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Entry: M5EFI8_9FIRM
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Original site: M5EFI8_9FIRM 
ID   M5EFI8_9FIRM            Unreviewed;       208 AA.
AC   M5EFI8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Thymidylate kinase {ECO:0000256|HAMAP-Rule:MF_00165};
DE            EC=2.7.4.9 {ECO:0000256|HAMAP-Rule:MF_00165};
DE   AltName: Full=dTMP kinase {ECO:0000256|HAMAP-Rule:MF_00165};
GN   Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165};
GN   ORFNames=HSACCH_01740 {ECO:0000313|EMBL:CCU79958.1};
OS   Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU79958.1, ECO:0000313|Proteomes:UP000012063};
RN   [1] {ECO:0000313|Proteomes:UP000012063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX   PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA   Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT   "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT   Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL   Genome Announc. 1:217-225(2013).
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:CCU79958.1}.
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DR   EMBL; CAUI01000021; CCU79958.1; -; Genomic_DNA.
DR   RefSeq; WP_005489265.1; NZ_CAUI01000021.1.
DR   AlphaFoldDB; M5EFI8; -.
DR   STRING; 1293054.HSACCH_01740; -.
DR   eggNOG; COG0125; Bacteria.
DR   InParanoid; M5EFI8; -.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000012063; 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; IPR018095; Thymidylate_kin_CS.
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.
DR   PROSITE; PS01331; THYMIDYLATE_KINASE; 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:CCU79958.1};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW   Rule:MF_00165};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000012063};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:CCU79958.1}.
FT   DOMAIN          9..199
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   208 AA;  23906 MW;  5549E45BEA462134 CRC64;
     MTEGFFITFE GIEGSGKTTQ INLLAEFLKN KGYDVLVSRE PGGTPLGEKI RHLLLDPQYE
     SMDYRTEILL YAADRAQHVK EKIKPAIEQG KIVISDRFAD SNLAYQAAGR GLDYEIVYQI
     NDWVIDSTWP DLTFILDIDI KEGLKRARAQ SFDAEGDRLE REVDEFHQRV REAYLKMAEK
     DRFALVNAGE SIENVQKNIE NIISRRLF
//
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