DGK_BACSU
ID DGK_BACSU Reviewed; 207 AA.
AC P37530;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Deoxyguanosine kinase;
DE Short=DGUO kinase;
DE Short=dGK;
DE EC=2.7.1.113;
GN Name=dgk; Synonyms=yaaG; OrderedLocusNames=BSU00150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, ACTIVITY REGULATION, NOMENCLATURE, AND SUBUNIT.
RX PubMed=11078735; DOI=10.1074/jbc.m007918200;
RA Andersen R.B., Neuhard J.;
RT "Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus
RT subtilis. Substrate specificity and kinetic analysis of deoxyguanosine
RT kinase with UTP as the preferred phosphate donor.";
RL J. Biol. Chem. 276:5518-5524(2001).
CC -!- FUNCTION: Plays an essential role in generating the deoxyribonucleotide
CC precursors dGTP for DNA metabolism. Highly specific toward
CC deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity
CC is observed with guanosine. UTP is slightly more efficient as phosphate
CC donor than CTP, ATP and GTP. {ECO:0000269|PubMed:11078735}.
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;
CC -!- ACTIVITY REGULATION: Inhibited by deoxyguanosine at concentrations
CC above 30 uM only with UTP as phosphate donor. dGTP is a potent
CC competitive inhibitor. {ECO:0000269|PubMed:11078735}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 uM for deoxyguanosine (with UTP at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=1.7 uM for deoxyguanosine (with CTP at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=6.5 uM for deoxyguanosine (with ATP at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=10.4 uM for deoxyguanosine (with GTP at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=6 uM for UTP (with deoxyguanosine at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=35 uM for CTP (with deoxyguanosine at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=36 uM for ATP (with deoxyguanosine at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC KM=46 uM for GTP (with deoxyguanosine at pH 7.8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:11078735};
CC Vmax=8.1 umol/min/mg enzyme toward deoxyguanosine (with 0.5 mM UTP at
CC pH 7.8 and at 37 degrees Celsius) {ECO:0000269|PubMed:11078735};
CC pH dependence:
CC Optimum pH is around pH 9 (with saturating concentrations of dGuo and
CC UTP). At pH 7.5 and 11.5 more than 80% of maximal activity is still
CC observed. At pH 6.0, 60% activity remains, whereas the enzyme is
CC completely inactive below pH 5.6. {ECO:0000269|PubMed:11078735};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11078735}.
CC -!- MASS SPECTROMETRY: Mass=24147; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11078735};
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; D26185; BAA05251.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11791.1; -; Genomic_DNA.
DR PIR; S66045; S66045.
DR RefSeq; NP_387896.1; NC_000964.3.
DR RefSeq; WP_003247138.1; NZ_JNCM01000024.1.
DR AlphaFoldDB; P37530; -.
DR STRING; 224308.BSU00150; -.
DR PaxDb; P37530; -.
DR PRIDE; P37530; -.
DR EnsemblBacteria; CAB11791; CAB11791; BSU_00150.
DR GeneID; 937037; -.
DR KEGG; bsu:BSU00150; -.
DR PATRIC; fig|224308.179.peg.15; -.
DR eggNOG; COG1428; Bacteria.
DR InParanoid; P37530; -.
DR OMA; IEEWSFQ; -.
DR PhylomeDB; P37530; -.
DR BioCyc; BSUB:BSU00150-MON; -.
DR BRENDA; 2.7.1.113; 658.
DR SABIO-RK; P37530; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; 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; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..207
FT /note="Deoxyguanosine kinase"
FT /id="PRO_0000049431"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 24145 MW; 0F77C6B31E9AA331 CRC64;
MNTAPFIAIE GPIGAGKTTL ATMLSQKFGF PMINEIVEDN PYLDKFYDNI KEWSFQLEMF
FLCHRYKQLE DTSDHFLKKG QPVIADYHIY KNVIFAERTL SPHQLEKYKK IYHLLTDDLP
KPNFIIYIKA SLPTLLHRIE KRGRPFEKKI ETSYLEQLIS DYEVAIKQLQ EADPELTVLT
VDGDSKDFVL NKSDFERIAA HVKELIV
