KTHY_THET8
ID KTHY_THET8 Reviewed; 198 AA.
AC Q5SHX3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=TTHA1607;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000255|HAMAP-Rule:MF_00165}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR EMBL; AP008226; BAD71430.1; -; Genomic_DNA.
DR RefSeq; WP_011173647.1; NC_006461.1.
DR RefSeq; YP_144873.1; NC_006461.1.
DR PDB; 5X7J; X-ray; 1.84 A; A/B=1-198.
DR PDB; 5X86; X-ray; 1.19 A; A/B=1-198.
DR PDB; 5X8A; X-ray; 2.51 A; A/B=1-198.
DR PDB; 5X8B; X-ray; 1.39 A; A/B=1-198.
DR PDB; 5X8C; X-ray; 2.07 A; A/B=1-198.
DR PDB; 5X8D; X-ray; 2.26 A; A/B=1-198.
DR PDB; 5X8J; X-ray; 1.80 A; A/B=1-198.
DR PDB; 5X8K; X-ray; 1.67 A; A/B=1-198.
DR PDB; 5X8V; X-ray; 1.66 A; A/B=1-198.
DR PDB; 5X98; X-ray; 1.76 A; A/B=1-198.
DR PDB; 5X99; X-ray; 1.73 A; A/B=1-198.
DR PDB; 5XAK; X-ray; 1.50 A; A/B=1-198.
DR PDB; 5XAL; X-ray; 1.84 A; A/B=1-198.
DR PDB; 5XT8; X-ray; 2.01 A; A/B=1-198.
DR PDB; 5ZAX; X-ray; 2.36 A; A/B=1-198.
DR PDB; 5ZB0; X-ray; 1.19 A; A/B=1-198.
DR PDB; 5ZB4; X-ray; 1.92 A; A/B=1-198.
DR PDBsum; 5X7J; -.
DR PDBsum; 5X86; -.
DR PDBsum; 5X8A; -.
DR PDBsum; 5X8B; -.
DR PDBsum; 5X8C; -.
DR PDBsum; 5X8D; -.
DR PDBsum; 5X8J; -.
DR PDBsum; 5X8K; -.
DR PDBsum; 5X8V; -.
DR PDBsum; 5X98; -.
DR PDBsum; 5X99; -.
DR PDBsum; 5XAK; -.
DR PDBsum; 5XAL; -.
DR PDBsum; 5XT8; -.
DR PDBsum; 5ZAX; -.
DR PDBsum; 5ZB0; -.
DR PDBsum; 5ZB4; -.
DR AlphaFoldDB; Q5SHX3; -.
DR SMR; Q5SHX3; -.
DR STRING; 300852.55772989; -.
DR EnsemblBacteria; BAD71430; BAD71430; BAD71430.
DR GeneID; 3169786; -.
DR KEGG; ttj:TTHA1607; -.
DR PATRIC; fig|300852.9.peg.1577; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_2_0; -.
DR OMA; VMTREPG; -.
DR PhylomeDB; Q5SHX3; -.
DR BRENDA; 2.7.4.9; 2305.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniRule.
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..198
FT /note="Thymidylate kinase"
FT /id="PRO_0000155361"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:5X86"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5X86"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:5X86"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:5X86"
FT TURN 100..104
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:5X86"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5X7J"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:5X7J"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:5X86"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5X86"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:5X86"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5X86"
SQ SEQUENCE 198 AA; 21979 MW; D2D908A11DC07F55 CRC64;
MPGLFLTLEG LDGSGKTTQA RRLAAFLEAQ GRPVLLTREP GGGLPEVRSL LLTQELSPEA
EYLLFSADRA EHVRKVILPG LAAGKVVISD RYLDSSLAYQ GYGRGLPLPW LREVAREATR
GLKPRLTFLL DLPPEAALRR VRRPDRLEGL GLEFFRRVRE GYLALARAEP GRFVVLDATL
PEEEIARAIQ AHLRPLLP
