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Database: UniProt
Entry: Q9PPP5
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Original site: Q9PPP5 
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   05-DEC-2018, entry version 102.
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
RT   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
RT   Ureaplasma urealyticum and investigations of possible drug targets for
RT   the enzyme.";
RL   FEBS J. 272:6365-6372(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + thymidine = ADP + dTMP + H(+);
CC         Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216;
CC         EC=2.7.1.21; 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
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   ProteinModelPortal; Q9PPP5; -.
DR   SMR; Q9PPP5; -.
DR   STRING; 273119.UU594; -.
DR   BindingDB; Q9PPP5; -.
DR   ChEMBL; CHEMBL1075130; -.
DR   DrugBank; DB02452; Thymidine-5'-Triphosphate.
DR   EnsemblBacteria; AAF31008; AAF31008; UU594.
DR   GeneID; 29672699; -.
DR   KEGG; uur:UU594; -.
DR   eggNOG; ENOG4107T8J; Bacteria.
DR   eggNOG; COG1435; LUCA.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; UPAR273119:G1FZ4-637-MONOMER; -.
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   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; Complete proteome; Cytoplasm;
KW   DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN         1    223       Thymidine kinase.
FT                                /FTId=PRO_0000175042.
FT   NP_BIND      19     26       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      96     99       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   REGION      178    182       Substrate binding.
FT   ACT_SITE     97     97       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       153    153       Zinc.
FT   METAL       156    156       Zinc.
FT   METAL       191    191       Zinc.
FT   METAL       194    194       Zinc.
FT   BINDING     128    128       Substrate; via amide nitrogen.
FT   BINDING     187    187       Substrate.
FT   STRAND       13     18       {ECO:0000244|PDB:2B8T}.
FT   HELIX        25     38       {ECO:0000244|PDB:2B8T}.
FT   STRAND       43     48       {ECO:0000244|PDB:2B8T}.
FT   HELIX        52     54       {ECO:0000244|PDB:2B8T}.
FT   STRAND       61     63       {ECO:0000244|PDB:2UZ3}.
FT   STRAND       65     67       {ECO:0000244|PDB:2UZ3}.
FT   STRAND       69     73       {ECO:0000244|PDB:2B8T}.
FT   HELIX        75     82       {ECO:0000244|PDB:2B8T}.
FT   STRAND       92     95       {ECO:0000244|PDB:2B8T}.
FT   HELIX        98    100       {ECO:0000244|PDB:2B8T}.
FT   HELIX       105    114       {ECO:0000244|PDB:2B8T}.
FT   STRAND      118    122       {ECO:0000244|PDB:2B8T}.
FT   STRAND      130    132       {ECO:0000244|PDB:2B8T}.
FT   HELIX       136    142       {ECO:0000244|PDB:2B8T}.
FT   STRAND      144    148       {ECO:0000244|PDB:2B8T}.
FT   TURN        154    156       {ECO:0000244|PDB:2B8T}.
FT   STRAND      158    160       {ECO:0000244|PDB:2B8T}.
FT   STRAND      162    167       {ECO:0000244|PDB:2B8T}.
FT   TURN        184    186       {ECO:0000244|PDB:2B8T}.
FT   STRAND      187    190       {ECO:0000244|PDB:2B8T}.
FT   HELIX       192    194       {ECO:0000244|PDB:2B8T}.
FT   HELIX       207    215       {ECO:0000244|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
//
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