P0A8V6 · FADR_ECOLI
- ProteinFatty acid metabolism regulator protein
- GenefadR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids239 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Multifunctional regulator of fatty acid metabolism (PubMed:11859088, PubMed:1569108, PubMed:19854834, PubMed:21276098, PubMed:8446033, PubMed:9388199).
Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE (PubMed:9388199).
Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes (PubMed:9388199).
Represses transcription of at least eight genes required for fatty acid transport and beta-oxidation including fadA, fadB, fadD, fadL and fadE (PubMed:9388199).
Activates transcription of at least three genes required for unsaturated fatty acid biosynthesis: fabA, fabB and iclR, the gene encoding the transcriptional regulator of the aceBAK operon encoding the glyoxylate shunt enzymes (PubMed:9388199).
Activity regulation
Binding of FadR to DNA is specifically inhibited by long chain acyl-CoA compounds, but not by long chain fatty acids (PubMed:1569108).
Long chain acyl-CoA binds directly to the protein preventing it from binding DNA, which derepresses genes for beta-oxidation and prevents activation of genes for unsaturated fatty acid biosynthesis (PubMed:19854834, PubMed:7836365).
Long chain acyl-CoA binds directly to the protein preventing it from binding DNA, which derepresses genes for beta-oxidation and prevents activation of genes for unsaturated fatty acid biosynthesis (PubMed:19854834, PubMed:7836365).
Features
Showing features for dna binding, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
DNA binding | 34-69 | H-T-H motif | |||
Binding site | 99 | CoA (UniProtKB | ChEBI) | |||
Binding site | 103-107 | CoA (UniProtKB | ChEBI) | |||
Binding site | 213 | CoA (UniProtKB | ChEBI) | |||
Binding site | 219 | CoA (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | DNA binding | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | fatty-acyl-CoA binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | fatty acid metabolic process | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of fatty acid biosynthetic process | |
Biological Process | regulation of fatty acid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFatty acid metabolism regulator protein
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0A8V6
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Decreased transcription of fabA, low to no change in levels of fabB (PubMed:11859088, PubMed:21276098).
Up-regulation of genes involved in beta-oxidation (fatty acid degradation, at least fadA, fadB, fadE, fadH, fadI and fadJ) (PubMed:11859088).
Increased levels of fatty acids; double fadR-fabR deletions have the same phenotype, suggesting a functional fadR gene is required for fabR function (PubMed:11859088).
Up-regulation of genes involved in beta-oxidation (fatty acid degradation, at least fadA, fadB, fadE, fadH, fadI and fadJ) (PubMed:11859088).
Increased levels of fatty acids; double fadR-fabR deletions have the same phenotype, suggesting a functional fadR gene is required for fabR function (PubMed:11859088).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 9 | Dominant negative to wild-type, decreased DNA-binding. | |||
Mutagenesis | 35 | Dominant negative to wild-type, decreased DNA-binding. | |||
Mutagenesis | 49 | Dominant negative to wild-type. | |||
Mutagenesis | 65 | Dominant negative to wild-type, decreased DNA-binding. | |||
Mutagenesis | 66 | Dominant negative to wild-type, decreased DNA-binding. | |||
Mutagenesis | 67 | Dominant negative to wild-type, decreased DNA-binding. | |||
Mutagenesis | 215 | Loss of FadR repression. | |||
Mutagenesis | 216 | Super-repressor, non-inducible phenotype, cells cannot use long chain fatty acids as carbon source. | |||
Mutagenesis | 218 | Reduced ability to repress. | |||
Mutagenesis | 219 | Reduced ability to repress. | |||
Mutagenesis | 219 | Super-repressor, non-inducible phenotype, cells cannot use long chain fatty acids as carbon source. Protein has 10-fold decreased affinity for C18:1-CoA, can still bind fabADNA and alter transcription. | |||
Mutagenesis | 220 | Loss of FadR repression. | |||
Mutagenesis | 223 | Super-repressor, non-inducible phenotype, cells cannot use long chain fatty acids as carbon source. | |||
Mutagenesis | 227 | Loss of FadR repression. | |||
Mutagenesis | 228 | Reduced ability to repress. | |||
Mutagenesis | 229 | Loss of FadR repression. | |||
Chemistry
Expression
Induction
By growth in the presence of long chain fatty acids (C14-C18) (PubMed:7836365).
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 6-74 | HTH gntR-type | |||
Region | 215-230 | Binds acyl-CoA | |||
Domain
The N-terminus binds DNA, the C-terminus (residues 83-239) is responsible for dimerization (PubMed:9388199).
The C-terminal domain binds acyl-CoA (PubMed:11296236, PubMed:7836365).
The C-terminal domain binds acyl-CoA (PubMed:11296236, PubMed:7836365).
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length239
- Mass (Da)26,969
- Last updated2007-01-23 v2
- MD5 Checksum48835AF5C3E5C8F2B7ABA321DFBE6AFF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X08087 EMBL· GenBank· DDBJ | CAA30881.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC74271.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAA36042.1 EMBL· GenBank· DDBJ | Genomic DNA |