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Fatty acid metabolism regulator protein

 FADR_ECOLI              Reviewed;         239 AA.
P0A8V6; P09371; P76827;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-AUG-2020, entry version 126.
RecName: Full=Fatty acid metabolism regulator protein {ECO:0000255|HAMAP-Rule:MF_00696};
Name=fadR {ECO:0000255|HAMAP-Rule:MF_00696}; Synonyms=oleR, thdB;
OrderedLocusNames=b1187, JW1176;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=2843809; DOI=10.1093/nar/16.16.7995;
Dirusso C.C.;
"Nucleotide sequence of the fadR gene, a multifunctional regulator of fatty
acid metabolism in Escherichia coli.";
Nucleic Acids Res. 16:7995-8009(1988).
[2]
SEQUENCE REVISION TO 147.
STRAIN=K12;
Dirusso C.C.;
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-11, FUNCTION, ACTIVITY REGULATION, AND DNA-BINDING.
PubMed=1569108;
DiRusso C.C., Heimert T.L., Metzger A.K.;
"Characterization of FadR, a global transcriptional regulator of fatty acid
metabolism in Escherichia coli. Interaction with the fadB promoter is
prevented by long chain fatty acyl coenzyme A.";
J. Biol. Chem. 267:8685-8691(1992).
[7]
FUNCTION, AND DNA-BINDING.
PubMed=8446033; DOI=10.1111/j.1365-2958.1993.tb01122.x;
DiRusso C.C., Metzger A.K., Heimert T.L.;
"Regulation of transcription of genes required for fatty acid transport and
unsaturated fatty acid biosynthesis in Escherichia coli by FadR.";
Mol. Microbiol. 7:311-322(1993).
[8]
FUNCTION, ACTIVITY REGULATION VIA ACYL-COA-BINDING, INDUCTION, DOMAIN,
MUTAGENESIS OF TYR-215; GLY-216; GLU-218; SER-219; GLY-220; TRP-223;
GLN-227; LYS-228 AND ASN-229, AND DNA-BINDING.
PubMed=7836365; DOI=10.1074/jbc.270.3.1092;
Raman N., DiRusso C.C.;
"Analysis of acyl coenzyme A binding to the transcription factor FadR and
identification of amino acid residues in the carboxyl terminus required for
ligand binding.";
J. Biol. Chem. 270:1092-1097(1995).
[9]
FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ALA-9; ARG-35; ARG-49;
HIS-65; GLY-66 AND LYS-67.
PubMed=9388199; DOI=10.1074/jbc.272.49.30645;
Raman N., Black P.N., Dirusso C.C.;
"Characterization of the fatty acid-responsive transcription factor FadR.
Biochemical and genetic analyses of the native conformation and functional
domains.";
J. Biol. Chem. 272:30645-30650(1997).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11859088; DOI=10.1074/jbc.m201399200;
Zhang Y.-M., Marrakchi H., Rock C.O.;
"The FabR (YijC) transcription factor regulates unsaturated fatty acid
biosynthesis in Escherichia coli.";
J. Biol. Chem. 277:15558-15565(2002).
[11]
FUNCTION, AND ACTIVITY REGULATION.
STRAIN=K12;
PubMed=19854834; DOI=10.1074/jbc.m109.068239;
Zhu K., Zhang Y.M., Rock C.O.;
"Transcriptional regulation of membrane lipid homeostasis in Escherichia
coli.";
J. Biol. Chem. 284:34880-34888(2009).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=K12;
PubMed=21276098; DOI=10.1111/j.1365-2958.2011.07564.x;
Feng Y., Cronan J.E.;
"Complex binding of the FabR repressor of bacterial unsaturated fatty acid
biosynthesis to its cognate promoters.";
Mol. Microbiol. 80:195-218(2011).
[13]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND SUBUNIT.
PubMed=11013219; DOI=10.1093/emboj/19.19.5167;
van Aalten D.M., DiRusso C.C., Knudsen J., Wierenga R.K.;
"Crystal structure of FadR, a fatty acid-responsive transcription factor
with a novel acyl coenzyme A-binding fold.";
EMBO J. 19:5167-5177(2000).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH COENZYME A OR DNA,
SUBUNIT, AND DOMAIN.
