ID J1GSY8_9STRE Unreviewed; 212 AA.
AC J1GSY8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ECO:0000313|EMBL:EJG85828.1};
GN ORFNames=SPAR10_1426 {ECO:0000313|EMBL:EJG85828.1};
OS Streptococcus infantis SPAR10.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1159208 {ECO:0000313|EMBL:EJG85828.1, ECO:0000313|Proteomes:UP000010312};
RN [1] {ECO:0000313|EMBL:EJG85828.1, ECO:0000313|Proteomes:UP000010312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPAR10 {ECO:0000313|EMBL:EJG85828.1,
RC ECO:0000313|Proteomes:UP000010312};
RA Chancey S., Kumar N., Sengamalay N., Matthews C., Hine E., Pallavajjal A.,
RA Abolude O., Daugherty S.C., Parankush S.P., Sadzewicz L., Tallon L.J.,
RA Farley M.M., Baughman W., McGee L., Stephens D.S., Tettelin H.;
RT "Genomic Sequence of Streptococcus mitis SPAR10.";
RL Submitted (MAY-2012) 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: 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:EJG85828.1}.
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DR EMBL; ALCH01000005; EJG85828.1; -; Genomic_DNA.
DR RefSeq; WP_004253264.1; NZ_ALCH01000005.1.
DR AlphaFoldDB; J1GSY8; -.
DR PATRIC; fig|1159208.3.peg.1354; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000010312; 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:EJG85828.1};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00165}.
FT DOMAIN 9..198
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 212 AA; 23683 MW; C92E28F6896810A6 CRC64;
MSKGFLVSLE GPEGAGKTSV LEAILPLLEE KNIEFLTTRE PGGVLIGEKI REVILDPSHT
QMDPKTELLL YIASRRQHLV EKVLPALAAG KLVIMDRFID SSVAYQGFGR GLDIEAIDWL
NQFATDGLKP DLTLYFDVEV EKGLERIAAN SDREVNRLDL EGLDLHRKVR QGYLSLLKKD
GERIAKIDAS LPLDQVVENT KQVLFDRMGL TE
//
