Dihydrofolate reductase
Details
- Name
- Dihydrofolate reductase
- Synonyms
- 1.5.1.3
- dhfR
- Gene Name
- folA
- Organism
- Lactobacillus casei
- Amino acid sequence
>lcl|BSEQ0011145|Dihydrofolate reductase MTAFLWAQDRDGLIGKDGHLPWHLPDDLHYFRAQTVGKIMVVGRRTYESFPKRPLPERTN VVLTHQEDYQAQGAVVVHDVAAVFAYAKQHPDQELVIAGGAQIFTAFKDDVDTLLVTRLA GSFEGDTKMIPLNWDDFTKVSSRTVEDTNPALTHTYEVWQKKA
- Number of residues
- 163
- Molecular Weight
- 18438.73
- Theoretical pI
- 6.14
- GO Classification
- Functionsdihydrofolate reductase activity / NADP bindingProcessesglycine biosynthetic process / nucleotide biosynthetic process / one-carbon metabolic process / response to antibiotic / response to methotrexate / tetrahydrofolate biosynthetic process
- General Function
- Nadp binding
- Specific Function
- Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
- Pfam Domain Function
- DHFR_1 (PF00186)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0003202|492 bp ATGACCGCATTTTTATGGGCACAGGATCGCGATGGCTTAATTGGCAAAGATGGTCATTTG CCATGGCATTTACCGGATGATTTACATTATTTCCGGGCGCAGACAGTTGGTAAGATCATG GTCGTTGGTCGGCGCACCTATGAAAGTTTTCCTAAACGTCCTTTACCTGAGCGAACCAAT GTTGTTTTGACCCATCAGGAAGACTATCAAGCGCAAGGTGCCGTGGTCGTGCATGATGTT GCGGCGGTTTTTGCTTATGCTAAGCAGCATCCCGATCAGGAACTGGTCATTGCTGGCGGT GCACAGATCTTTACGGCTTTTAAAGATGATGTCGATACGTTACTGGTAACACGTTTGGCT GGCAGTTTTGAAGGCGATACGAAAATGATTCCATTAAACTGGGATGATTTTACCAAAGTC TCCAGCCGCACCGTTGAAGATACCAATCCGGCGCTGACGCACACTTATGAGGTTTGGCAA AAGAAGGCTTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00381 UniProtKB Entry Name DYR_LACCA GenBank Protein ID 149540 GenBank Gene ID M10922 - General References
- Andrews J, Clore GM, Davies RW, Gronenborn AM, Gronenborn B, Kalderon D, Papadopoulos PC, Schafer S, Sims PF, Stancombe R: Nucleotide sequence of the dihydrofolate reductase gene of methotrexate-resistant Lactobacillus casei. Gene. 1985;35(1-2):217-22. [Article]
- Freisheim JH, Bitar KG, Reddy AV, Blankenship DT: Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei. Sequences of the cyanogen bromide peptides and complete sequences of the enzyme. J Biol Chem. 1978 Sep 25;253(18):6437-44. [Article]
- Batley KE, Morris HR: Dihydrofolate reductase from Lactobacillus casei: N-terminal sequence and comparison with the substrate binding region of other reductases. Biochem Biophys Res Commun. 1977 Apr 25;75(4):1010-4. [Article]
- Filman DJ, Bolin JT, Matthews DA, Kraut J: Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. II. Environment of bound NADPH and implications for catalysis. J Biol Chem. 1982 Nov 25;257(22):13663-72. [Article]
- Carr MD, Birdsall B, Frenkiel TA, Bauer CJ, Jimenez-Barbero J, Polshakov VI, McCormick JE, Roberts GC, Feeney J: Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution. Biochemistry. 1991 Jun 25;30(25):6330-41. [Article]
- Morgan WD, Birdsall B, Polshakov VI, Sali D, Kompis I, Feeney J: Solution structure of a brodimoprim analogue in its complex with Lactobacillus casei dihydrofolate reductase. Biochemistry. 1995 Sep 19;34(37):11690-702. [Article]
- Gargaro AR, Soteriou A, Frenkiel TA, Bauer CJ, Birdsall B, Polshakov VI, Barsukov IL, Roberts GC, Feeney J: The solution structure of the complex of Lactobacillus casei dihydrofolate reductase with methotrexate. J Mol Biol. 1998 Mar 20;277(1):119-34. [Article]
- Polshakov VI, Birdsall B, Frenkiel TA, Gargaro AR, Feeney J: Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate. Protein Sci. 1999 Mar;8(3):467-81. [Article]