ID A0A0R1W741_9LACO Unreviewed; 213 AA.
AC A0A0R1W741;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Deoxyadenosine kinase {ECO:0000313|EMBL:KRM13389.1};
GN ORFNames=FD16_GL000864 {ECO:0000313|EMBL:KRM13389.1};
OS Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM13389.1, ECO:0000313|Proteomes:UP000051820};
RN [1] {ECO:0000313|EMBL:KRM13389.1, ECO:0000313|Proteomes:UP000051820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM13389.1,
RC ECO:0000313|Proteomes:UP000051820};
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:KRM13389.1}.
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DR EMBL; AZGF01000002; KRM13389.1; -; Genomic_DNA.
DR RefSeq; WP_010621609.1; NZ_BACO01000023.1.
DR AlphaFoldDB; A0A0R1W741; -.
DR STRING; 1423807.FD16_GL000864; -.
DR PATRIC; fig|1423807.3.peg.877; -.
DR eggNOG; COG1428; Bacteria.
DR OrthoDB; 9776634at2; -.
DR Proteomes; UP000051820; 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:KRM13389.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Transferase {ECO:0000313|EMBL:KRM13389.1}.
FT DOMAIN 2..207
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 6..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 139..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
SQ SEQUENCE 213 AA; 24535 MW; FA9CED2157E56111 CRC64;
MIVLSGTIGA GKTSLTQMLA DHLGSKAFYE SVDDNEILPL FYKDPKKYAF LLQIYFLNKR
LDEIKGAFVN DTDVLDRSIF EDSLLFGLNA DMGRATKTEV QIYNSLLKNM MEELPDEPHK
KAPDLMVHIH VSFDTMLARI KKRGRTYEQI DSDPSLYDYY QKLNERYVTW FNNYDESPKI
NIDGDKYNFV EDPSAAQKVM SMIDEKISAL SIN
//