ID A0A0R1GSA2_9LACO Unreviewed; 208 AA.
AC A0A0R1GSA2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Deoxynucleoside kinase {ECO:0000313|EMBL:KRK36847.1};
GN ORFNames=FD07_GL000432 {ECO:0000313|EMBL:KRK36847.1};
OS Levilactobacillus parabrevis ATCC 53295.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1267003 {ECO:0000313|EMBL:KRK36847.1, ECO:0000313|Proteomes:UP000051176};
RN [1] {ECO:0000313|EMBL:KRK36847.1, ECO:0000313|Proteomes:UP000051176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53295 {ECO:0000313|EMBL:KRK36847.1,
RC ECO:0000313|Proteomes:UP000051176};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the DCK/DGK family.
CC {ECO:0000256|ARBA:ARBA00007420}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK36847.1}.
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DR EMBL; AZCZ01000015; KRK36847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1GSA2; -.
DR STRING; 357278.IV61_GL000507; -.
DR PATRIC; fig|1267003.4.peg.467; -.
DR eggNOG; COG1428; Bacteria.
DR Proteomes; UP000051176; Unassembled WGS sequence.
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; DEOXYNUCLEOSIDE KINASE; 1.
DR PANTHER; PTHR10513:SF15; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 10, MITOCHONDRIAL; 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:KRK36847.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Transferase {ECO:0000313|EMBL:KRK36847.1}.
FT DOMAIN 2..197
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 132..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
SQ SEQUENCE 208 AA; 24153 MW; 560083C3BFF61ED3 CRC64;
MIGVGKTTLT GKIASHLNTQ AFFEPVGDNP VLPLYYRDPK QYGFLLQIYF LNKRFSMIKR
ALADDNNVLD RSIYEDALFT RENNAEGNIT DTELEVYLQL LDNMMTELNE LPKKAPDLLV
YADADFDTIL HRIKKRGRDY EQFDNNPELE SYYKKMWTAY QGWFADYDIS PKIKIDLQKY
DLDKPGNTEL VLAQIDDALK DIRTDATV
//