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Database: UniProt
Entry: W0MTV3_PSESX
LinkDB: W0MTV3_PSESX
Original site: W0MTV3_PSESX 
ID   W0MTV3_PSESX            Unreviewed;       210 AA.
AC   W0MTV3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|ARBA:ARBA00017144, ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980, ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00029962, ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165,
GN   ECO:0000313|EMBL:AHG42004.1};
GN   ORFNames=N018_18020 {ECO:0000313|EMBL:AHG42004.1};
OS   Pseudomonas syringae CC1557.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=1357279 {ECO:0000313|EMBL:AHG42004.1, ECO:0000313|Proteomes:UP000019089};
RN   [1] {ECO:0000313|EMBL:AHG42004.1, ECO:0000313|Proteomes:UP000019089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC1557 {ECO:0000313|EMBL:AHG42004.1,
RC   ECO:0000313|Proteomes:UP000019089};
RA   Baltrus D., Hockett K., Karlsrud E., Dougherty K., Nishimura M.;
RT   "Interactions Between Genome Architecture and Virulence Genes in
RT   Pseudomonas syringae, strain CC1557 as a model.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC       salvage pathways of dTTP synthesis. {ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001008, ECO:0000256|HAMAP-
CC         Rule:MF_00165};
CC   -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00009776, ECO:0000256|HAMAP-Rule:MF_00165}.
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DR   EMBL; CP007014; AHG42004.1; -; Genomic_DNA.
DR   RefSeq; WP_024645698.1; NZ_CP007014.1.
DR   AlphaFoldDB; W0MTV3; -.
DR   STRING; 1357279.N018_18020; -.
DR   KEGG; psyr:N018_18020; -.
DR   eggNOG; COG0125; Bacteria.
DR   HOGENOM; CLU_049131_0_2_6; -.
DR   Proteomes; UP000019089; 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   CDD; cd01672; TMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00165; Thymidylate_kinase; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039430; Thymidylate_kin-like_dom.
DR   InterPro; IPR018094; Thymidylate_kinase.
DR   NCBIfam; TIGR00041; DTMP_kinase; 1.
DR   PANTHER; PTHR10344; THYMIDYLATE KINASE; 1.
DR   PANTHER; PTHR10344:SF4; UMP-CMP KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF02223; Thymidylate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AHG42004.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AHG42004.1}.
FT   DOMAIN          8..195
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   210 AA;  23258 MW;  6ED6347B8DF609D1 CRC64;
     MTGLFITLEG PEGAGKSTNR DYLATRLREQ GVEVLMTREP GGTPLAERIR ELLLVPSDEA
     MSADTELLLV FAARAQHLAE VIRPALARGE VVLCDRFTDA TYAYQGGGRG LPRERIAALE
     QFVQGDLRPD LTLVFDLPVE IGLSRAAARG RLDRFEQEGR AFFDAVRTTY LDRAKAEPAR
     YRLVDASQTL AEVQAFLDTL LPQLLELQRG
//
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