PubMed=11296236; DOI=10.1093/emboj/20.8.2041;
van Aalten D.M., DiRusso C.C., Knudsen J.;
"The structural basis of acyl coenzyme A-dependent regulation of the
transcription factor FadR.";
EMBO J. 20:2041-2050(2001).
[15]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF APOPROTEIN OR IN COMPLEX WITH DNA,
AND SUBUNIT.
PubMed=11279025; DOI=10.1074/jbc.m100195200;
Xu Y., Heath R.J., Li Z., Rock C.O., White S.W.;
"The FadR.DNA complex. Transcriptional control of fatty acid metabolism in
Escherichia coli.";
J. Biol. Chem. 276:17373-17379(2001).
-!- FUNCTION: 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). {ECO:0000269|PubMed:11859088,
ECO:0000269|PubMed:1569108, ECO:0000269|PubMed:19854834,
ECO:0000269|PubMed:21276098, ECO:0000269|PubMed:7836365,
ECO:0000269|PubMed:8446033, ECO:0000269|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:7836365, PubMed:19854834).
{ECO:0000269|PubMed:1569108, ECO:0000269|PubMed:19854834}.
-!- SUBUNIT: 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). {ECO:0000269|PubMed:11013219,
ECO:0000269|PubMed:11279025, ECO:0000269|PubMed:11296236,
ECO:0000269|PubMed:9388199}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00696}.
-!- INDUCTION: By growth in the presence of long chain fatty acids (C14-
C18) (PubMed:7836365). {ECO:0000269|PubMed:7836365}.
-!- 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:7836365, PubMed:11296236).
{ECO:0000269|PubMed:11296236, ECO:0000269|PubMed:7836365,
ECO:0000269|PubMed:9388199}.
-!- 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). {ECO:0000269|PubMed:11859088,
ECO:0000269|PubMed:21276098}.
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EMBL; X08087; CAA30881.1; -; Genomic_DNA.
EMBL; U00096; AAC74271.1; -; Genomic_DNA.
EMBL; AP009048; BAA36042.1; -; Genomic_DNA.
PIR; H64864; H64864.
RefSeq; NP_415705.1; NC_000913.3.
RefSeq; WP_000234823.1; NZ_STEB01000023.1.
PDB; 1E2X; X-ray; 2.00 A; A=1-239.
PDB; 1H9G; X-ray; 2.10 A; A=1-239.
PDB; 1H9T; X-ray; 3.25 A; A/B=1-239.
PDB; 1HW1; X-ray; 1.50 A; A/B=1-239.
PDB; 1HW2; X-ray; 3.25 A; A/B=1-239.
PDBsum; 1E2X; -.
PDBsum; 1H9G; -.
PDBsum; 1H9T; -.
PDBsum; 1HW1; -.
PDBsum; 1HW2; -.
SMR; P0A8V6; -.
BioGRID; 4260102; 14.
DIP; DIP-9564N; -.
IntAct; P0A8V6; 2.
STRING; 511145.b1187; -.
DrugBank; DB08231; Myristic acid.
jPOST; P0A8V6; -.
PaxDb; P0A8V6; -.
PRIDE; P0A8V6; -.
EnsemblBacteria; AAC74271; AAC74271; b1187.
EnsemblBacteria; BAA36042; BAA36042; BAA36042.
GeneID; 49585035; -.
GeneID; 948652; -.
KEGG; ecj:JW1176; -.
KEGG; eco:b1187; -.
PATRIC; fig|1411691.4.peg.1100; -.
EchoBASE; EB0277; -.
eggNOG; COG2186; Bacteria.
HOGENOM; CLU_017584_9_4_6; -.
InParanoid; P0A8V6; -.
KO; K03603; -.
PhylomeDB; P0A8V6; -.
BioCyc; EcoCyc:PD01520; -.
BioCyc; ECOL316407:JW1176-MONOMER; -.
EvolutionaryTrace; P0A8V6; -.
