KITH_THEMA
ID KITH_THEMA Reviewed; 184 AA.
AC Q9WYN2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Thymidine kinase;
DE EC=2.7.1.21;
GN Name=tdk; OrderedLocusNames=TM_0401;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS; THYMIDINE
RP AND ATP ANALOGS, AND SUBUNIT.
RX PubMed=17407781; DOI=10.1016/j.jmb.2007.02.104;
RA Segura-Pena D., Lutz S., Monnerjahn C., Konrad M., Lavie A.;
RT "Binding of ATP to TK1-like enzymes is associated with a conformational
RT change in the quaternary structure.";
RL J. Mol. Biol. 369:129-141(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP THYMIDINE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP HIS-53; GLY-55 AND LEU-129.
RX PubMed=18073106; DOI=10.1016/j.str.2007.09.025;
RA Segura-Pena D., Lichter J., Trani M., Konrad M., Lavie A., Lutz S.;
RT "Quaternary structure change as a mechanism for the regulation of thymidine
RT kinase 1-like enzymes.";
RL Structure 15:1555-1566(2007).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for ATP {ECO:0000269|PubMed:18073106};
CC KM=0.5 uM for thymidine {ECO:0000269|PubMed:18073106};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17407781,
CC ECO:0000269|PubMed:18073106}.
CC -!- INTERACTION:
CC Q9WYN2; Q9WYN2: tdk; NbExp=2; IntAct=EBI-15674853, EBI-15674853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35486.1; -; Genomic_DNA.
DR PIR; B72383; B72383.
DR RefSeq; NP_228211.1; NC_000853.1.
DR RefSeq; WP_004083238.1; NZ_CP011107.1.
DR PDB; 2ORW; X-ray; 1.50 A; A/B=1-184.
DR PDB; 2QPO; X-ray; 1.95 A; A/B/C/D=1-184.
DR PDB; 2QQ0; X-ray; 1.50 A; A/B=1-184.
DR PDB; 2QQE; X-ray; 1.90 A; A/B=1-184.
DR PDBsum; 2ORW; -.
DR PDBsum; 2QPO; -.
DR PDBsum; 2QQ0; -.
DR PDBsum; 2QQE; -.
DR AlphaFoldDB; Q9WYN2; -.
DR SMR; Q9WYN2; -.
DR DIP; DIP-29527N; -.
DR STRING; 243274.THEMA_02720; -.
DR EnsemblBacteria; AAD35486; AAD35486; TM_0401.
DR KEGG; tma:TM0401; -.
DR eggNOG; COG1435; Bacteria.
DR InParanoid; Q9WYN2; -.
DR OMA; ENTVNHK; -.
DR OrthoDB; 1279539at2; -.
DR BRENDA; 2.7.1.21; 6331.
DR SABIO-RK; Q9WYN2; -.
DR EvolutionaryTrace; Q9WYN2; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004797; F:thymidine kinase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046104; P:thymidine metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00124; Thymidine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..184
FT /note="Thymidine kinase"
FT /id="PRO_0000175040"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 83..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 161..164
FT /ligand="substrate"
FT BINDING 169
FT /ligand="substrate"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 53
FT /note="H->A: Reduced affinity for ATP."
FT /evidence="ECO:0000269|PubMed:18073106"
FT MUTAGEN 55
FT /note="G->W: Reduced affinity for ATP."
FT /evidence="ECO:0000269|PubMed:18073106"
FT MUTAGEN 129
FT /note="L->W: Reduced affinity for thymidine."
FT /evidence="ECO:0000269|PubMed:18073106"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2ORW"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2ORW"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2ORW"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2ORW"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:2ORW"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2ORW"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2QQE"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2ORW"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2ORW"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2ORW"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:2ORW"
SQ SEQUENCE 184 AA; 20654 MW; 906B2C1BE3A7EDDA CRC64;
MSGKLTVITG PMYSGKTTEL LSFVEIYKLG KKKVAVFKPK IDSRYHSTMI VSHSGNGVEA
HVIERPEEMR KYIEEDTRGV FIDEVQFFNP SLFEVVKDLL DRGIDVFCAG LDLTHKQNPF
ETTALLLSLA DTVIKKKAVC HRCGEYNATL TLKVAGGEEE IDVGGQEKYI AVCRDCYNTL
KKRV
