KTHY_SCHPO
ID KTHY_SCHPO Reviewed; 210 AA.
AC P36590; O74528;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Thymidylate kinase;
DE EC=2.7.4.9 {ECO:0000269|PubMed:1327149};
DE AltName: Full=dTMP kinase;
GN Name=tmp1; Synonyms=tmp; ORFNames=SPCC70.07c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=1327149; DOI=10.1016/0167-4781(92)90018-u;
RA Abaigar L.T., Yeh Y.I., Jong A.Y.;
RT "Functional and structural conservation of Schizosaccharomyces pombe dTMP
RT kinase gene.";
RL Biochim. Biophys. Acta 1132:222-224(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the conversion of dTMP to dTDP.
CC {ECO:0000269|PubMed:1327149}.
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:0000269|PubMed:1327149};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13518;
CC Evidence={ECO:0000305|PubMed:1327149};
CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis.
CC {ECO:0000305|PubMed:1327149}.
CC -!- SIMILARITY: Belongs to the thymidylate kinase family. {ECO:0000305}.
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DR EMBL; X65868; CAA46698.1; -; mRNA.
DR EMBL; CU329672; CAA19357.1; -; Genomic_DNA.
DR PIR; S28955; S28955.
DR PIR; T41553; T41553.
DR RefSeq; NP_588542.1; NM_001023529.2.
DR AlphaFoldDB; P36590; -.
DR SMR; P36590; -.
DR BioGRID; 275291; 1.
DR STRING; 4896.SPCC70.07c.1; -.
DR MaxQB; P36590; -.
DR PaxDb; P36590; -.
DR EnsemblFungi; SPCC70.07c.1; SPCC70.07c.1:pep; SPCC70.07c.
DR PomBase; SPCC70.07c; tmp1.
DR VEuPathDB; FungiDB:SPCC70.07c; -.
DR eggNOG; KOG3327; Eukaryota.
DR HOGENOM; CLU_049131_3_1_1; -.
DR InParanoid; P36590; -.
DR OMA; MCLFLRI; -.
DR PhylomeDB; P36590; -.
DR UniPathway; UPA00575; -.
DR PRO; PR:P36590; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IGI:PomBase.
DR GO; GO:0009041; F:uridylate kinase activity; IGI:PomBase.
DR GO; GO:0006233; P:dTDP biosynthetic process; IGI:PomBase.
DR GO; GO:0006235; P:dTTP biosynthetic process; IGI:PomBase.
DR GO; GO:0006227; P:dUDP biosynthetic process; IGI:PomBase.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide biosynthesis; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="Thymidylate kinase"
FT /id="PRO_0000155213"
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 33..39
FT /note="SQHEKAE -> LNMKRLK (in Ref. 1; CAA46698)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="K -> T (in Ref. 1; CAA46698)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..93
FT /note="TIQYIYEQINKGVT -> PSIYYRANQQRCN (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="P -> T (in Ref. 1; CAA46698)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="F -> L (in Ref. 1; CAA46698)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> YA (in Ref. 1; CAA46698)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="H -> D (in Ref. 1; CAA46698)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 24250 MW; 4266144AEDAB68C0 CRC64;
MSKQNRGRLI VIEGLDRSGK STQCQLLVDK LISQHEKAEL FKFPDRTTAI GKKIDDYLKE
SVQLNDQVIH LLFSANRWET IQYIYEQINK GVTCILDRYA FSGIAFSAAK GLDWEWCKSP
DRGLPRPDLV IFLNVDPRIA ATRGQYGEER YEKIEMQEKV LKNFQRLQKE FREEGLEFIT
LDASSSLEDV HSQIVDLVSN VNIHETLDVL
