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Database: UniProt
Entry: A0A0P0MGT9_9BURK
LinkDB: A0A0P0MGT9_9BURK
Original site: A0A0P0MGT9_9BURK 
ID   A0A0P0MGT9_9BURK        Unreviewed;       210 AA.
AC   A0A0P0MGT9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:ALK92181.1};
GN   ORFNames=L103DPR2_01783 {ECO:0000313|EMBL:ALK92181.1};
OS   Limnohabitans sp. 103DPR2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678129 {ECO:0000313|EMBL:ALK92181.1, ECO:0000313|Proteomes:UP000063254};
RN   [1] {ECO:0000313|EMBL:ALK92181.1, ECO:0000313|Proteomes:UP000063254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103DPR2 {ECO:0000313|EMBL:ALK92181.1,
RC   ECO:0000313|Proteomes:UP000063254};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) 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; CP011834; ALK92181.1; -; Genomic_DNA.
DR   RefSeq; WP_055360764.1; NZ_CP011834.1.
DR   AlphaFoldDB; A0A0P0MGT9; -.
DR   STRING; 1678129.L103DPR2_01783; -.
DR   KEGG; lim:L103DPR2_01783; -.
DR   PATRIC; fig|1678129.3.peg.1776; -.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000063254; 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; THYMIDYLATE KINASE; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00165};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ALK92181.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000063254};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:ALK92181.1}.
FT   DOMAIN          9..197
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   210 AA;  23569 MW;  6056583FD55C74EE CRC64;
     MKSAWFISFE GIDGAGKSTH IEGLAQWFKS RGHVVTLTRE PGGTPLAEKF RELALHESMD
     PLTEALVMFA ARREHLVQVI EPALARGEVV LCDRFTDATF AYQGGGRGFD WNVLKALEQM
     VQKVPATTLR QPDLTIWFDL DPAIAAQRLS TARVPDKFES QPQSFFQAVR DGYAKRMQES
     PLRFVQIAAD QSREGVWSEV LRAVELAYAK
//
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