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Database: UniProt
Entry: A0A413G218_9FIRM
LinkDB: A0A413G218_9FIRM
Original site: A0A413G218_9FIRM 
ID   A0A413G218_9FIRM        Unreviewed;       220 AA.
AC   A0A413G218;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=DWV16_11900 {ECO:0000313|EMBL:RGX54774.1};
OS   Anaerotruncus sp. AF02-27.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=2292191 {ECO:0000313|EMBL:RGX54774.1, ECO:0000313|Proteomes:UP000284135};
RN   [1] {ECO:0000313|EMBL:RGX54774.1, ECO:0000313|Proteomes:UP000284135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF02-27 {ECO:0000313|EMBL:RGX54774.1,
RC   ECO:0000313|Proteomes:UP000284135};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:RGX54774.1}.
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DR   EMBL; QSBX01000015; RGX54774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A413G218; -.
DR   Proteomes; UP000284135; 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   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   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:RGX54774.1};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW   Rule:MF_00165}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284135};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT   DOMAIN          8..198
FT                   /note="Thymidylate kinase-like"
FT                   /evidence="ECO:0000259|Pfam:PF02223"
SQ   SEQUENCE   220 AA;  25174 MW;  EF2E2A8A29E4FFBA CRC64;
     MNGKLIVIDG LDGSGKHTQT ERLAKRLRDE GERVRMVSFP DYAEPSSALV KQYLAGEFGQ
     AGDVSPYAAS SFYAVDRYAS YNKFWKKDYQ SGYTILADRY ATSNLIHQMS KLPKGAWDSF
     AGWMENFEYQ KLGLPRPDAV LYLDMHPDVS RTLITARYGG DESRRDIHES DFDYMARCRE
     CALYAAEHFG WFLIHCSDEK QAFPIEDISE EIYGLVKNIL
//
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