ID   F6FHR5_MYCHI            Unreviewed;       201 AA.
AC   F6FHR5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Thymidine kinase {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
DE            EC=2.7.1.21 {ECO:0000256|ARBA:ARBA00012118, ECO:0000256|RuleBase:RU000544};
GN   Name=tdk {ECO:0000313|EMBL:AEG73829.1};
GN   OrderedLocusNames=MHF_1599 {ECO:0000313|EMBL:AEG73829.1};
OS   Mycoplasma haemofelis (strain Ohio2).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=859194 {ECO:0000313|EMBL:AEG73829.1, ECO:0000313|Proteomes:UP000007952};
RN   [1] {ECO:0000313|EMBL:AEG73829.1, ECO:0000313|Proteomes:UP000007952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ohio2 {ECO:0000313|EMBL:AEG73829.1,
RC   ECO:0000313|Proteomes:UP000007952};
RX   PubMed=21317328; DOI=10.1128/JB.00133-11;
RA   Messick J.B., Santos A.P., Guimaraes A.M.;
RT   "Complete genome sequences of two hemotropic Mycoplasmas, Mycoplasma
RT   haemofelis strain Ohio2 and Mycoplasma suis strain Illinois.";
RL   J. Bacteriol. 193:2068-2069(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ohio2;
RA   Santos A.P., Guimaraes A.M.S., SanMiguel P.J., Martin S.W., Messick J.B.;
RT   "The Genome of Mycoplasma haemofelis Strain Ohio2, a pathogenic hemoplasma
RT   of the cat.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU000544};
CC   -!- SIMILARITY: Belongs to the thymidine kinase family.
CC       {ECO:0000256|ARBA:ARBA00007587, ECO:0000256|RuleBase:RU004165}.
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DR   EMBL; CP002808; AEG73829.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6FHR5; -.
DR   STRING; 859194.MHF_1599; -.
DR   KEGG; mhf:MHF_1599; -.
DR   eggNOG; COG1435; Bacteria.
DR   HOGENOM; CLU_064400_3_0_14; -.
DR   BioCyc; MHAE859194:G1GR7-1601-MONOMER; -.
DR   Proteomes; UP000007952; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001267; Thymidine_kinase.
DR   PANTHER; PTHR11441; THYMIDINE KINASE; 1.
DR   PANTHER; PTHR11441:SF0; THYMIDINE KINASE, CYTOSOLIC; 1.
DR   Pfam; PF00265; TK; 1.
DR   PIRSF; PIRSF035805; TK_cell; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000544};
KW   DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW   ECO:0000256|RuleBase:RU000544};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000544};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000544};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000544}.
FT   ACT_SITE        94
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR035805-1"
SQ   SEQUENCE   201 AA;  22863 MW;  193A7B944D4E12A1 CRC64;
     MSYFVPQIFV ICGPMKSGKS KELLIQLDKL RYSKIPYLLF KPNIDSRDQS KITSRYLEGH
     SEEAIDIDVH SPKDILRHID VNSISFPYYI VIDEAQFFDK SLIDLVVYLN SMGVSFIISG
     LDLDAQSKPF GPIPDLLSLA THVSKLTAVC EQCYSIATRS HLRTHDPEFS KNNIKIGDGE
     LYEVLCLKCY YAKFAVDNIE Q
//