KITH_MYCGA
ID KITH_MYCGA Reviewed; 224 AA.
AC Q8RLE0;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Thymidine kinase {ECO:0000255|HAMAP-Rule:MF_00124};
DE EC=2.7.1.21 {ECO:0000255|HAMAP-Rule:MF_00124};
GN Name=tdk {ECO:0000255|HAMAP-Rule:MF_00124}; OrderedLocusNames=MYCGA6630;
GN ORFNames=MGA_0502;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RA Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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:0000255|HAMAP-Rule:MF_00124};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00124}.
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00124}.
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DR EMBL; AY081866; AAL91131.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP57013.2; -; Genomic_DNA.
DR RefSeq; WP_011113924.1; NC_004829.2.
DR AlphaFoldDB; Q8RLE0; -.
DR SMR; Q8RLE0; -.
DR GeneID; 57203972; -.
DR KEGG; mga:MGA_0502; -.
DR HOGENOM; CLU_064400_3_0_14; -.
DR OMA; ENTVNHK; -.
DR OrthoDB; 1279539at2; -.
DR Proteomes; UP000001418; 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; 3.40.50.300; -; 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; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..224
FT /note="Thymidine kinase"
FT /id="PRO_0000174993"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 19..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 93..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT CONFLICT 10
FT /note="T -> S (in Ref. 1; AAL91131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 25259 MW; 8674C04BE5741FCC CRC64;
MAKKNAMTTT NGWIEAICGP MFAGKTDELI RKIKRYEYAD VKSLVFSPAT DTRSAQEIIN
SRDGRRIGSI KIKKAFEIYD YVLLHKPQLV GIDEVQFFDD SIVEVIQTLA DNQINVIVAG
LDRDFRGEPF GPIPKILGIA ESVIRLTAIC SECGAEASRS QRLIDNQPAD YNCETILIGD
TESYAPRCRH HHKVPNRPIN DQTKNFKRAL KNNFDKIVEQ SSKD