ID   KTHY_EHRCR              Reviewed;         202 AA.
AC   Q2GHN3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=ECH_0229;
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000236; ABD45252.1; -; Genomic_DNA.
DR   RefSeq; WP_006010009.1; NC_007799.1.
DR   PDB; 3LD9; X-ray; 2.15 A; A/B/C/D=1-202.
DR   PDBsum; 3LD9; -.
DR   AlphaFoldDB; Q2GHN3; -.
DR   SMR; Q2GHN3; -.
DR   STRING; 205920.ECH_0229; -.
DR   EnsemblBacteria; ABD45252; ABD45252; ECH_0229.
DR   KEGG; ech:ECH_0229; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_0_5; -.
DR   OMA; VMTREPG; -.
DR   OrthoDB; 1585072at2; -.
DR   BRENDA; 2.7.4.9; 2043.
DR   EvolutionaryTrace; Q2GHN3; -.
DR   Proteomes; UP000008320; 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..202
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_1000023190"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
FT   STRAND          1..6
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           13..28
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           43..53
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           60..77
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   STRAND          88..93
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           95..102
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   TURN            103..106
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           110..120
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   STRAND          126..132
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           152..168
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   TURN            170..172
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   STRAND          173..179
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:3LD9"
FT   HELIX           187..199
FT                   /evidence="ECO:0007829|PDB:3LD9"
SQ   SEQUENCE   202 AA;  23199 MW;  2E3B104B4CB40E17 CRC64;
     MFITFEGIDG SGKTTQSHLL AEYLSEIYGV NNVVLTREPG GTLLNESVRN LLFKAQGLDS
     LSELLFFIAM RREHFVKIIK PSLMQKKIVI CDRFIDSTIA YQGYGQGIDC SLIDQLNDLV
     IDVYPDITFI IDVDINESLS RSCKNGYEFA DMEFYYRVRD GFYDIAKKNP HRCHVITDKS
     ETYDIDDINF VHLEVIKVLQ MV