ID   KTHY_VIBCH              Reviewed;         212 AA.
AC   Q9KQI2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=VC_2016;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {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   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR   EMBL; AE003852; AAF95164.1; -; Genomic_DNA.
DR   PIR; A82128; A82128.
DR   RefSeq; NP_231650.1; NC_002505.1.
DR   RefSeq; WP_000991933.1; NZ_LT906614.1.
DR   PDB; 3LV8; X-ray; 1.80 A; A=1-212.
DR   PDB; 3N2I; X-ray; 2.25 A; A/B=1-212.
DR   PDBsum; 3LV8; -.
DR   PDBsum; 3N2I; -.
DR   AlphaFoldDB; Q9KQI2; -.
DR   SMR; Q9KQI2; -.
DR   STRING; 243277.VC_2016; -.
DR   DNASU; 2613395; -.
DR   EnsemblBacteria; AAF95164; AAF95164; VC_2016.
DR   GeneID; 57740637; -.
DR   KEGG; vch:VC_2016; -.
DR   PATRIC; fig|243277.26.peg.1926; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_1_6; -.
DR   OMA; VMTREPG; -.
DR   BioCyc; VCHO:VC2016-MON; -.
DR   EvolutionaryTrace; Q9KQI2; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR   GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR   GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
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..212
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155367"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   STRAND          5..11
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           16..29
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   STRAND          35..41
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           45..55
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           65..82
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           84..89
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   STRAND          93..98
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           100..106
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   TURN            107..111
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           115..126
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           141..146
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   TURN            156..159
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           162..178
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   STRAND          182..186
FT                   /evidence="ECO:0007829|PDB:3LV8"
FT   HELIX           191..206
FT                   /evidence="ECO:0007829|PDB:3LV8"
SQ   SEQUENCE   212 AA;  23666 MW;  8F4F51A00CE60F4D CRC64;
     MNAKFIVIEG LEGAGKSTAI QVVVETLQQN GIDHITRTRE PGGTLLAEKL RALVKEEHPG
     EELQDITELL LVYAARVQLV ENVIKPALAR GEWVVGDRHD MSSQAYQGGG RQIAPSTMQS
     LKQTALGDFK PDLTLYLDID PKLGLERARG RGELDRIEKM DISFFERARE RYLELANSDD
     SVVMIDAAQS IEQVTADIRR ALQDWLSQVN RV