Dihydrofolate reductase
Details
- Name
- Dihydrofolate reductase
- Synonyms
- 1.5.1.3
- dfrA
- Gene Name
- folA
- Organism
- Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
- Amino acid sequence
>lcl|BSEQ0051130|Dihydrofolate reductase MTMVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMGRRTWDSLPAKVRPLP GRRNVVLSRQADFMASGAEVVGSLEEALTSPETWVIGGGQVYALALPYATRCEVTEVDIG LPREAGDALAPVLDETWRGETGEWRFSRSGLRYRLYSYHRS
- Number of residues
- 161
- Molecular Weight
- 17872.18
- Theoretical pI
- Not Available
- GO Classification
- Functionsdihydrofolate reductase activity / NADP+ bindingProcessesglycine biosynthetic process / nucleotide biosynthetic process / one-carbon metabolic process / tetrahydrofolate biosynthetic process
- General Function
- Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
- Specific Function
- Dihydrofolate reductase activity
- Pfam Domain Function
- DHFR_1 (PF00186)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0051131|Dihydrofolate reductase (folA) ATGGTGGGGCTGATCTGGGCTCAAGCGACATCGGGTGTCATCGGCCGCGGCGGCGACATC CCCTGGCGCTTGCCCGAGGACCAGGCGCATTTCCGGGAGATCACCATGGGGCACACGATC GTGATGGGCCGGCGCACATGGGATTCGCTGCCGGCTAAAGTCCGGCCGCTGCCCGGCCGG CGAAATGTCGTACTGAGCCGCCAAGCTGACTTTATGGCCAGCGGGGCTGAGGTTGTCGGT TCACTCGAGGAGGCGCTGACCAGCCCGGAGACGTGGGTGATCGGAGGCGGACAAGTCTAT GCGCTGGCGCTGCCGTACGCGACCAGATGTGAGGTTACCGAGGTCGACATCGGCCTGCCG CGCGAAGCCGGTGACGCGCTGGCCCCCGTGCTGGACGAGACATGGCGGGGCGAGACGGGG GAGTGGCGCTTCAGCCGGTCCGGGTTGCGGTACCGGTTGTACAGCTACCACCGCTCATGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P9WNX1 UniProtKB Entry Name DYR_MYCTU - General References
- Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
- Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
- Li R, Sirawaraporn R, Chitnumsub P, Sirawaraporn W, Wooden J, Athappilly F, Turley S, Hol WG: Three-dimensional structure of M. tuberculosis dihydrofolate reductase reveals opportunities for the design of novel tuberculosis drugs. J Mol Biol. 2000 Jan 14;295(2):307-23. [Article]
- Argyrou A, Vetting MW, Aladegbami B, Blanchard JS: Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid. Nat Struct Mol Biol. 2006 May;13(5):408-13. Epub 2006 Apr 30. [Article]