ID H8KCF4_RICMS Unreviewed; 203 AA.
AC H8KCF4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Thymidylate kinase {ECO:0000256|ARBA:ARBA00017144, ECO:0000256|HAMAP-Rule:MF_00165};
DE EC=2.7.4.9 {ECO:0000256|ARBA:ARBA00012980, ECO:0000256|HAMAP-Rule:MF_00165};
DE AltName: Full=dTMP kinase {ECO:0000256|ARBA:ARBA00029962, ECO:0000256|HAMAP-Rule:MF_00165};
GN Name=tmk {ECO:0000256|HAMAP-Rule:MF_00165,
GN ECO:0000313|EMBL:AFC73412.1};
GN OrderedLocusNames=MCI_02500 {ECO:0000313|EMBL:AFC73412.1};
OS Rickettsia montanensis (strain OSU 85-930).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=1105114 {ECO:0000313|EMBL:AFC73412.1, ECO:0000313|Proteomes:UP000008008};
RN [1] {ECO:0000313|Proteomes:UP000008008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU 85-930 {ECO:0000313|Proteomes:UP000008008};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT "Complete genome sequence of Rickettsia montanensis strain OSU 85-930.";
RL Submitted (FEB-2012) 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; CP003340; AFC73412.1; -; Genomic_DNA.
DR RefSeq; WP_014409514.1; NC_017043.1.
DR AlphaFoldDB; H8KCF4; -.
DR KEGG; rmo:MCI_02500; -.
DR HOGENOM; CLU_049131_0_2_5; -.
DR Proteomes; UP000008008; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AFC73412.1};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165, ECO:0000313|EMBL:AFC73412.1}.
FT DOMAIN 12..199
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 203 AA; 23434 MW; ECC91941E8FED608 CRC64;
MNNLKQGKFI TFEGGEGIGK STQSQMLYEY LQSQNIPVIL TREVGGTIVA EKMREILVHE
ELLPTSELLQ VMAARYDHMV RKIIPALQEG HIVICDRFID STACYQGLEL ENGIDLVYNL
HKTLMPSLMP DITFFIDVEP DTAIKRVNSR NMSNKFDIRG IDFYKKIYDC FKELSNRFPE
RIKTIKTLDL SPLEVHELIK KHL
//