PRO; PR:P0A8V6; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:EcoCyc.
GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
GO; GO:0019395; P:fatty acid oxidation; EXP:EcoCyc.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:EcoCyc.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:CACAO.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:EcoCyc.
GO; GO:0019217; P:regulation of fatty acid metabolic process; IGI:CACAO.
CDD; cd07377; WHTH_GntR; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 1.20.120.530; -; 1.
HAMAP; MF_00696; HTH_FadR; 1.
InterPro; IPR014178; FA-response_TF_FadR.
InterPro; IPR028374; FadR_C.
InterPro; IPR008920; TF_FadR/GntR_C.
InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR43537:SF10; PTHR43537:SF10; 1.
Pfam; PF07840; FadR_C; 1.
Pfam; PF00392; GntR; 1.
PRINTS; PR00035; HTHGNTR.
SMART; SM00345; HTH_GNTR; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF48008; SSF48008; 1.
TIGRFAMs; TIGR02812; fadR_gamma; 1.
PROSITE; PS50949; HTH_GNTR; 1.
1: Evidence at protein level;
3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
Fatty acid metabolism; Lipid metabolism; Reference proteome; Repressor;
Transcription; Transcription regulation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000269|PubMed:1569108"
CHAIN 2..239
/note="Fatty acid metabolism regulator protein"
/id="PRO_0000050626"
DOMAIN 6..74
/note="HTH gntR-type"
/evidence="ECO:0000255|HAMAP-Rule:MF_00696"
DNA_BIND 34..69
/note="H-T-H motif"
/evidence="ECO:0000269|PubMed:11279025,
ECO:0000269|PubMed:11296236"
REGION 103..107
/note="Coenzyme A binding"
/evidence="ECO:0000269|PubMed:11296236"
REGION 215..230
/note="Binds acyl-CoA"
/evidence="ECO:0000305|PubMed:7836365"
BINDING 99
/note="Coenzyme A; via carbonyl oxygen"
/evidence="ECO:0000269|PubMed:11296236"
BINDING 213
/note="Coenzyme A"
/evidence="ECO:0000269|PubMed:11296236"
BINDING 219
/note="Coenzyme A"
/evidence="ECO:0000269|PubMed:11296236"
MUTAGEN 9
/note="A->V: Dominant negative to wild-type, decreased DNA-
binding."
/evidence="ECO:0000269|PubMed:9388199"
MUTAGEN 35
/note="R->C: Dominant negative to wild-type, decreased DNA-
binding."
/evidence="ECO:0000269|PubMed:9388199"
MUTAGEN 49
/note="R->A: Dominant negative to wild-type."
/evidence="ECO:0000269|PubMed:9388199"
MUTAGEN 65
/note="H->Y: Dominant negative to wild-type, decreased DNA-
binding."
/evidence="ECO:0000269|PubMed:9388199"
MUTAGEN 66
/note="G->D: Dominant negative to wild-type, decreased DNA-
binding."
/evidence="ECO:0000269|PubMed:9388199"
MUTAGEN 67
/note="K->S: Dominant negative to wild-type, decreased DNA-
binding."
/evidence="ECO:0000269|PubMed:9388199"
MUTAGEN 215
/note="Y->A: Loss of FadR repression."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 216
/note="G->A: Super-repressor, non-inducible phenotype,
cells cannot use long chain fatty acids as carbon source."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 218
/note="E->A: Reduced ability to repress."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 219
/note="S->A: Reduced ability to repress."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 219
/note="S->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."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 220
/note="G->A: Loss of FadR repression."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 223
/note="W->A: Super-repressor, non-inducible phenotype,
cells cannot use long chain fatty acids as carbon source."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 227
/note="Q->A: Loss of FadR repression."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 228
/note="K->A: Reduced ability to repress."
/evidence="ECO:0000269|PubMed:7836365"
MUTAGEN 229
/note="N->A: Loss of FadR repression."
