ID G2M4I0_HELPX Unreviewed; 191 AA.
AC G2M4I0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
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:AEN16022.1};
GN ORFNames=HPPN120_07215 {ECO:0000313|EMBL:AEN16022.1};
OS Helicobacter pylori Puno120.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055528 {ECO:0000313|EMBL:AEN16022.1, ECO:0000313|Proteomes:UP000008532};
RN [1] {ECO:0000313|EMBL:AEN16022.1, ECO:0000313|Proteomes:UP000008532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puno120 {ECO:0000313|EMBL:AEN16022.1,
RC ECO:0000313|Proteomes:UP000008532};
RA Kersulyte D., Cabrera L., Hooper C.C., Jahuira Arias H., Gilman R.H.,
RA Berg D.E.;
RL Submitted (AUG-2011) 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; CP002980; AEN16022.1; -; Genomic_DNA.
DR RefSeq; WP_000289744.1; NC_017378.1.
DR AlphaFoldDB; G2M4I0; -.
DR KEGG; hep:HPPN120_07215; -.
DR PATRIC; fig|1055528.4.peg.1435; -.
DR HOGENOM; CLU_049131_0_0_7; -.
DR Proteomes; UP000008532; 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; 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; UMP-CMP KINASE 2, MITOCHONDRIAL; 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|HAMAP-Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AEN16022.1};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00165};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AEN16022.1}.
FT DOMAIN 5..183
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 191 AA; 21384 MW; 8DDA97A1F0F4C693 CRC64;
MYVVLEGVDG AGKSTQVGLL KDRFKNALFT KEPGGTRMGE SLRHIALNES ISELARAFLF
LSDRAEHIES VIKPALKEKK LIISDRSLIS GMAYSEFSSL ELNLLATQSV LPEKIILLLI
DKEGLKQRLS LKSLDKIENQ GTEKLLTIQQ KLKTHAHALK EKFGCEVLEL DAQKSVWDLH
RQIVAFIECV V
//