ID A0A0A3ITV0_9BACI Unreviewed; 222 AA.
AC A0A0A3ITV0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Deoxycytidine kinase {ECO:0000313|EMBL:KGR88194.1};
GN ORFNames=CD32_02105 {ECO:0000313|EMBL:KGR88194.1};
OS Lysinibacillus odysseyi 34hs-1 = NBRC 100172.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1220589 {ECO:0000313|EMBL:KGR88194.1, ECO:0000313|Proteomes:UP000030437};
RN [1] {ECO:0000313|EMBL:KGR88194.1, ECO:0000313|Proteomes:UP000030437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100172 {ECO:0000313|EMBL:KGR88194.1,
RC ECO:0000313|Proteomes:UP000030437};
RA Zhang F., Wang G., Zhang L.;
RT "Draft genome sequence of Lysinibacillus odysseyi NBRC 100172.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KGR88194.1}.
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DR EMBL; JPVP01000042; KGR88194.1; -; Genomic_DNA.
DR RefSeq; WP_036150705.1; NZ_JPVP01000042.1.
DR AlphaFoldDB; A0A0A3ITV0; -.
DR STRING; 1220589.CD32_02105; -.
DR eggNOG; COG1428; Bacteria.
DR OrthoDB; 9776634at2; -.
DR Proteomes; UP000030437; 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:KGR88194.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000705-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000030437};
KW Transferase {ECO:0000313|EMBL:KGR88194.1}.
FT DOMAIN 15..211
FT /note="Deoxynucleoside kinase"
FT /evidence="ECO:0000259|Pfam:PF01712"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-1"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
FT BINDING 150..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-3"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000705-2"
SQ SEQUENCE 222 AA; 26134 MW; 4A9A21DE8A0F78FF CRC64;
MNLRDKYGIP ANAVITIAGT VGVGKSTMTK ALAEGLNFRT SFEKVDTNPY LDKFYDDFEK
WSFHLQVYFL AERFKEQKRI FEYGGGFIQD RSIYEDTGIF AKMHYDKGTM SPTDYETYTN
LFDAMVMTPY FPHPDLLVYL EGPIDHIIAR IQERGRAMEQ QTSNDYWYEM HERYENWINS
FNSCPVLRLD INDYDLVKQP SQIEGIIERI GYMLEQTSHL RK
//