KTHY_DICDI
ID KTHY_DICDI Reviewed; 222 AA.
AC Q54GN2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9 {ECO:0000250|UniProtKB:P23919};
DE AltName: Full=dTMP kinase;
GN Name=dtymk; Synonyms=tmkA; ORFNames=DDB_G0290033;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of thymidine monophosphate
CC (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the
CC DNA building block dTTP, with ATP as the preferred phosphoryl donor in
CC the presence of Mg(2+). {ECO:0000250|UniProtKB:P23919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528,
CC ChEBI:CHEBI:456216; EC=2.7.4.9;
CC Evidence={ECO:0000250|UniProtKB:P23919};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P23919};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000250|UniProtKB:P23919}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23919}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000151; EAL62422.1; -; Genomic_DNA.
DR RefSeq; XP_635930.1; XM_630838.1.
DR AlphaFoldDB; Q54GN2; -.
DR SMR; Q54GN2; -.
DR STRING; 44689.DDB0230101; -.
DR PaxDb; Q54GN2; -.
DR EnsemblProtists; EAL62422; EAL62422; DDB_G0290033.
DR GeneID; 8627451; -.
DR KEGG; ddi:DDB_G0290033; -.
DR dictyBase; DDB_G0290033; dtymk.
DR eggNOG; KOG3327; Eukaryota.
DR HOGENOM; CLU_049131_3_2_1; -.
DR InParanoid; Q54GN2; -.
DR OMA; CYAPERG; -.
DR PhylomeDB; Q54GN2; -.
DR UniPathway; UPA00575; -.
DR PRO; PR:Q54GN2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0004798; F:thymidylate kinase activity; ISS:dictyBase.
DR GO; GO:0009041; F:uridylate kinase activity; ISS:dictyBase.
DR GO; GO:0006233; P:dTDP biosynthetic process; ISS:dictyBase.
DR GO; GO:0006235; P:dTTP biosynthetic process; ISS:dictyBase.
DR GO; GO:0006227; P:dUDP biosynthetic process; ISS:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00165; Thymidylate_kinase; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039430; Thymidylate_kin-like_dom.
DR InterPro; IPR018095; Thymidylate_kin_CS.
DR InterPro; IPR018094; Thymidylate_kinase.
DR Pfam; PF02223; Thymidylate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00041; DTMP_kinase; 1.
DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Thymidylate kinase"
FT /id="PRO_0000328101"
FT REGION 146..170
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P23919"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23919"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P23919"
SQ SEQUENCE 222 AA; 25582 MW; AFB7D8A5C0858C9D CRC64;
MINTKKEEGE EEKTMIKRGL FILFEGVDRV GKSTQVQSLT NHISNVQKLP TKSLRFPDRT
TPIGQIINQY LQNATNMDDR ALHLLFSSNR WEARDSILEL LNNGTNIVVD RYSYSGVAYS
AAKGIDFDWC YACEKGLPKP DLIFYLSMSS EDATKRGEYG GERYEKLEFQ KKIKQIYEEK
LVDDQWKIIN ANRSIDEISN EISSIFDSEF KKIQLTSIAK LE
