ID   KITH_UREPA              Reviewed;         223 AA.
AC   Q9PPP5;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=UU594;
OS   Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=273119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700970;
RX   PubMed=11048724; DOI=10.1038/35037619;
RA   Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA   Cassell G.H.;
RT   "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL   Nature 407:757-762(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP   THYMIDINE, AND SUBUNIT.
RX   PubMed=15611477; DOI=10.1073/pnas.0406332102;
RA   Welin M., Kosinska U., Mikkelsen N.E., Carnrot C., Zhu C., Wang L.,
RA   Eriksson S., Munch-Petersen B., Eklund H.;
RT   "Structures of thymidine kinase 1 of human and mycoplasmic origin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17970-17975(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND
RP   THYMIDINE, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=16336273; DOI=10.1111/j.1742-4658.2005.05030.x;
RA   Kosinska U., Carnrot C., Eriksson S., Wang L., Eklund H.;
RT   "Structure of the substrate complex of thymidine kinase from Ureaplasma
RT   urealyticum and investigations of possible drug targets for the enzyme.";
RL   FEBS J. 272:6365-6372(2005).
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         ECO:0000269|PubMed:16336273};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00124,
CC       ECO:0000269|PubMed:15611477, ECO:0000269|PubMed:16336273}.
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; AF222894; AAF31008.1; -; Genomic_DNA.
DR   RefSeq; WP_006688765.1; NC_002162.1.
DR   PDB; 2B8T; X-ray; 2.00 A; A/B/C/D=1-223.
DR   PDB; 2UZ3; X-ray; 2.50 A; A/B/C/D=1-223.
DR   PDBsum; 2B8T; -.
DR   PDBsum; 2UZ3; -.
DR   AlphaFoldDB; Q9PPP5; -.
DR   SMR; Q9PPP5; -.
DR   STRING; 273119.UU594; -.
DR   BindingDB; Q9PPP5; -.
DR   ChEMBL; CHEMBL1075130; -.
DR   DrugBank; DB02452; Thymidine 5'-triphosphate.
DR   DrugCentral; Q9PPP5; -.
DR   EnsemblBacteria; AAF31008; AAF31008; UU594.
DR   GeneID; 29672699; -.
DR   KEGG; uur:UU594; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_3_0_14; -.
DR   OMA; ENTVNHK; -.
DR   BRENDA; 2.7.1.21; 9209.
DR   EvolutionaryTrace; Q9PPP5; -.
DR   PRO; PR:Q9PPP5; -.
DR   Proteomes; UP000000423; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; DNA synthesis; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..223
FT                   /note="Thymidine kinase"
FT                   /id="PRO_0000175042"
FT   ACT_SITE        97
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         96..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00124"
FT   BINDING         128
FT                   /ligand="substrate"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         178..182
FT                   /ligand="substrate"
FT   BINDING         187
FT                   /ligand="substrate"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   STRAND          13..18
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           25..38
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:2UZ3"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:2UZ3"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           75..82
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           136..142
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   TURN            154..156
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          158..160
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           192..194
FT                   /evidence="ECO:0007829|PDB:2B8T"
FT   HELIX           207..215
FT                   /evidence="ECO:0007829|PDB:2B8T"
SQ   SEQUENCE   223 AA;  25367 MW;  27F3061B26979A0B CRC64;
     MAKVNAFSKK IGWIELITGP MFAGKTAELI RRLHRLEYAD VKYLVFKPKI DTRSIRNIQS
     RTGTSLPSVE VESAPEILNY IMSNSFNDET KVIGIDEVQF FDDRICEVAN ILAENGFVVI
     ISGLDKNFKG EPFGPIAKLF TYADKITKLT AICNECGAEA THSLRKIDGK HADYNDDIVK
     IGCQEFYSAV CRHHHKVPNR PYLNSNSEEF IKFFKNKKRN KNI