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Database: UniProt
Entry: F1W1J9_9BURK
LinkDB: F1W1J9_9BURK
Original site: F1W1J9_9BURK 
ID   F1W1J9_9BURK            Unreviewed;       205 AA.
AC   F1W1J9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   ORFNames=IMCC9480_111 {ECO:0000313|EMBL:EGF31265.1};
OS   Oxalobacteraceae bacterium IMCC9480.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae.
OX   NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF31265.1, ECO:0000313|Proteomes:UP000004494};
RN   [1] {ECO:0000313|EMBL:EGF31265.1, ECO:0000313|Proteomes:UP000004494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF31265.1,
RC   ECO:0000313|Proteomes:UP000004494};
RX   PubMed=21572000; DOI=10.1128/JB.05088-11;
RA   Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT   "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT   betaproteobacterium isolated from the Arctic Ocean.";
RL   J. Bacteriol. 193:3421-3421(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGF31265.1}.
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DR   EMBL; AEPR01000475; EGF31265.1; -; Genomic_DNA.
DR   AlphaFoldDB; F1W1J9; -.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000004494; Unassembled WGS sequence.
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:EGF31265.1};
KW   Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004494};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   DOMAIN          12..196
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
FT   BINDING         14..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ   SEQUENCE   205 AA;  22837 MW;  989F4F649A22DD11 CRC64;
     MSTPSKPKFI TFEGIDGAGK SSHLSFVADL LVARGIRVTS TREPGGTPLG EQLRSVLLHQ
     KMHLETEALL MFASRREHLA QVIEPALARG DWVISDRFTD ATFAYQGGGR HLPVAKLEQL
     EQWVHPHLQP DLTLLFDVPL DVARARLDAT RSLDKFEQEQ SDFFAGVRGE YLRRAAQFPA
     RFRIVDSTQS MAQVRAALTA IMASL
//
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