/evidence="ECO:0000269|PubMed:7836365"
HELIX 8..21
/evidence="ECO:0000244|PDB:1HW1"
HELIX 34..41
/evidence="ECO:0000244|PDB:1HW1"
HELIX 45..57
/evidence="ECO:0000244|PDB:1HW1"
STRAND 60..64
/evidence="ECO:0000244|PDB:1HW1"
STRAND 67..71
/evidence="ECO:0000244|PDB:1HW1"
HELIX 74..77
/evidence="ECO:0000244|PDB:1HW1"
HELIX 80..82
/evidence="ECO:0000244|PDB:1HW1"
HELIX 83..89
/evidence="ECO:0000244|PDB:1HW1"
HELIX 91..93
/evidence="ECO:0000244|PDB:1HW1"
HELIX 94..119
/evidence="ECO:0000244|PDB:1HW1"
HELIX 121..129
/evidence="ECO:0000244|PDB:1HW1"
TURN 130..133
/evidence="ECO:0000244|PDB:1HW1"
HELIX 138..155
/evidence="ECO:0000244|PDB:1HW1"
HELIX 159..179
/evidence="ECO:0000244|PDB:1HW1"
HELIX 183..202
/evidence="ECO:0000244|PDB:1HW1"
HELIX 206..227
/evidence="ECO:0000244|PDB:1HW1"
SEQUENCE 239 AA; 26969 MW; 1FECA0DDAD5EB830 CRC64;
MVIKAQSPAG FAEEYIIESI WNNRFPPGTI LPAERELSEL IGVTRTTLRE VLQRLARDGW
LTIQHGKPTK VNNFWETSGL NILETLARLD HESVPQLIDN LLSVRTNIST IFIRTAFRQH
PDKAQEVLAT ANEVADHADA FAELDYNIFR GLAFASGNPI YGLILNGMKG LYTRIGRHYF
ANPEARSLAL GFYHKLSALC SEGAHDQVYE TVRRYGHESG EIWHRMQKNL PGDLAIQGR


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E0344m ELISA E-FABP,Epidermal-type fatty acid-binding protein,Fabp5,Fabpe,Fatty acid-binding protein 5,Fatty acid-binding protein, epidermal,Keratinocyte lipid-binding protein,Klbp,Mal1,Mouse,Mus musculus,PA 96T
E2204r Fabp1,Fatty acid-binding protein 1,Fatty acid-binding protein, liver,L-FABP,Liver-type fatty acid-binding protein,p14,Rat,Rattus norvegicus,SCP,Squalene- and sterol-carrier protein,Z-protein
20-321-175102 HEART FATTY ACID BINDING PROTEIN (H-FABP) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN HEART FATTY ACID BINDING PROTEIN (H-FABP); H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-bindin 0.05 mg
20-321-175100 HEART FATTY ACID BINDING PROTEIN (H-FABP) - BIOTINYLATED MONOCLONAL ANTIBODY TO HUMAN HEART FATTY ACID BINDING PROTEIN (H-FABP); H-FABP; Heart-type fatty acid-binding protein; Muscle fatty acid-bindin 0.05 mg
Pathways :
WP1648: Fatty acid metabolism
WP1700: Selenoamino acid metabolism
WP2316: PPAR signaling pathway
WP2102: Fatty acid metabolism
WP1817: Fatty acid, triacylglycerol, and ketone body metabolism
WP1689: Porphyrin and chlorophyll metabolism
WP1207: Fatty Acid Beta Oxidation
WP336: Fatty Acid Biosynthesis
WP16: Fatty Acid Elongation, Unsaturated
WP1654: gamma-Hexachlorocyclohexane degradation
WP357: Fatty Acid Biosynthesis
WP568: Fatty Acid Biosynthesis
WP143: Fatty Acid Beta Oxidation
WP1853: Metabolism of proteins
WP148: Fatty Acid Beta Oxidation 2
WP1639: Cyanoamino acid metabolism
WP2318: Fatty acid oxidation
WP1714: Tyrosine metabolism
WP209: Fatty Acid Beta Oxidation Meta
WP38: Fatty Acid Biosynthesis
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP105: Fatty Acid Beta Oxidation 2
WP1690: Propanoate metabolism
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1352: Fatty Acid Biosynthesis

Related Genes :

Bibliography :
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