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Protein

Fatty acid metabolism regulator protein

Gene

fadR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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-KW
  • DNA binding transcription factor activity Source: EcoCyc
  • fatty-acyl-CoA binding Source: InterPro

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-KW

Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processFatty acid metabolism, Lipid metabolism, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciEcoCyc:PD01520

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

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

Chemistry databases

DrugBankiDB08231 MYRISTIC ACID

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
STRINGi316385.ECDH10B_1240

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

Phylogenomic databases

eggNOGiENOG4105C05 Bacteria
COG2186 LUCA
HOGENOMiHOG000278467
InParanoidiP0A8V6
KOiK03603
OMAiWETAGPN
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
InterProiView protein in InterPro
IPR014178 FA-response_TF_FadR
IPR028374 FadR_C
IPR008920 TF_FadR/GntR_C
IPR000524 Tscrpt_reg_HTH_GntR
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PANTHERiPTHR43537:SF10 PTHR43537:SF10, 1 hit
PfamiView protein in Pfam
PF07840 FadR_C, 1 hit
PF00392 GntR, 1 hit
PRINTSiPR00035 HTHGNTR
SMARTiView protein in SMART
SM00345 HTH_GNTR, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF48008 SSF48008, 1 hit
TIGRFAMsiTIGR02812 fadR_gamma, 1 hit
PROSITEiView protein in PROSITE
PS50949 HTH_GNTR, 1 hit

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
PATRICifig|1411691.4.peg.1100

Similar proteinsi

Entry informationi

Entry nameiFADR_ECOLI
AccessioniPrimary (citable) accession number: P0A8V6
Secondary accession number(s): P09371, P76827
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 113 of the entry and version 2 of the sequence. See 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

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