ID E4PTG4_MYCLG Unreviewed; 209 AA.
AC E4PTG4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
DE EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|HAMAP-Rule:MF_00124};
GN Name=tdk {ECO:0000256|HAMAP-Rule:MF_00124,
GN ECO:0000313|EMBL:ADR23822.1};
GN OrderedLocusNames=MSB_A0193 {ECO:0000313|EMBL:ADR23822.1};
OS Mycoplasma leachii (strain DSM 21131 / NCTC 10133 / N29 / PG50).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=880447 {ECO:0000313|EMBL:ADR23822.1, ECO:0000313|Proteomes:UP000008712};
RN [1] {ECO:0000313|Proteomes:UP000008712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21131 / NCTC 10133 / N29 / PG50
RC {ECO:0000313|Proteomes:UP000008712};
RA Wise K., Calcutt M.J., Foecking M.F., Madupu R., DeBoy R.T., Roske K.,
RA Martin T.R., Hvinden M.L., Durkin A.S., Glass J., Methe B.A.;
RT "Genome sequence of Mycoplasma leachii PG50 MU clone A8.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR23822.1, ECO:0000313|Proteomes:UP000008712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21131 / NCTC 10133 / N29 / PG50
RC {ECO:0000313|Proteomes:UP000008712};
RX PubMed=22843585; DOI=10.1128/JB.00761-12;
RA Wise K.S., Calcutt M.J., Foecking M.F., Madupu R., Deboy R.T., Roske K.,
RA Hvinden M.L., Martin T.R., Durkin A.S., Glass J.I., Methe B.A.;
RT "Complete Genome Sequences of Mycoplasma leachii Strain PG50T and the
RT Pathogenic Mycoplasma mycoides subsp. mycoides Small Colony Biotype Strain
RT Gladysdale.";
RL J. Bacteriol. 194:4448-4449(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00124,
CC ECO:0000256|RuleBase:RU000544};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family.
CC {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|HAMAP-Rule:MF_00124,
CC ECO:0000256|RuleBase:RU004165}.
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DR EMBL; CP002108; ADR23822.1; -; Genomic_DNA.
DR RefSeq; WP_013447508.1; NC_014751.1.
DR AlphaFoldDB; E4PTG4; -.
DR KEGG; mlc:MSB_A0193; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_3_0_14; -.
DR OrthoDB; 9781579at2; -.
DR Proteomes; UP000008712; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00124; Thymidine_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00124}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00124};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, ECO:0000256|HAMAP-
KW Rule:MF_00124};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00124};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00124};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00124}; Zinc {ECO:0000256|HAMAP-Rule:MF_00124}.
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124,
FT ECO:0000256|PIRSR:PIRSR035805-1"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 103..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00124"
SQ SEQUENCE 209 AA; 23802 MW; 0E65FD0FECD1BB2B CRC64;
MIELDINEIE AYNSNKMGWI ELITGCMFAG KTEEFIRRLK VLSYAKKRVL AFKPSIDNRY
SVENIISHSG SKLDSYLVKS SDEIKQIVEK ENQIQQVDVI GIDEVQFFDE NVVDIVEQLA
DNGIIVIVNG LDKDFRGLPF KNVDKLLVKA EFVTKLRARC HLCGSFANRS QRIVNGQPAL
WNSPLILVDG KESYEARCRK CFIAPKKDV
//
