KITH_AYWBP
ID KITH_AYWBP Reviewed; 209 AA.
AC Q2NIM1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=AYWB_605;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(2006).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC65722.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000061; ABC65722.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041639918.1; NC_007716.1.
DR AlphaFoldDB; Q2NIM1; -.
DR SMR; Q2NIM1; -.
DR STRING; 322098.AYWB_605; -.
DR EnsemblBacteria; ABC65722; ABC65722; AYWB_605.
DR KEGG; ayw:AYWB_605; -.
DR eggNOG; COG1435; Bacteria.
DR HOGENOM; CLU_064400_3_0_14; -.
DR OrthoDB; 1279539at2; -.
DR Proteomes; UP000001934; 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: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 PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA synthesis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..209
FT /note="Thymidine kinase"
FT /id="PRO_0000242787"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 16..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT BINDING 90..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
SQ SEQUENCE 209 AA; 23466 MW; B82A9EA00E668308 CRC64;
MTQKEQGQGF IEVICGPMFA GKTESLIQRR NKALKLKKKI LSFKPRIDDR YSVKEEIVSH
NRNNIPAILI DKSKDILTFI TPEINVVIID ESQFLDNDII AIVDYLANCN IEVIISGLEL
DFCGKPFGPM PYLLAIADTV TKLTSICAIS GGKANRTQRL IEGKPAQSNE PVVLVGGKEY
HEPRCRKHHC LADIDKTKVN WKNFANQSK
