KTHY_BURTA
ID KTHY_BURTA Reviewed; 206 AA.
AC Q2SWM4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=BTH_I2154;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC37302.1; -; Genomic_DNA.
DR RefSeq; WP_009890673.1; NZ_CP008785.1.
DR PDB; 3V9P; X-ray; 1.90 A; A/B=1-206.
DR PDBsum; 3V9P; -.
DR AlphaFoldDB; Q2SWM4; -.
DR SMR; Q2SWM4; -.
DR PRIDE; Q2SWM4; -.
DR EnsemblBacteria; ABC37302; ABC37302; BTH_I2154.
DR GeneID; 66547363; -.
DR KEGG; bte:BTH_I2154; -.
DR HOGENOM; CLU_049131_0_2_4; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR Proteomes; UP000001930; Chromosome I.
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; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..206
FT /note="Thymidylate kinase"
FT /id="PRO_1000023165"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 18..32
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3V9P"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3V9P"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:3V9P"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:3V9P"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3V9P"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 160..178
FT /evidence="ECO:0007829|PDB:3V9P"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3V9P"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3V9P"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:3V9P"
SQ SEQUENCE 206 AA; 23084 MW; F505F81A4825AAE4 CRC64;
MARGKFITFE GIDGAGKTTH LQWFCDRLQE RLGPAGRHVV VTREPGGTRL GETLREILLN
QPMDLETEAL LMFAGRREHL ALVIEPALAR GDWVVSDRFT DATFAYQGGG RGLPRDKLEA
LERWVQGGFQ PDLTVLFDVP PQIASARRGA VRMPDKFESE SDAFFARTRA EYLRRAQEAP
HRFVIVDSSE PIAQIRKQLE GVLAAL
