KTHY_CHRSD
ID KTHY_CHRSD Reviewed; 212 AA.
AC Q1QX49;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Thymidylate kinase {ECO:0000255|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000255|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000255|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000255|HAMAP-Rule:MF_00165}; OrderedLocusNames=Csal_1606;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
CC -!- FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and
CC salvage pathways of dTTP synthesis. {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00165};
CC -!- SIMILARITY: Belongs to the thymidylate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00165}.
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DR EMBL; CP000285; ABE58959.1; -; Genomic_DNA.
DR RefSeq; WP_011506905.1; NC_007963.1.
DR AlphaFoldDB; Q1QX49; -.
DR SMR; Q1QX49; -.
DR STRING; 290398.Csal_1606; -.
DR EnsemblBacteria; ABE58959; ABE58959; Csal_1606.
DR KEGG; csa:Csal_1606; -.
DR eggNOG; COG0125; Bacteria.
DR HOGENOM; CLU_049131_0_2_6; -.
DR OMA; VMTREPG; -.
DR OrthoDB; 1585072at2; -.
DR Proteomes; UP000000239; 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 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; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Thymidylate kinase"
FT /id="PRO_1000023177"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00165"
SQ SEQUENCE 212 AA; 23342 MW; 0D4F022AC5AA3BA5 CRC64;
MTPGRFITLE GGEGVGKSTN VAFVCDWLSA RGIEVVRTRE PGGTPRAEAI RELLLDPAPQ
EPLDETAELL LMFAARAQHL AARIRPALAR GAWVVCDRFT DATFAYQGGG RGLDETRIAT
LEALVQQGLQ PDLTLLLDMP VEAAQRRVER RGIERDRFER ERGAFFNAVR ESYLARAAQA
PTRFAVIDAD RSLEAVQASI AAHLTERLAS WS