ID   E0RDB7_PAEP6            Unreviewed;       208 AA.
AC   E0RDB7;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 2.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN   OrderedLocusNames=PPE_02825 {ECO:0000313|EMBL:ADM70652.2};
OS   Paenibacillus polymyxa (strain E681).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM70652.2, ECO:0000313|Proteomes:UP000002227};
RN   [1] {ECO:0000313|EMBL:ADM70652.2, ECO:0000313|Proteomes:UP000002227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E681 {ECO:0000313|EMBL:ADM70652.2,
RC   ECO:0000313|Proteomes:UP000002227};
RX   PubMed=20851896; DOI=10.1128/JB.00983-10;
RA   Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M.,
RA   Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.;
RT   "Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium
RT   Paenibacillus polymyxa E681.";
RL   J. Bacteriol. 192:6103-6104(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC         Evidence={ECO:0000256|RuleBase:RU000544};
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP000154; ADM70652.2; -; Genomic_DNA.
DR   AlphaFoldDB; E0RDB7; -.
DR   KEGG; ppy:PPE_02825; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_3_0_9; -.
DR   Proteomes; UP000002227; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   InterPro; IPR020633; Thymidine_kinase_CS.
DR   PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR   PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW   ECO:0000256|RuleBase:RU000544};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000544};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT   ACT_SITE        101
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ   SEQUENCE   208 AA;  23466 MW;  617E61DD8D01ED0A CRC64;
     MYMLQRGEFA LPTGRITIIT GPMFSEKSGE LIRRCQKLIQ YGHRKVVAYK PAEDNRYAED
     EIVSRIGYRL PAISIPRKLT DELVQRILQE TKDADVVAFD EVQFFSRHIM SLVQELAYYG
     KHVIADGLNL DYRGKEFGYV GGLLAMADDI EKLTSFCAVC GSSEAVFTQR MVNGKPSTVG
     PIVMIGDSEA YEPRCRNCFI PPHKVNCD
//