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Database: UniProt
Entry: Q9CKE9
LinkDB: Q9CKE9
Original site: Q9CKE9 
ID   KTHY_PASMU              Reviewed;         209 AA.
AC   Q9CKE9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Thymidylate kinase;
DE            EC=2.7.4.9;
DE   AltName: Full=dTMP kinase;
GN   Name=tmk; OrderedLocusNames=PM1673;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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   -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK03757.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE004439; AAK03757.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_005718577.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKE9; -.
DR   SMR; Q9CKE9; -.
DR   STRING; 272843.PM1673; -.
DR   EnsemblBacteria; AAK03757; AAK03757; PM1673.
DR   KEGG; pmu:PM1673; -.
DR   PATRIC; fig|272843.6.peg.1693; -.
DR   HOGENOM; CLU_049131_0_1_6; -.
DR   OrthoDB; 9774907at2; -.
DR   Proteomes; UP000000809; 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; 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; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..209
FT                   /note="Thymidylate kinase"
FT                   /id="PRO_0000155317"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   209 AA;  23480 MW;  96CFF095398A8FD2 CRC64;
     MTTGKFIVLE GIEGAGKTTA RDSIVRALHA HGIHDIVFTR EPGGTPLAEK LRQLIKHETE
     EPVTDKAELL MLYAARIQLV ENVIKPALAQ GKWVIGDRHD MSSQAYQGGG RQLDQHLLHT
     LKQTILGEFE PDLTLYLDID PVLGLSRAKG RGALDRIEQQ NLDFFHRTRQ RYQELVRHNP
     KAVTIDASQT MSKVAEDVES AIETWLTTR
//
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