Bifunctional dihydrofolate reductase-thymidylate synthase
Details
- Name
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Synonyms
- DHFR-TS
- Gene Name
- Not Available
- Organism
- Plasmodium falciparum (isolate K1 / Thailand)
- Amino acid sequence
>lcl|BSEQ0010391|Bifunctional dihydrofolate reductase-thymidylate synthase MMEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCNSLDMKYFRA VTTYVNESKYEKLKYKRCKYLNKETVDNVNDMPNSKKLQNVVVMGRTNWESIPKKFKPLS NRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFIIGGSVVYQEFLEKKLIK KIYFTRINSTYECDVFFPEINENEYQIISVSDVYTSNNTTLDFIIYKKTNNKMLNEQNCI KGEEKNNDMPLKNDDKDTCHMKKLTEFYKNVDKYKINYENDDDDEEEDDFVYFNFNKEKE EKNKNSIHPNDFQIYNSLKYKYHPEYQYLNIIYDIMMNGNKQSDRTGVGVLSKFGYIMKF DLSQYFPLLTTKKLFLRGIIEELLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFH REVNDLGPIYGFQWRHFGAEYTNMYDNYENKGVDQLKNIINLIKNDPTSRRILLCAWNVK DLDQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSIFTHMIAQVCNLQP AQFIHVLGNAHVYNNHIDSLKIQLNRIPYPFPTLKLNPDIKNIEDFTISDFTIQNYVHHE KISMDMAA
- Number of residues
- 608
- Molecular Weight
- 71816.775
- Theoretical pI
- 7.41
- GO Classification
- Functionsdihydrofolate reductase activity / thymidylate synthase activityProcessesdTMP biosynthetic process / glycine biosynthetic process / one-carbon metabolic process / tetrahydrofolate biosynthetic process
- General Function
- Thymidylate synthase activity
- Specific Function
- Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0001123|1827 bp ATGATGGAACAAGTCTGCGACGTTTTCGATATTTATGCCATATGTGCATGTTGTAAGGTT GAAAGCAAAAATGAGGGGAAAAAAAATGAGGTTTTTAATAACTACACATTTAGAGGTCTA GGAAATAAAGGAGTATTACCATGGAAATGTAATTCCCTAGATATGAAATATTTTCGTGCA GTTACAACATATGTGAATGAATCAAAATATGAAAAATTGAAATATAAGAGATGTAAATAT TTAAACAAAGAAACTGTGGATAATGTAAATGATATGCCTAATTCTAAAAAATTACAAAAT GTTGTAGTTATGGGAAGAACAAACTGGGAAAGCATTCCAAAAAAATTTAAACCTTTAAGC AATAGGATAAATGTTATATTGTCTAGAACCTTAAAAAAAGAAGATTTTGATGAAGATGTT TATATCATTAACAAAGTTGAAGATCTAATAGTTTTACTTGGGAAATTAAATTACTATAAA TGTTTTATTATAGGAGGTTCCGTTGTTTATCAAGAATTTTTAGAAAAGAAATTAATAAAA AAAATATATTTTACTAGAATAAATAGTACATATGAATGTGATGTATTTTTTCCAGAAATA AATGAAAATGAGTATCAAATTATTTCTGTTAGCGATGTATATACTAGTAACAATACAACA TTGGATTTTATCATTTATAAGAAAACGAATAATAAAATGTTAAATGAACAAAATTGTATA AAAGGAGAAGAAAAAAATAATGATATGCCTTTAAAGAATGATGACAAAGATACATGTCAT ATGAAAAAATTAACAGAATTTTACAAAAATGTAGACAAATATAAAATTAATTATGAAAAT GATGATGATGATGAAGAAGAAGATGATTTTGTTTATTTTAATTTTAATAAAGAAAAAGAA GAGAAAAATAAAAATTCTATACATCCAAATGATTTTCAAATATATAATAGCTTGAAATAT AAATATCATCCTGAATACCAATATTTAAATATTATTTATGATATTATGATGAATGGAAAT AAACAAAGTGATCGAACGGGAGTAGGTGTTTTAAGTAAATTCGGATATATTATGAAATTT GATTTAAGTCAATATTTCCCATTATTAACTACGAAGAAATTATTTTTAAGAGGAATTATT GAAGAATTGCTTTGGTTTATTAGAGGAGAAACAAATGGTAATACGTTGTTAAATAAGAAT GTAAGGATATGGGAAGCTAATGGTACTAGGGAATTTTTAGATAATAGAAAATTATTTCAT AGAGAAGTTAACGATTTAGGACCTATTTATGGTTTTCAATGGAGACATTTCGGTGCTGAA TATACAAATATGTATGATAATTATGAAAATAAAGGAGTGGATCAATTAAAAAATATAATA AATTTAATTAAAAATGATCCTACAAGTAGAAGAATTCTTTTGTGTGCATGGAATGTAAAA GATCTTGACCAAATGGCATTACCTCCTTGTCATATTTTATGTCAGTTTTATGTTTTCGAT GGGAAATTATCATGTATTATGTATCAAAGATCATGTGATTTAGGGCTAGGAGTACCTTTT AATATTGCTTCTTATTCTATTTTTACTCATATGATTGCACAAGTCTGTAATTTGCAACCT GCGCAGTTCATACACGTTTTAGGAAATGCACATGTTTATAATAATCACATTGATAGTTTA AAAATTCAACTTAACAGAATACCCTATCCATTCCCAACACTTAAATTAAATCCAGATATT AAAAATATTGAAGATTTTACAATTTCGGATTTTACAATACAAAATTATGTTCATCATGAA AAAATTTCAATGGATATGGCTGCTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P13922 UniProtKB Entry Name DRTS_PLAFK GenBank Protein ID 160260 GenBank Gene ID M22159 - General References
- Snewin VA, England SM, Sims PF, Hyde JE: Characterisation of the dihydrofolate reductase-thymidylate synthetase gene from human malaria parasites highly resistant to pyrimethamine. Gene. 1989 Mar 15;76(1):41-52. [Article]
- Zolg JW, Plitt JR, Chen GX, Palmer S: Point mutations in the dihydrofolate reductase-thymidylate synthase gene as the molecular basis for pyrimethamine resistance in Plasmodium falciparum. Mol Biochem Parasitol. 1989 Oct;36(3):253-62. [Article]
- Cowman AF, Morry MJ, Biggs BA, Cross GA, Foote SJ: Amino acid changes linked to pyrimethamine resistance in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum. Proc Natl Acad Sci U S A. 1988 Dec;85(23):9109-13. doi: 10.1073/pnas.85.23.9109. [Article]
- Bzik DJ, Li WB, Horii T, Inselburg J: Molecular cloning and sequence analysis of the Plasmodium falciparum dihydrofolate reductase-thymidylate synthase gene. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8360-4. [Article]
- Yuvaniyama J, Chitnumsub P, Kamchonwongpaisan S, Vanichtanankul J, Sirawaraporn W, Taylor P, Walkinshaw MD, Yuthavong Y: Insights into antifolate resistance from malarial DHFR-TS structures. Nat Struct Biol. 2003 May;10(5):357-65. [Article]
- Dasgupta T, Chitnumsub P, Kamchonwongpaisan S, Maneeruttanarungroj C, Nichols SE, Lyons TM, Tirado-Rives J, Jorgensen WL, Yuthavong Y, Anderson KS: Exploiting structural analysis, in silico screening, and serendipity to identify novel inhibitors of drug-resistant falciparum malaria. ACS Chem Biol. 2009 Jan 16;4(1):29-40. doi: 10.1021/cb8002804. [Article]