ID F8IIA9_ALIAT Unreviewed; 146 AA.
AC F8IIA9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:AEJ42068.1};
GN OrderedLocusNames=TC41_0089 {ECO:0000313|EMBL:AEJ42068.1};
OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ42068.1, ECO:0000313|Proteomes:UP000000292};
RN [1] {ECO:0000313|EMBL:AEJ42068.1, ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ42068.1,
RC ECO:0000313|Proteomes:UP000000292};
RX PubMed=21914900; DOI=10.1128/JB.05709-11;
RA Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT 4-1.";
RL J. Bacteriol. 193:5602-5603(2011).
RN [2] {ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA Chen Y., He Y., Dong Z., Hu S.;
RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT 1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002902; AEJ42068.1; -; Genomic_DNA.
DR AlphaFoldDB; F8IIA9; -.
DR STRING; 1048834.TC41_0089; -.
DR KEGG; aad:TC41_0089; -.
DR PATRIC; fig|1048834.4.peg.81; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_2_1_9; -.
DR Proteomes; UP000000292; 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 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}.
SQ SEQUENCE 146 AA; 16584 MW; 11CA79C8BC328890 CRC64;
MGISKQALVV EEDTDLFESV RAQMPDCVLV DEVQFLRAYH VQQLARVADD LDIPVIMYGL
LKDYRNRLFE GSEAAILWAD RIEEIKTICA HPGCDRKATM ILKVKDGRPV YEGEQIEVGG
NDLYKSVCRK HYFHPDVEGL MRATGP
//
