true 1986-07-21 2008-07-22 33 DYR_ECOLI Dihydrofolate reductase The amino-acid sequence of the dihydrofolate reductase of a trimethoprim-resistant strain of Escherichia coli. Stone D. Phillips A.W. Burchall J.J. 1977 Eur. J. Biochem. 72 613-624 PROTEIN SEQUENCE (ISOZYME 1) B [RT500] Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli. Bennett C.D. Rodkey J.A. Sondey J.M. Hirschmann R. doi:10.1021/bi00600a030 1978 Biochemistry 17 1328-1337 PROTEIN SEQUENCE B [MB1428] Nucleotide sequence of the E coli gene coding for dihydrofolate reductase. Smith D.R. Calvo J.M. doi:10.1093/nar/8.10.2255 1980 Nucleic Acids Res. 8 2255-2274 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding. Baccanari D.P. Stone D. Kuyper L. 1981 J. Biol. Chem. 256 1738-1747 PROTEIN SEQUENCE (ISOZYME 2) B [RT500] Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim. Flensburg J. Skoeld O. 1987 Eur. J. Biochem. 162 473-476 NUCLEOTIDE SEQUENCE [GENOMIC DNA] 1810 Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Yura T. Mori H. Nagai H. Nagata T. Ishihama A. Fujita N. Isono K. Mizobuchi K. Nakata A. doi:10.1093/nar/20.13.3305 1992 Nucleic Acids Res. 20 3305-3308 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 The complete genome sequence of Escherichia coli K-12. Blattner F.R. Plunkett G. III Bloch C.A. Perna N.T. Burland V. Riley M. Collado-Vides J. Glasner J.D. Rode C.K. Mayhew G.F. Gregor J. Davis N.W. Kirkpatrick H.A. Goeden M.A. Rose D.J. Mau B. Shao Y. doi:10.1126/science.277.5331.1453 1997 Science 277 1453-1474 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K. Morooka N. Yamamoto Y. Fujita K. Isono K. Choi S. Ohtsubo E. Baba T. Wanner B.L. Mori H. Horiuchi T. doi:10.1038/msb4100049 2006 Mol. Syst. Biol. 2 E1-E5 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 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. Filman D.J. Bolin J.T. Matthews D.A. Kraut J. 1982 J. Biol. Chem. 257 13663-13672 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate.NADP+ ternary complex. Substrate binding and a model for the transition state. Bystroff C. Oatley S.J. Kraut J. doi:10.1021/bi00465a018 1990 Biochemistry 29 3263-3277 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Bystroff C. Kraut J. doi:10.1021/bi00222a028 1991 Biochemistry 30 2227-2239 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) folA tmrA b0048 JW0047 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. Cofactor biosynthesis; tetrahydrofolate biosynthesis; tetrahydrofolate from dihydrofolate: step 1/1. The strain K12 sequence is shown. Strain B [RT500] is resistant to 500 micrograms per milliliter of trimethoprim. Strain B [MB1428] is methotrexate-resistant. The reaction catalyzed by this enzyme represents an essential step for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP. Belongs to the dihydrofolate reductase family. Contains 1 DHFR (dihydrofolate reductase) domain. Dihydrofolate reductase 1 159 DHFR 1 158 In strain: B[RT500] isozyme 2. R 28 28 In strain: 1810. G 30 30 In strain: B[MB1428]. K 154 154 In strain: 1810. Q 154 154 2 5 10 12 25 35 38 43 44 50 57 62 70 77 78 83 91 95 97 103 104 106 107 115 132 141 151 158 EMBL EMBL EMBL EMBL PIR A93704 RefSeq RefSeq PDB 2.45 A/B=1-159 PDB 2.20 A/B=1-159 PDB 1.90 A/B=1-159 PDB 1.80 A/B=1-159 PDB 1.90 A/B=1-159 PDB 1.96 A/B=1-159 PDB 2.60 A=1-159 PDB 2.30 A=1-159 PDB 1.90 A/B=1-159 PDB 1.90 A/B=1-159 PDB 1.85 A/B=1-159 PDB 1.96 A/B=1-159 PDB 1.90 A=1-159 PDB 1.90 A=1-159 PDB 1.60 A=1-159 PDB 1.80 A=1-159 PDB 1.80 A=1-159 PDB 1.55 A=1-159 PDB 2.10 A/B=1-159 PDB 2.30 A/B=1-159 PDB 1.90 A=1-159 PDB 2.60 A/B=1-159 PDB 2.60 A/B=1-159 PDB 1.80 A=1-159 PDB 2.00 A=1-159 PDB 2.40 A=1-159 PDB 2.00 A=1-159 PDB 1.80 A=1-159 PDB 2.20 A=1-159 PDB 2.20 A=1-159 PDB 2.30 A=1-159 PDB 2.00 A=1-159 PDB 2.30 A=1-159 PDB 2.80 A=1-159 PDB 1.90 A=1-159 PDB 2.50 A/B=1-159 PDB 2.68 A=1-159 PDB 2.13 A=1-159 PDB 1.90 A/B=1-159 PDB 1.90 A/B=1-159 PDB 2.20 A/B=1-159 PDB 1.90 A/B=1-159 PDB 1.70 A/B=1-159 PDB 2.30 A=1-159 PDB 2.40 A=1-159 PDB 2.50 A=1-159 PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum PDBsum IntAct SWISS-2DPAGE ECO2DBASE 6TH EDITION GeneID GenomeReviews b0048 GenomeReviews JW0047 KEGG KEGG EchoBASE EcoGene folA HOGENOM BioCyc BindingDB LinkHub InterPro DHFR InterPro DHFR_reg PANTHER DHFR 1 Pfam DHFR_1 1 PRINTS DHFR PROSITE DHFR_1 1 PROSITE DHFR_2 1 1986-07-21 1 17999 MISLIAALAV DRVIGMENAM PWNLPADLAW FKRNTLNKPV IMGRHTWESI GRPLPGRKNI ILSSQPGTDD RVTWVKSVDE AIAACGDVPE IMVIGGGRVY EQFLPKAQKL YLTHIDAEVE GDTHFPDYEP DDWESVFSEF HDADAQNSHS YCFEILERR