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Database: UniProt
Entry: G2M4I0_HELPX
LinkDB: G2M4I0_HELPX
Original site: G2M4I0_HELPX 
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
//
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