KTHY_THEMA
ID KTHY_THEMA Reviewed; 197 AA.
AC Q9X0I3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=TM_1099;
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).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36175.1; -; Genomic_DNA.
DR PIR; E72294; E72294.
DR RefSeq; NP_228905.1; NC_000853.1.
DR RefSeq; WP_004080341.1; NZ_CP011107.1.
DR PDB; 3HJN; X-ray; 2.10 A; A/B=1-197.
DR PDBsum; 3HJN; -.
DR AlphaFoldDB; Q9X0I3; -.
DR SMR; Q9X0I3; -.
DR STRING; 243274.THEMA_08850; -.
DR EnsemblBacteria; AAD36175; AAD36175; TM_1099.
DR KEGG; tma:TM1099; -.
DR eggNOG; COG0125; Bacteria.
DR InParanoid; Q9X0I3; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR EvolutionaryTrace; Q9X0I3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..197
FT /note="Thymidylate kinase"
FT /id="PRO_0000155359"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:3HJN"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 57..79
FT /evidence="ECO:0007829|PDB:3HJN"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3HJN"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:3HJN"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:3HJN"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:3HJN"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3HJN"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3HJN"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:3HJN"
SQ SEQUENCE 197 AA; 22849 MW; 302D2EF3BAB6658E CRC64;
MFITFEGIDG SGKSTQIQLL AQYLEKRGKK VILKREPGGT ETGEKIRKIL LEEEVTPKAE
LFLFLASRNL LVTEIKQYLS EGYAVLLDRY TDSSVAYQGF GRNLGKEIVE ELNDFATDGL
IPDLTFYIDV DVETALKRKG ELNRFEKREF LERVREGYLV LAREHPERIV VLDGKRSIEE
IHRDVVREVK RRWKLDV
