ID KTHY_VACCW Reviewed; 204 AA.
AC Q80HT9; P13410;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 13-SEP-2023, entry version 70.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9 {ECO:0000269|PubMed:16336263};
DE AltName: Full=dTMP kinase;
GN Name=OPG178; Synonyms=TMK; OrderedLocusNames=VACWR174; ORFNames=A48R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2552411; DOI=10.1093/nar/17.19.7581;
RA Smith G.L., de Carlos A., Chan Y.S.;
RT "Vaccinia virus encodes a thymidylate kinase gene: sequence and
RT transcriptional mapping.";
RL Nucleic Acids Res. 17:7581-7590(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2045793; DOI=10.1099/0022-1317-72-6-1349;
RA Smith G.L., Chan Y.S., Howard S.T.;
RT "Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the
RT right inverted terminal repeat.";
RL J. Gen. Virol. 72:1349-1376(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=1657913; DOI=10.1016/s0021-9258(18)54896-1;
RA Hughes S.J., Johnston L.H., de Carlos A., Smith G.L.;
RT "Vaccinia virus encodes an active thymidylate kinase that complements a
RT cdc8 mutant of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 266:20103-20109(1991).
RN [5]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=16336263; DOI=10.1111/j.1742-4658.2005.05006.x;
RA Topalis D., Collinet B., Gasse C., Dugue L., Balzarini J., Pochet S.,
RA Deville-Bonne D.;
RT "Substrate specificity of vaccinia virus thymidylate kinase.";
RL FEBS J. 272:6254-6265(2005).
CC -!- FUNCTION: Poxvirus TMP kinase is able to phosphorylate dTMP, dUMP and
CC also dGMP from any purine and pyrimidine nucleoside triphosphate. The
CC large substrate specificity is explained by the presence of a canal
CC connecting the edge of the dimer interface to the TMP base binding
CC pocket, canal not found in the human homolog.
CC {ECO:0000269|PubMed:16336263, ECO:0000269|PubMed:1657913}.
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 Evidence={ECO:0000269|PubMed:16336263};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC -!- SUBUNIT: Homodimer; the dimer arrangement is orthogonal and not
CC antiparallel as in human enzyme. {ECO:0000269|PubMed:16336263}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO89453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X16259; CAA34345.1; -; Genomic_DNA.
DR EMBL; D11079; BAA01822.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89453.1; ALT_INIT; Genomic_DNA.
DR PIR; E42522; KIVZ5W.
DR SMR; Q80HT9; -.
DR UniPathway; UPA00575; -.
DR Proteomes; UP000000344; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004798; F:thymidylate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006233; P:dTDP biosynthetic process; IEA:InterPro.
DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00041; DTMP_kinase; 1.
DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR PANTHER; PTHR10344:SF1; THYMIDYLATE KINASE; 1.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Early protein; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..204
FT /note="Thymidylate kinase"
FT /id="PRO_0000155219"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
SQ SEQUENCE 204 AA; 23219 MW; 911DFD2C671CF6B3 CRC64;
MSRGALIVFE GLDKSGKTTQ CMNIMESIPA NTIKYLNFPQ RSTVTGKMID DYLTRKKTYN
DHIVNLLFCA NRWEFASFIQ EQLEQGITLI VDRYAFSGVA YAAAKGASMT LSKSYESGLP
KPDLVIFLES GSKEINRNVG EEIYEDVTFQ QKVLQEYKKM IEEGDIHWQI ISSEFEEDVK
KELIKNIVIE AIHTVTGPVG QLWM
//
