Gene Details


gene name: folA


locus tag k12ECK0049 Crenarchaeota Euryarchaeota Nanoarcheota Alphaproteobacteria Betaproteobacteria Gammaproteobacteria Deltaproteobacteria Epsilonproteobacteria Cyanobacteria Actinobacteridae Firmicutes Spirochaetes others Protist Microsporidia Fungi Metazoa Plantae
information on phylogenetic profile
locus tag mg1655b0048
locus tag w3110JW0047
gene name k12folA
locus namefolA
synonyms of locus nametmrA, tmr

scop id53597
superfamilyDihydrofolate reductases
pfam idPF00186
pfam domainDihydrofolate reductase
TIGRFAMno information

swissprot nameDYR_ECOLI
descriptionDihydrofolate reductase (EC 1.5.1.3).
seq length159
fastaseq

go idGO:0046656; GO:0009257; GO:0009257; GO:0009257
go termfolic acid biosynthesis; 10-formyltetrahydrofolate biosynthesis; 10-formylTHF biosyn; 10-formylTHF biosynth

gene product descriptiondihydrofolate reductase
comment gene product description
evidenceE
context
gene product descEnzyme
cell locationCytoplasmic
featuresCDS

functional category codeH
functional categoryCoenzyme transport and metabolism

reference #1Structure, dynamics, and catalytic function of dihydrofolate reductase.

Schnell J., Dyson H., Wright P.
reference #2Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites.

Frieden C. (Proc Natl Acad Sci U S A. 1990 Jun; 87(12):4413-6)
reference #3Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli.

Falzone C., Wright P., Benkovic S. (Biochemistry. 1991 Feb 26; 30(8):2184-91)
reference #415N NMR studies of the conformation of E. coli dihydrofolate reductase in complex with folate or methotrexate.

Huang F., Yang Q., Huang T. (FEBS Lett. 1991 Sep 9; 289(2):231-4)
reference #5Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding.

Bystroff C., Kraut J. (Biochemistry. 1991 Feb 26; 30(8):2227-39)
reference #6Crystal 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., Kraut J. (Biochemistry. 1990 Apr 3; 29(13):3263-77)
reference #7The amino-acid sequence of the dihydrofolate reductase of a trimethoprim-resistant strain of Escherichia coli.

Stone D., Phillips A., Burchall J. (Eur J Biochem. 1977 Feb; 72(3):613-24)
reference #8Dihydrofolate reductase: the amino acid sequence of the enzyme from a methotrexate-resistant mutant of Escherichia coli.

Bennett C., Rodkey J., Sondey J., Hirschmann R. (Biochemistry. 1978 Apr 4; 17(7):1328-37)
reference #9Massive overproduction of dihydrofolate reductase in bacteria as a response to the use of trimethoprim.

Flensburg J., Sköld O. (Eur J Biochem. 1987 Feb 2; 162(3):473-6)
reference #10Nucleotide sequence of the E coli gene coding for dihydrofolate reductase.

Smith D., Calvo J. (Nucleic Acids Res. 1980 May 24; 8(10):2255-74)
reference #11Crystal 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., Bolin J., Matthews D., Kraut J. (J Biol Chem. 1982 Nov 25; 257(22):13663-72)
reference #12Effect of a single amino acid substitution on Escherichia coli dihydrofolate reductase catalysis and ligand binding.

Baccanari D., Stone D., Kuyper L. (J Biol Chem. 1981 Feb 25; 256(4):1738-47)

phylogenetic profile
 
1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 94
89 82 85 102 86 92 86 86 92 70 1 1 124 1 1 107 114 115 114 139
139 137 123 121 1 1 1 123 53 143 142 144 136 136 135 119 119 139 141 1
84 1 1 1 1 1 1 97 75 1 116 1 1 1 1 1 135 136 133 140
127 142 102 102 1 101 82 101 78 117 122 122 122 122 62 57 1 58 1 77
55 61 108 85 107 104 107 104 107 94 94 89 97 97 62 63 65 65 65 1
54 92 112 144 153 151 139 274 333 328 328 172 117 117 174 147 172 268 139 131
136 328 328 328 150 300 333 165 177 171 139 117 119 124 127 277 277 277 1 91
96 71 71 71 70 66 63 1 114 1 1 95 108 1 1 1 1 1 1 1
62 60 78 60 50 61 1 87 108 69 65 66 60 62 70 86 57 72 58