RegulonDB RegulonDB 10.8: Gene Form
   

fadB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fadB pepQ fadA ArcA Fis FadR anti-anti-terminator anti-terminator terminator pepQp pepQp TSS_4518 TSS_4518 fadBp fadBp

Gene      
Name: fadB    Texpresso search in the literature
Synonym(s): ECK3838, EG10279, b3846, oldB
Genome position(nucleotides): 4028782 <-- 4030971 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
55.21
External database links:  
ASAP:
ABE-0012564
CGSC:
793
ECHOBASE:
EB0275
OU-MICROARRAY:
b3846
PortEco:
fadB
STRING:
511145.b3846
COLOMBOS: fadB


Product      
Name: multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Δ3-cis- Δ2-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase
Synonym(s): FadB, OldB
Sequence: Get amino acid sequence Fasta Format
Molecular weight: 79.594
Isoelectric point: 6.046
Motif(s):
 
Type Positions Sequence
1 -> 189 MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVK
14 -> 205 EDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAI
450 -> 450 H
664 -> 664 F
311 -> 729 ETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA

 

Classification:
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:0003857 - 3-hydroxyacyl-CoA dehydrogenase activity
GO:0004165 - dodecenoyl-CoA delta-isomerase activity
GO:0004300 - enoyl-CoA hydratase activity
GO:0008692 - 3-hydroxybutyryl-CoA epimerase activity
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
GO:0055114 - oxidation-reduction process
Note(s): Note(s): ...[more].
Reference(s): [1] DiRusso CC. 1990
[2] Klein K., et al., 1971
[3] Mahalik S., et al., 2017
[4] Mehrer CR., et al., 2018
[5] Nakahigashi K., et al., 1990
[6] Nishimaki-Mogami T., et al., 1987
[7] Smeland TE., et al., 1992
[8] Waterson RM., et al., 1981
[9] Yang SY. 1992
[10] Yang SY., et al., 1986
[11] Yang SY., et al., 1986
[12] Yang SY., et al., 1988
[13] Yang SY., et al., 1990
[14] Yang XY., et al., 1991
External database links:  
DIP:
DIP-9560N
ECOCYC:
FADB-MONOMER
ECOLIWIKI:
b3846
INTERPRO:
IPR008927
INTERPRO:
IPR036291
INTERPRO:
IPR029045
INTERPRO:
IPR018376
INTERPRO:
IPR012799
INTERPRO:
IPR006180
INTERPRO:
IPR006176
INTERPRO:
IPR006108
INTERPRO:
IPR001753
MODBASE:
P21177
PFAM:
PF02737
PFAM:
PF00725
PFAM:
PF00378
PRIDE:
P21177
PROSITE:
PS00166
PROSITE:
PS00067
REFSEQ:
NP_418288
SMR:
P21177
SWISSMODEL:
P21177
UNIPROT:
P21177


Operon      
Name: fadBA         
Operon arrangement:
Transcription unit        Promoter
fadBA


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


RNA cis-regulatory element    
Attenuation: Transcriptional


Elements in the selected gene context region unrelated to any object in RegulonDB      

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


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.


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