KTHY_HELPY
ID KTHY_HELPY Reviewed; 191 AA.
AC O26009;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9;
DE AltName: Full=dTMP kinase;
GN Name=tmk; OrderedLocusNames=HP_1474;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000250}.
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 -!- INTERACTION:
CC O26009; O25533: coaX; NbExp=2; IntAct=EBI-528054, EBI-528040;
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; AE000511; AAD08513.1; -; Genomic_DNA.
DR PIR; B64704; B64704.
DR RefSeq; NP_208265.1; NC_000915.1.
DR RefSeq; WP_000289698.1; NC_018939.1.
DR AlphaFoldDB; O26009; -.
DR SMR; O26009; -.
DR DIP; DIP-3553N; -.
DR IntAct; O26009; 1.
DR MINT; O26009; -.
DR STRING; 85962.C694_07630; -.
DR PaxDb; O26009; -.
DR EnsemblBacteria; AAD08513; AAD08513; HP_1474.
DR KEGG; hpy:HP_1474; -.
DR PATRIC; fig|85962.47.peg.1585; -.
DR eggNOG; COG0125; Bacteria.
DR OMA; GMAYSQF; -.
DR PhylomeDB; O26009; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central.
DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central.
DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..191
FT /note="Thymidylate kinase"
FT /id="PRO_0000155283"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 191 AA; 21363 MW; 58F9F4BEA2F909C7 CRC64;
MYVVLEGVDG AGKSTQVELL KDRFKNALFT KEPGGTRMGE SLRRIALNEN ISELARAFLF
LSDRAEHTES VIKPALKEKK LIISDRSLIS GMAYSQFSSL ELNLLATQSV LPAKIILLLI
DKEGLKQRLS LKSLDKIENQ GIEKLLHIQQ KLKTHAYALQ EKFGCEVLEL DAKESVKNLH
EKIAAFIKCA V