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Database: UniProt
Entry: P75070
LinkDB: P75070
Original site: P75070 
ID   KITH_MYCPN              Reviewed;         191 AA.
AC   P75070;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   05-DEC-2018, entry version 105.
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=MPN_044;
GN   ORFNames=MP110;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
RA   Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=11271496;
RX   DOI=10.1002/1522-2683(200011)21:17<3765::AID-ELPS3765>3.0.CO;2-6;
RA   Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M.,
RA   Herrmann R., Frank R.;
RT   "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL   Electrophoresis 21:3765-3780(2000).
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   -!- 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00124}.
DR   EMBL; U00089; AAB95758.1; -; Genomic_DNA.
DR   PIR; S73436; S73436.
DR   RefSeq; NP_109732.1; NC_000912.1.
DR   RefSeq; WP_010874401.1; NC_000912.1.
DR   ProteinModelPortal; P75070; -.
DR   SMR; P75070; -.
DR   IntAct; P75070; 1.
DR   EnsemblBacteria; AAB95758; AAB95758; MPN_044.
DR   GeneID; 877408; -.
DR   KEGG; mpn:MPN044; -.
DR   PATRIC; fig|272634.6.peg.44; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; MPNE272634:G1GJ3-61-MONOMER; -.
DR   BRENDA; 2.7.1.21; 3534.
DR   Proteomes; UP000000808; 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   PANTHER; PTHR11441; PTHR11441; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Zinc.
FT   CHAIN         1    191       Thymidine kinase.
FT                                /FTId=PRO_0000174999.
FT   NP_BIND      20     27       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      93     96       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     94     94       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       150    150       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       153    153       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       183    183       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       186    186       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   191 AA;  21500 MW;  C333AF82EFC21F15 CRC64;
     MSFSQVFHQS PRGWIEVICG PMFSGKTEEL LRKIKRWKLA KIPVIIFKPK IDTRQQHLVK
     SRNGHSDEAI EINSPLEIYD YLTKDRFDVV AIDEAQFFSS EIVEVVKSLN DLGINVIVSG
     LDTDFRAEPF GSIPQLLAIA DKICKLDAVC NVCGQLAQRT QRIVSKSNET VLIGDIEAYE
     PRCKLHQPSA G
//
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