Thymidylate kinase (P00572)

Identification
NameThymidylate kinase
Synonyms
  • dTMP kinase
Gene NameCDC8
Enzyme Class
Biological Properties
General FunctionInvolved in thymidylate kinase activity
Specific FunctionCatalyzes the conversion of dTMP to dTDP
Cellular LocationNot Available
SMPDB Pathways
Pyrimidine metabolismPW002469 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Pyrimidine metabolismec00240 Map00240
SMPDB ReactionsNot Available
KEGG Reactions
Adenosine triphosphate + 5-Thymidylic acid ↔ dTDP + ADP
Metabolites
YMDB IDNameView
YMDB00109Adenosine triphosphateShow
YMDB001625-Thymidylic acidShow
YMDB00205dTDPShow
YMDB00914ADPShow
GO Classification
Component
Not Available
Function
transferase activity, transferring phosphorus-containing groups
phosphotransferase activity, phosphate group as acceptor
thymidylate kinase activity
binding
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
catalytic activity
ATP binding
transferase activity
Process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
pyrimidine nucleoside diphosphate biosynthetic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
pyrimidine deoxyribonucleoside diphosphate biosynthetic process
nucleobase, nucleoside and nucleotide metabolic process
dTDP biosynthetic process
nucleoside phosphate metabolic process
nucleotide metabolic process
pyrimidine nucleotide metabolic process
metabolic process
pyrimidine nucleotide biosynthetic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJR057W
Gene Sequence>651 bp ATGATGGGTCGTGGCAAATTAATACTGATAGAAGGATTGGATAGGACTGGTAAAACCACG CAATGTAATATTCTTTACAAAAAATTGCAACCAAACTGTAAACTATTGAAGTTCCCCGAA AGGTCTACCCGAATCGGAGGACTCATAAACGAATATTTGACGGATGATACTTTCCAATTA TCAGATCAGGCAATTCACCTCTTGTTTTCGGCAAATAGATGGGAAATAGTTGACAAGATA AAGAAAGATTTACTAGAAGGCAAGAACATTGTCATGGACAGATATGTTTATTCTGGAGTG GCATATTCTGCCGCTAAGGGGACAAATGGAATGGATTTGGATTGGTGCTTGCAACCCGAT GTAGGGTTGCTGAAACCGGATTTGACATTATTTTTAAGCACTCAAGATGTCGACAATAAC GCCGAAAAATCTGGATTTGGTGACGAAAGATACGAAACTGTTAAGTTTCAAGAAAAAGTG AAGCAAACTTTTATGAAGCTATTGGATAAAGAGATAAGGAAAGGCGATGAGTCAATCACG ATTGTAGACGTTACTAATAAGGGCATTCAGGAAGTTGAAGCGCTTATTTGGCAAATCGTT GAGCCTGTTTTGAGTACGCATATTGATCATGATAAATTTTCGTTCTTCTAG
Protein Properties
Pfam Domain Function
Protein Residues216
Protein Molecular Weight24687.19922
Protein Theoretical pI5.41
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Thymidylate kinase MMGRGKLILIEGLDRTGKTTQCNILYKKLQPNCKLLKFPERSTRIGGLINEYLTDDSFQL SDQAIHLLFSANRWEIVDKIKKDLLEGKNIVMDRYVYSGVAYSAAKGTNGMDLDWCLQPD VGLLKPDLTLFLSTQDVDNNAEKSGFGDERYETVKFQEKVKQTFMKLLDKEIRKGDESIT IVDVTNKGIQEVEALIWQIVEPVLSTHIDHDKFSFF
References
External Links
ResourceLink
Saccharomyces Genome Database CDC8
Uniprot IDP00572
Uniprot NameKTHY_YEAST
GenBank Gene IDK01783
Genebank Protein ID171204
PDB ID
3TMK
General Reference
  • Jong, A. Y., Kuo, C. L., Campbell, J. L. (1984). "The CDC8 gene of yeast encodes thymidylate kinase." J Biol Chem 259:11052-11059.6088527
  • Birkenmeyer, L. G., Hill, J. C., Dumas, L. B. (1984). "Saccharomyces cerevisiae CDC8 gene and its product." Mol Cell Biol 4:583-590.6371491
  • Huang, M. E., Manus, V., Chuat, J. C., Galibert, F. (1996). "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading frames and a gene cluster with a counterpart on chromosome XI." Yeast 12:869-875.8840504
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Lavie, A., Vetter, I. R., Konrad, M., Goody, R. S., Reinstein, J., Schlichting, I. (1997). "Structure of thymidylate kinase reveals the cause behind the limiting step in AZT activation." Nat Struct Biol 4:601-604.9253404
  • Lavie, A., Konrad, M., Brundiers, R., Goody, R. S., Schlichting, I., Reinstein, J. (1998). "Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation." Biochemistry 37:3677-3686.9521686