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Protein

Fatty acid metabolism regulator protein

Gene

fadR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional regulator of fatty acid metabolism (PubMed:1569108, PubMed:8446033, PubMed:9388199, PubMed:11859088, PubMed:19854834, PubMed:21276098). 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).7 Publications

Enzyme regulationi

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:7836365, PubMed:19854834).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei99Coenzyme A; via carbonyl oxygen1 Publication1
Binding sitei213Coenzyme A1 Publication1
Binding sitei219Coenzyme A1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi34 – 69H-T-H motif2 PublicationsAdd BLAST36

GO - Molecular functioni

  • DNA binding Source: UniProtKB-HAMAP
  • fatty-acyl-CoA binding Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

  • fatty acid oxidation Source: EcoCyc
  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • positive regulation of fatty acid biosynthetic process Source: CACAO
  • positive regulation of transcription, DNA-templated Source: EcoCyc
  • regulation of fatty acid metabolic process Source: CACAO
  • transcription, DNA-templated Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD01520.
ECOL316407:JW1176-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid metabolism regulator proteinUniRule annotation
Gene namesi
Name:fadRUniRule annotation
Synonyms:oleR, thdB
Ordered Locus Names:b1187, JW1176
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10281. fadR.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9A → V: Dominant negative to wild-type, decreased DNA-binding. 1 Publication1
Mutagenesisi35R → C: Dominant negative to wild-type, decreased DNA-binding. 1 Publication1
Mutagenesisi49R → A: Dominant negative to wild-type. 1 Publication1
Mutagenesisi65H → Y: Dominant negative to wild-type, decreased DNA-binding. 1 Publication1
Mutagenesisi66G → D: Dominant negative to wild-type, decreased DNA-binding. 1 Publication1
Mutagenesisi67K → S: Dominant negative to wild-type, decreased DNA-binding. 1 Publication1
Mutagenesisi215Y → A: Loss of FadR repression. 1 Publication1
Mutagenesisi216G → A: Super-repressor, non-inducible phenotype, cells cannot use long chain fatty acids as carbon source. 1 Publication1
Mutagenesisi218E → A: Reduced ability to repress. 1 Publication1
Mutagenesisi219S → A: Reduced ability to repress. 1 Publication1
Mutagenesisi219S → N: 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 fabA DNA and alter transcription. 1 Publication1
Mutagenesisi220G → A: Loss of FadR repression. 1 Publication1
Mutagenesisi223W → A: Super-repressor, non-inducible phenotype, cells cannot use long chain fatty acids as carbon source. 1 Publication1
Mutagenesisi227Q → A: Loss of FadR repression. 1 Publication1
Mutagenesisi228K → A: Reduced ability to repress. 1 Publication1
Mutagenesisi229N → A: Loss of FadR repression. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000506262 – 239Fatty acid metabolism regulator proteinAdd BLAST238

Proteomic databases

PaxDbiP0A8V6.
PRIDEiP0A8V6.

Expressioni

Inductioni

By growth in the presence of long chain fatty acids (C14-C18) (PubMed:7836365).1 Publication

Interactioni

Subunit structurei

Homodimer (PubMed:9388199, PubMed:11013219, PubMed:11296236, PubMed:11279025). Binding of acyl-CoA alters conformation of the dimer, separating the DNA-binding regions and disrupting DNA-binding (PubMed:11296236).4 Publications

Protein-protein interaction databases

BioGridi4260102. 14 interactors.
DIPiDIP-9564N.
IntActiP0A8V6. 2 interactors.
MINTiMINT-1264978.
STRINGi511145.b1187.

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 21Combined sources14
Helixi34 – 41Combined sources8
Helixi45 – 57Combined sources13
Beta strandi60 – 64Combined sources5
Beta strandi67 – 71Combined sources5
Helixi74 – 77Combined sources4
Helixi80 – 82Combined sources3
Helixi83 – 89Combined sources7
Helixi91 – 93Combined sources3
Helixi94 – 119Combined sources26
Helixi121 – 129Combined sources9
Turni130 – 133Combined sources4
Helixi138 – 155Combined sources18
Helixi159 – 179Combined sources21
Helixi183 – 202Combined sources20
Helixi206 – 227Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E2XX-ray2.00A1-239[»]
1H9GX-ray2.10A1-239[»]
1H9TX-ray3.25A/B1-239[»]
1HW1X-ray1.50A/B1-239[»]
1HW2X-ray3.25A/B1-239[»]
ProteinModelPortaliP0A8V6.
SMRiP0A8V6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A8V6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 74HTH gntR-typeUniRule annotationAdd BLAST69

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 107Coenzyme A binding1 Publication5
Regioni215 – 230Binds acyl-CoA1 PublicationAdd BLAST16

Domaini

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:7836365, PubMed:11296236).3 Publications

Sequence similaritiesi

Contains 1 HTH gntR-type DNA-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C05. Bacteria.
COG2186. LUCA.
HOGENOMiHOG000278467.
InParanoidiP0A8V6.
KOiK03603.
OMAiIWETSGL.
PhylomeDBiP0A8V6.

