RegulonDB

Gene
Name:	fadA
Synonym(s):	ECK3837, EG10278, b3845, oldA
Genome position(nucleotides):	4027609 <-- 4028772 Genome Browser
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	57.73
External database links:

ASAP:	ABE-0012562
CGSC:	794
ECHOBASE:	EB0274
ECOLIHUB:	fadA
OU-MICROARRAY:	b3845
STRING:	511145.b3845
COLOMBOS:	fadA

Gene

Name:

fadA

Synonym(s):

ECK3837, EG10278, b3845, oldA

Genome position(nucleotides):

4027609 <-- 4028772 Genome Browser

Strand:

reverse

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

57.73

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

OU-MICROARRAY:

STRING:

COLOMBOS:

Type

Positions

Sequence

371 -> 374

TMCI

37 -> 37

261 -> 386

LKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSASDIGVFEMNEAFAAQILPCIKDLGLIEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER

119 -> 119

4 -> 254

VVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQTLEQGFNIARNAALLAEVPHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEHMGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGISREMQDAFAARSHARAWAATQSAAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVNGMVTAGTSSALSDGAAAMLVMSES

Type

Positions

Sequence

371 -> 374

TMCI

37 -> 37

261 -> 386

LKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSASDIGVFEMNEAFAAQILPCIKDLGLIEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLMERKDVQFGLATMCIGLGQGIATVFER

119 -> 119

4 -> 254

Multifun Terms (GenProtEC)

1 - metabolism --> 1.1 - carbon utilization --> 1.1.2 - fatty acids

Gene Ontology Terms (GO)

cellular_component

GO:0005737 - cytoplasm
GO:0005829 - cytosol
GO:0036125 - fatty acid beta-oxidation multienzyme complex

molecular_function

GO:0005515 - protein binding
GO:0016740 - transferase activity
GO:0016746 - acyltransferase activity
GO:0016747 - acyltransferase activity, transferring groups other than amino-acyl groups
GO:0003988 - acetyl-CoA C-acyltransferase activity

biological_process

GO:0006629 - lipid metabolic process
GO:0006631 - fatty acid metabolic process
GO:0010124 - phenylacetate catabolic process
GO:0009062 - fatty acid catabolic process
GO:0016042 - lipid catabolic process
GO:0006635 - fatty acid beta-oxidation

Transcriptional Regulation
	Display Regulation
Activated by:	Fis
Repressed by:	FadR, Rob, ArcA

Transcriptional Regulation

Display Regulation

Activated by:

Fis

Repressed by:

FadR, Rob, ArcA

	Type	Name	Post Left	Post Right	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
	promoter	TSS_4517	4027285		forward	nd	[RS-EPT-CBR]	[14]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

TSS_4517

4027285

forward

[RS-EPT-CBR]

[14]

