KTHY_ONYPE
ID KTHY_ONYPE Reviewed; 207 AA.
AC Q7WSH2; Q6YQZ3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; Synonyms=tmk-B;
GN OrderedLocusNames=PAM_230;
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=262768;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12904564; DOI=10.1099/mic.0.25834-0;
RA Miyata S., Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Kuboyama T.,
RA Ugaki M., Namba S.;
RT "Two different thymidylate kinase gene homologues, including one that has
RT catalytic activity, are encoded in the onion yellows phytoplasma genome.";
RL Microbiology 149:2243-2250(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M;
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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}.
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DR EMBL; AB094668; BAC81721.1; -; Genomic_DNA.
DR EMBL; AP006628; BAD04315.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WSH2; -.
DR SMR; Q7WSH2; -.
DR STRING; 262768.PAM_230; -.
DR EnsemblBacteria; BAD04315; BAD04315; PAM_230.
DR KEGG; poy:PAM_230; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_2_14; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR BioCyc; OYEL262768:G1G26-276-MON; -.
DR Proteomes; UP000002523; 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..207
FT /note="Thymidylate kinase"
FT /id="PRO_0000155315"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ SEQUENCE 207 AA; 24083 MW; 189AAD655D674ABD CRC64;
MFISFEGCEG TGKTTHSRYL FEKLSKKYSC VLTKEPGGGL FNEVIRNILL HSSNKQIDFH
TEALLFAADR AEHLSKLIIP ALQQNKIVIC DRYLDSTIAY QVYARGLSQD FVLNINNFAL
NYIPNITFYL DLDPKIGIQR VKQFRPKEIN SFDLQKLSFH KKVRKGYLDL CQKDQQKRIF
LIDASKPLEN IYNIIEQKLK EVFQIEL
