ID U1LZF5_9BACL Unreviewed; 212 AA.
AC U1LZF5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=M467_12685 {ECO:0000313|EMBL:ERG68124.1};
OS Exiguobacterium chiriqhucha RW-2.
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1345023 {ECO:0000313|EMBL:ERG68124.1, ECO:0000313|Proteomes:UP000016464};
RN [1] {ECO:0000313|EMBL:ERG68124.1, ECO:0000313|Proteomes:UP000016464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RW-2 {ECO:0000313|EMBL:ERG68124.1,
RC ECO:0000313|Proteomes:UP000016464};
RX PubMed=23929485;
RA White R.A.III., Grassa C.J., Suttle C.A.;
RT "Draft Genome Sequence of Exiguobacterium pavilionensis Strain RW-2, with
RT Wide Thermal, Salinity, and pH Tolerance, Isolated from Modern Freshwater
RT Microbialites.";
RL Genome Announc. 1:e00597-e00513(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERG68124.1}.
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DR EMBL; ATCL01000010; ERG68124.1; -; Genomic_DNA.
DR RefSeq; WP_021065764.1; NZ_ATCL01000010.1.
DR AlphaFoldDB; U1LZF5; -.
DR STRING; 1385984.GCA_000702565_00003; -.
DR PATRIC; fig|1345023.5.peg.606; -.
DR eggNOG; COG0125; Bacteria.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000016464; Unassembled WGS sequence.
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; 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.
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:ERG68124.1};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727, ECO:0000256|HAMAP-
KW Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00165}; Reference proteome {ECO:0000313|Proteomes:UP000016464};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT DOMAIN 8..197
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 212 AA; 24068 MW; 3862215C36B71346 CRC64;
MKGMFITVEG PDGSGKTTQL QLLVRSLTEK GYEVVVTREP GGTKVGNSIR EVLLSPEHDE
MTPRVEMMLY AASRAQNIDQ VIRPALKRGA IVVCDRFVDA SIAYQGYGLQ YDLNQILSLN
EWATAGIKPD LTFLFDLPPD QASRRMKDRG QLDRIESRDE SFHQRVYDGF KKILEQHPDR
MVRIDANATI EMIQDEVLDI TLERLNERGV TQ
//
