ID A0A160P4U1_STRLU Unreviewed; 220 AA.
AC A0A160P4U1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Deoxyadenosine kinase {ECO:0000313|EMBL:BAU86727.1};
DE EC=2.7.1.76 {ECO:0000313|EMBL:BAU86727.1};
GN ORFNames=SLA_5858 {ECO:0000313|EMBL:BAU86727.1};
OS Streptomyces laurentii.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU86727.1, ECO:0000313|Proteomes:UP000217676};
RN [1] {ECO:0000313|EMBL:BAU86727.1, ECO:0000313|Proteomes:UP000217676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU86727.1,
RC ECO:0000313|Proteomes:UP000217676};
RA Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT ATCC 31255.";
RL Genome Announc. 4:e00360-16(2016).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP017424; BAU86727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160P4U1; -.
DR KEGG; slau:SLA_5858; -.
DR Proteomes; UP000217676; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004136; F:deoxyadenosine 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; 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 4: Predicted;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Kinase {ECO:0000313|EMBL:BAU86727.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000217676};
KW Transferase {ECO:0000313|EMBL:BAU86727.1}.
FT DOMAIN 4..213
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 147..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
SQ SEQUENCE 220 AA; 25176 MW; 015A415C4D7F3544 CRC64;
MPVICVGGMI GIGKTSVAEL LAESLGSEVF YESVEDNPIL PLFYTASPEE IQAKRYPFLL
QLYFLQTRFA AIKDAYKEGN NVLDRSIYED WYFAKVNHDL GRISTLEMQV YEGLLDEMMR
EIDGLPYRKA PDLMVYLKAD FETVMHRIGL RGRDFEQDES LVEYYRTLWS GYDDWVHKHY
SASEVLVIDM NCTDVVNNPE DAIRVAQEVK EALAAGGCQV
//
