PRO_0000449298"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-1"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16854"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 190..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-2"
FT BINDING 242..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PIRSR:PIRSR000705-3"
SQ SEQUENCE 265 AA; 31399 MW; 92CCFDCEC1047210 CRC64;
MKSQTTKPLQ QSISTNLSSN KEMQVKRLSV EGNIAVGKST FLRLLSNTFQ EWSFATEPLK
KWQNIQSTSF QTTTSSKPPM DNLLQLMYDD PKRWSYTFQT FSCMSRFKIQ IQPLSEPVLK
QQEHVQIFER SVYSDRYIFA KTLYELQHLN EMEWTLYQEW HTFLIQEFSR RVALDGIIYL
WATPEKCFER LQRRARKEEK TLQLQYLEKL HDQHESWLTK KTTEVSFENM KNIPVLLLNV
EEDFENNSAA GDELNNRVKA FVAGL