folA dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: folA
Official Full Name: dihydrofolate reductase
Primary source: ECOCYC:EG10326
Locus tag: b0048
See related: ASAP:ABE-0000164
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: ECK0049; tmr; tmrA
Summary: folA is an essential gene. [More information is available at EcoGene: EG10326]. Dihydrofolate reductase catalyzes the reduction of dihydrofolate to tetrahydrofolate, which is an important intermediate in the biosynthesis of proteins and nucleic acids . [More information is available at EcoCyc: EG10326].
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Genomic context

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Sequence:: NC_000913.3 (49823..50302)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Solution Ionic Strength Can Modulate Functional Loop Conformations in E. coli Dihydrofolate Reductase.
Title: Solution Ionic Strength Can Modulate Functional Loop Conformations in E. coli Dihydrofolate Reductase.
DHFR Mutants Modulate Their Synchronized Dynamics with the Substrate by Shifting Hydrogen Bond Occupancies.
Title: DHFR Mutants Modulate Their Synchronized Dynamics with the Substrate by Shifting Hydrogen Bond Occupancies.
Mutational and computational analyses in EcDHFR and in DHFR enzymes from Staphylococcus aureus and Mycobacterium tuberculosis demonstrate that natural variation at this site and its interacting hydrophobic residues modulates trimethoprim resistance in other bacterial DHFRs as well
Title: Trade-offs with stability modulate innate and mutationally acquired drug resistance in bacterial dihydrofolate reductase enzymes.
NADP+ not only binds to the native form but also a partially unfolded form of dihydrofolate reductase.
Title: Ligand binding to a high-energy partially unfolded protein.
Quantum mechanics/molecular dynamics simulations reveal that the M20 loop conformational dynamics of dihydrofolate reductase (DHFR) is severely restricted at the transition state of the hydride transfer as a result of the M42W/G121V double mutation.
Title: Connecting protein conformational dynamics with catalytic function as illustrated in dihydrofolate reductase.
Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle
Title: Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle.
The data presented here provide a glimpse into the evolutionary trajectory of functional DHFR through its protein sequence space that lead to the diverged binding and catalytic properties of the E. coli and human enzymes.
Title: Functional significance of evolving protein sequence in dihydrofolate reductase from bacteria to humans.
Present a general kinetic framework that can be used to study conformation changes, apply this framework to E. coli DHFR and find the conformational change occurs predominantly prior to unbinding.
Title: Conformational selection and induced changes along the catalytic cycle of Escherichia coli dihydrofolate reductase.
Protein interface remodeling in a chemically induced protein dimer.
Title: Protein interface remodeling in a chemically induced protein dimer.
Dihydrofolate reductase is bound to endogenous tetrahydrofolate
Title: Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables NADP binding	IBA Inferred from Biological aspect of Ancestor more info
enables NADP binding	IEA Inferred from Electronic Annotation more info
enables NADP+ binding	IDA Inferred from Direct Assay more info	PubMed
enables NADP+ binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables NADPH binding	IDA Inferred from Direct Assay more info	PubMed
enables NADPH binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables dihydrofolate reductase activity	IBA Inferred from Biological aspect of Ancestor more info
enables dihydrofolate reductase activity	IDA Inferred from Direct Assay more info	PubMed
enables dihydrofolate reductase activity	IEA Inferred from Electronic Annotation more info
enables dihydrofolate reductase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables dihydrofolic acid binding	IDA Inferred from Direct Assay more info	PubMed
enables folic acid binding	IDA Inferred from Direct Assay more info	PubMed
enables folic acid binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables methotrexate binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
acts_upstream_of_or_within 10-formyltetrahydrofolate biosynthetic process	EXP Inferred from Experiment more info	PubMed
involved_in dihydrofolate metabolic process	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within folic acid biosynthetic process	EXP Inferred from Experiment more info	PubMed
involved_in folic acid metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in one-carbon metabolic process	IEA Inferred from Electronic Annotation more info
involved_in response to antibiotic	IEA Inferred from Electronic Annotation more info
involved_in response to methotrexate	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within response to xenobiotic stimulus	IDA Inferred from Direct Assay more info	PubMed
involved_in tetrahydrofolate biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in tetrahydrofolate biosynthetic process	IEA Inferred from Electronic Annotation more info