KTHY_MYCTO
ID KTHY_MYCTO Reviewed; 214 AA.
AC P9WKE0; L0TDK8; O05891; Q7D5U8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=MT3345;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. This ion is required for
CC catalysis, binding to the active site transiently (at the TMP-binding
CC site), and probably acting as a clamp between the phosphoryl donor and
CC acceptor. {ECO:0000250};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47687.1; -; Genomic_DNA.
DR PIR; A70593; A70593.
DR RefSeq; WP_003417036.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WKE0; -.
DR SMR; P9WKE0; -.
DR EnsemblBacteria; AAK47687; AAK47687; MT3345.
DR KEGG; mtc:MT3345; -.
DR PATRIC; fig|83331.31.peg.3601; -.
DR HOGENOM; CLU_049131_1_0_11; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..214
FT /note="Thymidylate kinase"
FT /id="PRO_0000427670"
FT REGION 147..159
FT /note="LID"
FT /evidence="ECO:0000250"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 70
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 95
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 103
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="dTMP"
FT /ligand_id="ChEBI:CHEBI:63528"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 153
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
SQ SEQUENCE 214 AA; 22635 MW; E435123C250F46E7 CRC64;
MLIAIEGVDG AGKRTLVEKL SGAFRAAGRS VATLAFPRYG QSVAADIAAE ALHGEHGDLA
SSVYAMATLF ALDRAGAVHT IQGLCRGYDV VILDRYVASN AAYSAARLHE NAAGKAAAWV
QRIEFARLGL PKPDWQVLLA VSAELAGERS RGRAQRDPGR ARDNYERDAE LQQRTGAVYA
ELAAQGWGGR WLVVGADVDP GRLAATLAPP DVPS