Evidence
[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Evidence

[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Reference(s)
[1] Binstock JF., Schulz H., 1981, Fatty acid oxidation complex from Escherichia coli., Methods Enzymol 71 Pt C:403-11
[2] DiRusso CC., 1990, Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes., J Bacteriol 172(11):6459-68
[3] Goh EB., Baidoo EE., Keasling JD., Beller HR., 2012, Engineering of bacterial methyl ketone synthesis for biofuels., Appl Environ Microbiol 78(1):70-80
[4] Kim S., Clomburg JM., Gonzalez R., 2015, Synthesis of medium-chain length (C6-C10) fuels and chemicals via β-oxidation reversal in Escherichia coli., J Ind Microbiol Biotechnol 42(3):465-75
[5] Mehrer CR., Incha MR., Politz MC., Pfleger BF., 2018, Anaerobic production of medium-chain fatty alcohols via a β-reduction pathway., Metab Eng 48:63-71
[6] Nakahigashi K., Inokuchi H., 1990, Nucleotide sequence of the fadA and fadB genes from Escherichia coli., Nucleic Acids Res 18(16):4937
[7] Nishimaki-Mogami T., Yamanaka H., Mizugaki M., 1987, Involvement of the fatty acid oxidation complex in acetyl-CoA-dependent chain elongation of fatty acids in Escherichia coli., J Biochem 102(2):427-32
[8] O'Brien WJ., Frerman FE., 1977, Evidence for a complex of three beta-oxidation enzymes in Escherichia coli: induction and localization., J Bacteriol 132(2):532-40
[9] Overath P., Pauli G., Schairer HU., 1969, Fatty acid degradation in Escherichia coli. An inducible acyl-CoA synthetase, the mapping of old-mutations, and the isolation of regulatory mutants., Eur J Biochem 7(4):559-74
[10] Park SJ., Park JP., Lee SY., 2002, Metabolic engineering of Escherichia coli for the production of medium-chain-length polyhydroxyalkanoates rich in specific monomers., FEMS Microbiol Lett 214(2):217-22
[11] Pramanik A., Schulz H., 1983, Multienzyme complexes of fatty acid oxidation from Escherichia coli K12 and from a mutant with a defective L-3-hydroxyacyl coenzyme A dehydrogenase., Biochim Biophys Acta 750(1):41-6
[12] Yang SY., He Yang XY., Healy-Louie G., Schulz H., Elzinga M., 1991, Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon., J Biol Chem 266(24):16255
[13] Yang SY., Yang XY., Healy-Louie G., Schulz H., Elzinga M., 1990, Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon., J Biol Chem 265(18):10424-9
[14] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

Reference(s)

[1] Binstock JF., Schulz H., 1981, Fatty acid oxidation complex from Escherichia coli., Methods Enzymol 71 Pt C:403-11

[2] DiRusso CC., 1990, Primary sequence of the Escherichia coli fadBA operon, encoding the fatty acid-oxidizing multienzyme complex, indicates a high degree of homology to eucaryotic enzymes., J Bacteriol 172(11):6459-68

[3] Goh EB., Baidoo EE., Keasling JD., Beller HR., 2012, Engineering of bacterial methyl ketone synthesis for biofuels., Appl Environ Microbiol 78(1):70-80

[4] Kim S., Clomburg JM., Gonzalez R., 2015, Synthesis of medium-chain length (C6-C10) fuels and chemicals via β-oxidation reversal in Escherichia coli., J Ind Microbiol Biotechnol 42(3):465-75

[5] Mehrer CR., Incha MR., Politz MC., Pfleger BF., 2018, Anaerobic production of medium-chain fatty alcohols via a β-reduction pathway., Metab Eng 48:63-71

[6] Nakahigashi K., Inokuchi H., 1990, Nucleotide sequence of the fadA and fadB genes from Escherichia coli., Nucleic Acids Res 18(16):4937

[7] Nishimaki-Mogami T., Yamanaka H., Mizugaki M., 1987, Involvement of the fatty acid oxidation complex in acetyl-CoA-dependent chain elongation of fatty acids in Escherichia coli., J Biochem 102(2):427-32

[8] O'Brien WJ., Frerman FE., 1977, Evidence for a complex of three beta-oxidation enzymes in Escherichia coli: induction and localization., J Bacteriol 132(2):532-40

[9] Overath P., Pauli G., Schairer HU., 1969, Fatty acid degradation in Escherichia coli. An inducible acyl-CoA synthetase, the mapping of old-mutations, and the isolation of regulatory mutants., Eur J Biochem 7(4):559-74

[10] Park SJ., Park JP., Lee SY., 2002, Metabolic engineering of Escherichia coli for the production of medium-chain-length polyhydroxyalkanoates rich in specific monomers., FEMS Microbiol Lett 214(2):217-22

[11] Pramanik A., Schulz H., 1983, Multienzyme complexes of fatty acid oxidation from Escherichia coli K12 and from a mutant with a defective L-3-hydroxyacyl coenzyme A dehydrogenase., Biochim Biophys Acta 750(1):41-6

[12] Yang SY., He Yang XY., Healy-Louie G., Schulz H., Elzinga M., 1991, Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon., J Biol Chem 266(24):16255

[13] Yang SY., Yang XY., Healy-Louie G., Schulz H., Elzinga M., 1990, Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon., J Biol Chem 265(18):10424-9

[14] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.