Family and domain databases

CDDicd07377. WHTH_GntR. 1 hit.
Gene3Di1.10.10.10. 1 hit.
1.20.120.530. 1 hit.
HAMAPiMF_00696. HTH_FadR. 1 hit.
InterProiIPR014178. FA-response_TF_FadR.
IPR028374. FadR_C.
IPR008920. TF_FadR/GntR_C.
IPR000524. Tscrpt_reg_HTH_GntR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF07840. FadR_C. 1 hit.
PF00392. GntR. 1 hit.
[Graphical view]
PRINTSiPR00035. HTHGNTR.
SMARTiSM00345. HTH_GNTR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48008. SSF48008. 1 hit.
TIGRFAMsiTIGR02812. fadR_gamma. 1 hit.
PROSITEiPS50949. HTH_GNTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A8V6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIKAQSPAG FAEEYIIESI WNNRFPPGTI LPAERELSEL IGVTRTTLRE
60 70 80 90 100
VLQRLARDGW LTIQHGKPTK VNNFWETSGL NILETLARLD HESVPQLIDN
110 120 130 140 150
LLSVRTNIST IFIRTAFRQH PDKAQEVLAT ANEVADHADA FAELDYNIFR
160 170 180 190 200
GLAFASGNPI YGLILNGMKG LYTRIGRHYF ANPEARSLAL GFYHKLSALC
210 220 230
SEGAHDQVYE TVRRYGHESG EIWHRMQKNL PGDLAIQGR
Length:239
Mass (Da):26,969
Last modified:January 23, 2007 - v2
Checksum:i1FECA0DDAD5EB830
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X08087 Genomic DNA. Translation: CAA30881.1.
U00096 Genomic DNA. Translation: AAC74271.1.
AP009048 Genomic DNA. Translation: BAA36042.1.
PIRiH64864.
RefSeqiNP_415705.1. NC_000913.3.
WP_000234823.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74271; AAC74271; b1187.
BAA36042; BAA36042; BAA36042.
GeneIDi948652.
KEGGiecj:JW1176.
eco:b1187.
PATRICi32117620. VBIEscCol129921_1232.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X08087 Genomic DNA. Translation: CAA30881.1.
U00096 Genomic DNA. Translation: AAC74271.1.
AP009048 Genomic DNA. Translation: BAA36042.1.
PIRiH64864.
RefSeqiNP_415705.1. NC_000913.3.
WP_000234823.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E2XX-ray2.00A1-239[»]
1H9GX-ray2.10A1-239[»]
1H9TX-ray3.25A/B1-239[»]
1HW1X-ray1.50A/B1-239[»]
1HW2X-ray3.25A/B1-239[»]
ProteinModelPortaliP0A8V6.
SMRiP0A8V6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260102. 14 interactors.
DIPiDIP-9564N.
IntActiP0A8V6. 2 interactors.
MINTiMINT-1264978.
STRINGi511145.b1187.

Proteomic databases

PaxDbiP0A8V6.
PRIDEiP0A8V6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74271; AAC74271; b1187.
BAA36042; BAA36042; BAA36042.
GeneIDi948652.
KEGGiecj:JW1176.
eco:b1187.
PATRICi32117620. VBIEscCol129921_1232.

Organism-specific databases

EchoBASEiEB0277.
EcoGeneiEG10281. fadR.

Phylogenomic databases

eggNOGiENOG4105C05. Bacteria.
COG2186. LUCA.
HOGENOMiHOG000278467.
InParanoidiP0A8V6.
KOiK03603.
OMAiIWETSGL.
PhylomeDBiP0A8V6.

Enzyme and pathway databases

BioCyciEcoCyc:PD01520.
ECOL316407:JW1176-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A8V6.
PROiP0A8V6.

Family and domain databases

CDDicd07377. WHTH_GntR. 1 hit.
Gene3Di1.10.10.10. 1 hit.
1.20.120.530. 1 hit.
HAMAPiMF_00696. HTH_FadR. 1 hit.
InterProiIPR014178. FA-response_TF_FadR.
IPR028374. FadR_C.
IPR008920. TF_FadR/GntR_C.
IPR000524. Tscrpt_reg_HTH_GntR.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF07840. FadR_C. 1 hit.
PF00392. GntR. 1 hit.
[Graphical view]
PRINTSiPR00035. HTHGNTR.
SMARTiSM00345. HTH_GNTR. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF48008. SSF48008. 1 hit.
TIGRFAMsiTIGR02812. fadR_gamma. 1 hit.
PROSITEiPS50949. HTH_GNTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADR_ECOLI
AccessioniPrimary (citable) accession number: P0A8V6
Secondary accession number(s): P09371, P76827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.