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Database: UniProt
Entry: Q63R50_BURPS
LinkDB: Q63R50_BURPS
Original site: Q63R50_BURPS 
ID   Q63R50_BURPS            Unreviewed;       227 AA.
AC   Q63R50;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Deoxyguanosine kinase/deoxyadenosine kinase {ECO:0000313|EMBL:CAH36833.1};
GN   OrderedLocusNames=BPSL2823 {ECO:0000313|EMBL:CAH36833.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH36833.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH36833.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH36833.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA   Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA   Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA   Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA   Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA   Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA   Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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DR   EMBL; BX571965; CAH36833.1; -; Genomic_DNA.
DR   RefSeq; WP_004532195.1; NZ_CP009538.1.
DR   RefSeq; YP_109418.1; NC_006350.1.
DR   AlphaFoldDB; Q63R50; -.
DR   STRING; 272560.BPSL2823; -.
DR   GeneID; 56528375; -.
DR   KEGG; bps:BPSL2823; -.
DR   PATRIC; fig|272560.51.peg.2481; -.
DR   eggNOG; COG1428; Bacteria.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019136; F:deoxynucleoside kinase activity; IEA:InterPro.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Kinase {ECO:0000313|EMBL:CAH36833.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605};
KW   Transferase {ECO:0000313|EMBL:CAH36833.1}.
FT   DOMAIN          20..210
FT                   /note="Deoxynucleoside kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01712"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT   BINDING         24..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT   BINDING         150..154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
SQ   SEQUENCE   227 AA;  25774 MW;  C5C78A6A0151CD1F CRC64;
     MNSTPLTVTA PDWRPPCRYL AIEGPIGVGK TTLATLLAER WSMRALLERP QDNPFLERFY
     RDTARYALPT QLAFALQRER QAREIAAAHE ANTPIVADFM PQKNEIFARL TLPDDEWQLY
     RSLAAHLDAP APAPDLVVYL QASPEVLFSR IQKRGEPMEL QIGDAYLRSL CDAYNEFFYH
     YDRTPVLTVA AEHLNPLDSP DDLALLVDRI ASMRGRKEFF VKGGSAR
//
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