ID A0A196L0C8_9MICO Unreviewed; 209 AA.
AC A0A196L0C8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=A4X16_04385 {ECO:0000313|EMBL:OAN36639.1};
OS Microbacterium sp. H83.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1827324 {ECO:0000313|EMBL:OAN36639.1, ECO:0000313|Proteomes:UP000078289};
RN [1] {ECO:0000313|EMBL:OAN36639.1, ECO:0000313|Proteomes:UP000078289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H83 {ECO:0000313|EMBL:OAN36639.1,
RC ECO:0000313|Proteomes:UP000078289};
RA Lymperopoulou D., Adams R.I., Lindow S., Coil D.A., Jospin G., Eisen J.A.;
RT "Draft Genome Sequences of Staphylococcus capitis Strain H36, S. capitis
RT Strain H65, S. cohnii Strain H62, S. hominis Strain H69, Mycobacterium
RT iranicum Strain H39, Plantibacter sp. Strain H53, Pseudomonas oryzihabitans
RT Strain H72, and Microbacterium sp. Strain H83, isolated from residential
RT settings.";
RL Submitted (APR-2016) 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}.
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:OAN36639.1}.
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DR EMBL; LWCU01000034; OAN36639.1; -; Genomic_DNA.
DR RefSeq; WP_067121325.1; NZ_LWCU01000034.1.
DR AlphaFoldDB; A0A196L0C8; -.
DR STRING; 1827324.A4X16_04385; -.
DR OrthoDB; 9774907at2; -.
DR Proteomes; UP000078289; 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:OAN36639.1};
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 11..200
FT /note="Thymidylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF02223"
FT BINDING 13..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00165"
SQ SEQUENCE 209 AA; 22464 MW; C02E1102BD898C4D CRC64;
MNSGGGVWIT LEGGDGSGKT TQSNLLAEWL EGAGRTVVRT REPGGSEVGQ LIRDIVLHHR
GDIAPRAEAL LYAADRAHHV STVVRPALER GEVVLQDRYL DSSVAYQGAG RVLDGDEIRD
LSLWAAEGAL PDLTVLLDLS PEAARVRLDS ADKPFDRLEA EKNDFHARVR DGYLGLAAAE
PERFLVLDAA AAPDVIAAQI RERVTALLG
//
