ID U2XWX1_9PROT Unreviewed; 214 AA.
AC U2XWX1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=RS24_00294 {ECO:0000313|EMBL:ERL47356.1};
OS Candidatus Micropelagos thuwalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade; Micropelagos.
OX NCBI_TaxID=1397666 {ECO:0000313|EMBL:ERL47356.1, ECO:0000313|Proteomes:UP000016762};
RN [1] {ECO:0000313|EMBL:ERL47356.1, ECO:0000313|Proteomes:UP000016762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS24 {ECO:0000313|EMBL:ERL47356.1,
RC ECO:0000313|Proteomes:UP000016762};
RX PubMed=24785133; DOI=10.1111/1574-6941.12348;
RA Jimenez-Infante F., Ngugi D.K., Alam I., Rashid M., Baalawi W., Kamau A.A.,
RA Bajic V.B., Stingl U.;
RT "Genomic differentiation among two strains of the PS1 clade isolated from
RT geographically separated marine habitats.";
RL FEMS Microbiol. Ecol. 89:181-197(2014).
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:ERL47356.1}.
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DR EMBL; AWXE01000001; ERL47356.1; -; Genomic_DNA.
DR RefSeq; WP_021776374.1; NZ_AWXE01000001.1.
DR AlphaFoldDB; U2XWX1; -.
DR STRING; 1397666.RS24_00294; -.
DR PATRIC; fig|1397666.3.peg.269; -.
DR eggNOG; COG0125; Bacteria.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000016762; 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; 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}; Kinase {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00165};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00165}; Transferase {ECO:0000256|HAMAP-Rule:MF_00165}.
FT DOMAIN 15..204
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 214 AA; 23521 MW; CBE1F8AD076EBBDF CRC64;
MDAPSVKNPG RFITLEGGEG AGKSTQIQVV KDFLLTRGND VVVTREPGGT SEGQEIRNLL
VSGDKDKWSP LSETLLILAD RAAHLERVIR PALAEGKYVV CDRFFDSTRA YQGVAGGLGL
DVIHNLQQPV LGTTLPDVTL LLDIDPEKGL RRAQERGGEL RFESKTLAYH RTLRNAFLDF
AAQEPDRIFV IDADRDVEVV SADILAVLDE RLDV
//
