ID Q63HF3_BACCZ Unreviewed; 211 AA.
AC Q63HF3;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Deoxyguanosine kinase {ECO:0000313|EMBL:AAU20213.1};
DE EC=2.7.1.113 {ECO:0000313|EMBL:AAU20213.1};
GN Name=dgk {ECO:0000313|EMBL:AAU20213.1};
GN OrderedLocusNames=BCE33L0016 {ECO:0000313|EMBL:AAU20213.1};
OS Bacillus cereus (strain ZK / E33L).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU20213.1, ECO:0000313|Proteomes:UP000002612};
RN [1] {ECO:0000313|Proteomes:UP000002612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC {ECO:0000256|ARBA:ARBA00007420}.
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DR EMBL; CP000001; AAU20213.1; -; Genomic_DNA.
DR RefSeq; WP_000148224.1; NZ_CP009968.1.
DR AlphaFoldDB; Q63HF3; -.
DR GeneID; 75083278; -.
DR KEGG; bcz:BCE33L0016; -.
DR PATRIC; fig|288681.22.peg.140; -.
DR Proteomes; UP000002612; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IEA:UniProtKB-EC.
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; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10513:SF46; DEOXYGUANOSINE KINASE; 1.
DR PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Kinase {ECO:0000313|EMBL:AAU20213.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Transferase {ECO:0000313|EMBL:AAU20213.1}.
FT DOMAIN 7..204
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 11..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 138..142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ SEQUENCE 211 AA; 24688 MW; 26D5A12CAE702621 CRC64;
MTGVPFITVE GPIGVGKTSL AKEISTHMQL HLLKEIVDEN PFLGKFYEDI DEWSFQTEMF
FLCNRYKQLE DINIKYLNQR KPVVADYHIF KNVIFASRTL KDSQYDKYMQ IYRILTQDMP
VPNVIVYLTA SLETLQKRIA MRGREFEKNM DPNYLLQLTK DYETAMDAFK KDHPDIPVLK
FNGDDMDFVK NPDDLNVILS ALQNTLLKES K
//
