KTHY_SHIFL
ID KTHY_SHIFL Reviewed; 213 AA.
AC P0A721; P37345;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=Thymidine monophosphate kinase;
DE AltName: Full=dTMP kinase;
DE Short=TMPK;
GN Name=tmk; OrderedLocusNames=SF1102, S1182;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine
CC monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as
CC its preferred phosphoryl donor. Situated at the junction of both de
CC novo and salvage pathways of deoxythymidine triphosphate (dTTP)
CC synthesis, is essential for DNA synthesis and cellular growth (By
CC similarity). {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 -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DOMAIN: The LID domain is a solvent-exposed domain that closes over the
CC site of phosphoryl transfer upon ATP binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; AE005674; AAN42721.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16609.1; -; Genomic_DNA.
DR RefSeq; NP_707014.1; NC_004337.2.
DR RefSeq; WP_001257000.1; NZ_WPGW01000001.1.
DR AlphaFoldDB; P0A721; -.
DR SMR; P0A721; -.
DR STRING; 198214.SF1102; -.
DR DrugBank; DB03280; p1-(5'-adenosyl)p5-(5'-thymidyl)pentaphosphate.
DR EnsemblBacteria; AAN42721; AAN42721; SF1102.
DR EnsemblBacteria; AAP16609; AAP16609; S1182.
DR GeneID; 1024058; -.
DR GeneID; 66670636; -.
DR KEGG; sfl:SF1102; -.
DR KEGG; sfx:S1182; -.
DR PATRIC; fig|198214.7.peg.1290; -.
DR HOGENOM; CLU_049131_0_1_6; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..213
FT /note="Thymidylate kinase"
FT /id="PRO_0000155337"
FT REGION 147..159
FT /note="LID"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 213 AA; 23783 MW; 16BC0A725AAFCB72 CRC64;
MRSKYIVIEG LEGAGKTTAR NVVVETLEQL GIRDMVFTRE PGGTQLAEKL RSLVLDIKSV
GDEVITDKAE VLMFYAARVQ LVETVIKPAL ANGTWVIGDR HDLSTQAYQG GGRGIDQHML
ATLRDAVLGD FRPDLTLYLD VTPEVGLKRA RARGELDRIE QESFDFFNRT RARYLELAAQ
DKSIHTIDAT QPLEAVMDAI RTTVTHWVKE LDA
