GenomeNet

Database: UniProt
Entry: Q5ZZT0
LinkDB: Q5ZZT0
Original site: Q5ZZT0 
ID   KITH_MYCH2              Reviewed;         184 AA.
AC   Q5ZZT0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   16-JAN-2019, 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=mhp627;
OS   Mycoplasma hyopneumoniae (strain 232).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=295358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232;
RX   PubMed=15489423; DOI=10.1128/JB.186.21.7123-7133.2004;
RA   Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA   Mahairas G.G.;
RT   "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent
RT   of swine mycoplasmosis.";
RL   J. Bacteriol. 186:7123-7133(2004).
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; AE017332; AAV27647.1; -; Genomic_DNA.
DR   RefSeq; WP_011206458.1; NC_006360.1.
DR   ProteinModelPortal; Q5ZZT0; -.
DR   SMR; Q5ZZT0; -.
DR   PRIDE; Q5ZZT0; -.
DR   EnsemblBacteria; AAV27647; AAV27647; mhp627.
DR   KEGG; mhy:mhp627; -.
DR   HOGENOM; HOG000076390; -.
DR   KO; K00857; -.
DR   OMA; KEQFGWI; -.
DR   BioCyc; MHYO295358:G1G11-652-MONOMER; -.
DR   Proteomes; UP000006822; 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   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA synthesis; Kinase;
KW   Metal-binding; Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    184       Thymidine kinase.
FT                                /FTId=PRO_0000174995.
FT   NP_BIND      15     22       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   NP_BIND      89     92       ATP. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   ACT_SITE     90     90       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00124}.
FT   METAL       146    146       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       149    149       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       178    178       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
FT   METAL       181    181       Zinc. {ECO:0000255|HAMAP-Rule:MF_00124}.
SQ   SEQUENCE   184 AA;  20911 MW;  D9F531A695AC2BED CRC64;
     MYKKFFDGVI EVITGPMFSG KSDELIKRIK ILTYADIKTL VIKPSVDYRF SQCEIVSRSG
     LKIPTFLART TQEIRDLFTR DNYQAIAIDE IQFFDEEIVT FLEQIADKGI RVIVSGLDQD
     FRRKPFGSLP NLMAIAENVT KLQAVCSLCK RAATTTARKV LNEAQTLIGD QDEYEARCRA
     CHSL
//
DBGET integrated database retrieval system