ID E3E848_PAEPS Unreviewed; 220 AA.
AC E3E848;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 Name=tdk {ECO:0000313|EMBL:ADO57161.1};
GN ORFNames=PPSC2_14985 {ECO:0000313|EMBL:ADO57161.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57161.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO57161.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO57161.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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; CP002213; ADO57161.1; -; Genomic_DNA.
DR AlphaFoldDB; E3E848; -.
DR STRING; 1406.LK13_02620; -.
DR KEGG; ppm:PPSC2_14985; -.
DR PATRIC; fig|886882.15.peg.3198; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_3_0_9; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000006868; 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 Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ SEQUENCE 220 AA; 24792 MW; 4DA84AA28405E3DA CRC64;
MAFSFGDEDL QRYVHVKRGE FALPTGRITI ITGPMFSEKS GELIRRCQKL IQYGHRKVVA
YKPAEDNRYA EDEIVSRIGY RLPAISIPRK LTDELVQRIL QETKDADVVA FDEVQFFSRH
IMSLIQELAY CGKHVIADGL NLDYRGKEFG YVGGLLAMAD DIEKLTSFCA VCGSSEAVFT
QRMVNGKPST VGPIVMIGDS EAYEPRCRNC FIPPHKVNCE
//
