RegulonDB

Gene
Name:	fadB
Synonym(s):	ECK3838, EG10279, b3846, oldB
Genome position(nucleotides):	4028782 <-- 4030971
Strand:	reverse
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	55.21
External database links:

ASAP:	ABE-0012564
CGSC:	793
ECHOBASE:	EB0275
ECOLIHUB:	fadB
OU-MICROARRAY:	b3846
STRING:	511145.b3846
COLOMBOS:	fadB

Gene

Name:

fadB

Synonym(s):

ECK3838, EG10279, b3846, oldB

Genome position(nucleotides):

4028782 <-- 4030971

Strand:

reverse

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

55.21

External database links:

ASAP:

CGSC:

ECHOBASE:

ECOLIHUB:

OU-MICROARRAY:

STRING:

COLOMBOS:

Type

Positions

Sequence

Comment

1 -> 189

MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVK

UniProt: Enoyl-CoA hydratase/isomerase; Sequence Annotation Type: region of interest.

14 -> 205

EDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAI

116 -> 116

UniProt: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected..

311 -> 729

ETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA

UniProt: 3-hydroxyacyl-CoA dehydrogenase; Sequence Annotation Type: region of interest.

316 -> 494

AAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDC

Type

Positions

Sequence

Comment

1 -> 189

MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVK

UniProt: Enoyl-CoA hydratase/isomerase; Sequence Annotation Type: region of interest.

14 -> 205

EDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAI

116 -> 116

UniProt: Absence of both enoyl-CoA hydratase and 3-hydroxyacyl-CoA epimerase activities. Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase is only slightly affected..

311 -> 729

UniProt: 3-hydroxyacyl-CoA dehydrogenase; Sequence Annotation Type: region of interest.

316 -> 494

AAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDC

322 -> 322

UniProt: 10-fold increase in KM for NADH..

400 -> 402

VVE

UniProt: NAD.

450 -> 450

UniProt: Almost complete loss of 3-hydroxyacyl-CoA dehydrogenase activity..

496 -> 592

GFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRY

518 -> 518

UniProt: In Ref. 1; AAA23750..

627 -> 691

IIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQ

664 -> 664

UniProt: In Ref. 3; CAB40809..

666 -> 666

UniProt: In Ref. 3; CAB40809..

708 -> 729

RHNEPYYPPVEPARPVGDLKTA

UniProt: Disordered; Sequence Annotation Type: region of interest.

Multifun Terms (GenProtEC)

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

Gene Ontology Terms (GO)

cellular_component

GO:0036125 - fatty acid beta-oxidation multienzyme complex

molecular_function

GO:0016509 - long-chain-3-hydroxyacyl-CoA dehydrogenase activity
GO:0003824 - catalytic activity
GO:0016829 - lyase activity
GO:0016853 - isomerase activity
GO:0016491 - oxidoreductase activity
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0003857 - 3-hydroxyacyl-CoA dehydrogenase activity
GO:0004165 - delta(3)-delta(2)-enoyl-CoA isomerase activity
GO:0004300 - enoyl-CoA hydratase activity
GO:0008692 - 3-hydroxybutyryl-CoA epimerase activity
GO:0070403 - NAD+ binding

biological_process

GO:0008152 - metabolic process
GO:0006629 - lipid metabolic process
GO:0006631 - fatty acid metabolic 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

RNA cis-regulatory element

Attenuation:	Transcriptional

RNA cis-regulatory element

Attenuation:

Transcriptional

	Type	Name	Post Left	Post Right	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
	promoter	TSS_4518	4031130		forward	nd	[RS-EPT-CBR]	[15]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

TSS_4518

4031130

forward

[RS-EPT-CBR]

[15]

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] 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
[2] Klein K., Steinberg R., Fiethen B., Overath P., 1971, Fatty acid degradation in Escherichia coli. An inducible system for the uptake of fatty acids and further characterization of old mutants., Eur J Biochem 19(3):442-50
[3] Mahalik S., Sharma AK., Jain P., Mukherjee KJ., 2017, Identifying genomic targets for protein over-expression by "omics" analysis of Quiescent Escherichia coli cultures., Microb Cell Fact 16(1):133
[4] 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
[5] Nakahigashi K., Inokuchi H., 1990, Nucleotide sequence of the fadA and fadB genes from Escherichia coli., Nucleic Acids Res 18(16):4937
[6] 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
[7] Smeland TE., Li J., Cuebas D., Schulz H., 1992, The mechanism and function of 3-hydroxyacyl-CoA epimerase in rat liver and Escherichia coli., Prog Clin Biol Res 375:85-93
[8] Waterson RM., Conway RS., 1981, Enoyl-CoA hydratases from Clostridium acetobutylicum and Escherichia coli., Methods Enzymol 71 Pt C:421-30
[9] Yang SY., 1992, The fadBA operon of Escherichia coli and evidence for the endosymbiont origin of peroxisomes., Prog Clin Biol Res 375:183-8
[10] Yang SY., Cuebas D., Schulz H., 1986, 3-Hydroxyacyl-CoA epimerases of rat liver peroxisomes and Escherichia coli function as auxiliary enzymes in the beta-oxidation of polyunsaturated fatty acids., J Biol Chem 261(26):12238-43
[11] Yang SY., Cuebas D., Schulz H., 1986, Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli., J Biol Chem 261(33):15390-5
[12] Yang SY., Li JM., He XY., Cosloy SD., Schulz H., 1988, Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase., J Bacteriol 170(6):2543-8
[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] Yang XY., Schulz H., Elzinga M., Yang SY., 1991, Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli., Biochemistry 30(27):6788-95
[15] 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] 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

[2] Klein K., Steinberg R., Fiethen B., Overath P., 1971, Fatty acid degradation in Escherichia coli. An inducible system for the uptake of fatty acids and further characterization of old mutants., Eur J Biochem 19(3):442-50

[3] Mahalik S., Sharma AK., Jain P., Mukherjee KJ., 2017, Identifying genomic targets for protein over-expression by "omics" analysis of Quiescent Escherichia coli cultures., Microb Cell Fact 16(1):133

[4] 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

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

[6] 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

[7] Smeland TE., Li J., Cuebas D., Schulz H., 1992, The mechanism and function of 3-hydroxyacyl-CoA epimerase in rat liver and Escherichia coli., Prog Clin Biol Res 375:85-93

[8] Waterson RM., Conway RS., 1981, Enoyl-CoA hydratases from Clostridium acetobutylicum and Escherichia coli., Methods Enzymol 71 Pt C:421-30

[9] Yang SY., 1992, The fadBA operon of Escherichia coli and evidence for the endosymbiont origin of peroxisomes., Prog Clin Biol Res 375:183-8

[10] Yang SY., Cuebas D., Schulz H., 1986, 3-Hydroxyacyl-CoA epimerases of rat liver peroxisomes and Escherichia coli function as auxiliary enzymes in the beta-oxidation of polyunsaturated fatty acids., J Biol Chem 261(26):12238-43

[11] Yang SY., Cuebas D., Schulz H., 1986, Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli., J Biol Chem 261(33):15390-5

[12] Yang SY., Li JM., He XY., Cosloy SD., Schulz H., 1988, Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase., J Bacteriol 170(6):2543-8

[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] Yang XY., Schulz H., Elzinga M., Yang SY., 1991, Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli., Biochemistry 30(27):6788-95

[15] 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.