KTHY_BUCBP
ID KTHY_BUCBP Reviewed; 212 AA.
AC P59500;
DT 04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=bbp_323;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO27045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE016826; AAO27045.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P59500; -.
DR SMR; P59500; -.
DR STRING; 224915.bbp_323; -.
DR EnsemblBacteria; AAO27045; AAO27045; bbp_323.
DR KEGG; bab:bbp_323; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_1_6; -.
DR OMA; VMTREPG; -.
DR Proteomes; UP000000601; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Thymidylate kinase"
FT /id="PRO_0000155251"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ SEQUENCE 212 AA; 24547 MW; CD75D163C2B03AA1 CRC64;
MLKGKFIVIE GIEGSGKTTI CKTLKNILYE HGIKNVICVR DPGSTPLAEK IRSLLITKDK
NEYMVNETEL LLFYAARIQL IKNIIQPALN KGVWVISDRY FLSSLAYQCA GRKIKEEIVL
LLQSLFLKNF NPNITFYLDV TPEIGLNRIK NRNEIDRIEQ NTKFFFNNVR NKYLNLIKTK
PGIIKINANR KIDKVKHSCK QQMLSWLNTE NL