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MetaCyc Enzyme: fatty acid oxidation complex, β component

Gene: fadA Accession Numbers: EG10278 (MetaCyc), b3845, ECK3837

Synonyms: oldA

Species: Escherichia coli K-12 substr. MG1655

Component of: aerobic fatty acid oxidation complex

Subunit composition of fatty acid oxidation complex, β component = [FadA]2
         3-ketoacyl-CoA thiolase = FadA

Summary:
3-ketoacyl-CoA thiolase is involved in the degradation of fatty acids via the β-oxidation cycle. It has broad chain-length specificity for substrates although it exhibits its highest activity with medium-chain substrates. It is part of a multienzyme complex and is coded for by the fadA gene [Yang90a, Binstock81]

Locations: cytosol

Map Position: [4,025,632 <- 4,026,795]

Molecular Weight of Polypeptide: 40.876 kD (from nucleotide sequence)

pI: 6.72

Unification Links: ASAP:ABE-0012562 , CGSC:794 , DIP:DIP-9559N , EchoBASE:EB0274 , EcoGene:EG10278 , EcoliWiki:b3845 , ModBase:P21151 , OU-Microarray:b3845 , PortEco:fadA , Pride:P21151 , Protein Model Portal:P21151 , RefSeq:YP_026272 , RegulonDB:EG10278 , SMR:P21151 , String:511145.b3845 , Swiss-Model:P21151 , UniProt:P21151

Relationship Links: InterPro:IN-FAMILY:IPR002155 , InterPro:IN-FAMILY:IPR012805 , InterPro:IN-FAMILY:IPR016038 , InterPro:IN-FAMILY:IPR016039 , InterPro:IN-FAMILY:IPR020610 , InterPro:IN-FAMILY:IPR020613 , InterPro:IN-FAMILY:IPR020615 , InterPro:IN-FAMILY:IPR020616 , InterPro:IN-FAMILY:IPR020617 , Panther:IN-FAMILY:PTHR18919 , Pfam:IN-FAMILY:PF00108 , Pfam:IN-FAMILY:PF02803 , Prosite:IN-FAMILY:PS00098 , Prosite:IN-FAMILY:PS00099 , Prosite:IN-FAMILY:PS00737

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reaction of [a cis-3-enoyl-CoA ↔ a trans-2-enoyl-CoA] (5.3.3.8):
i18: 3-cis-dodecenoyl-CoA → trans-dodec-2-enoyl-CoA (5.3.3.8)

Instance reactions of [a 2,3,4-saturated fatty acyl CoA + acetyl-CoA ← a 3-oxoacyl-CoA + coenzyme A] (2.3.1.16):
i19: octanoyl-CoA + acetyl-CoA ← 3-oxodecanoyl-CoA + coenzyme A (2.3.1.16)

i20: hexanoyl-CoA + acetyl-CoA = 3-oxooctanoyl-CoA + coenzyme A (2.3.1.16)

i21: lauroyl-CoA + acetyl-CoA ← 3-oxo-myristoyl-CoA + coenzyme A (2.3.1.16)

i22: butanoyl-CoA + acetyl-CoA → 3-oxohexanoyl-CoA + coenzyme A (2.3.1.16)

i23: acetyl-CoA + propanoyl-CoA = β-ketovaleryl-CoA + coenzyme A (2.3.1.9)

i24: acetyl-CoA + myristoyl-CoA = 3-oxo-palmitoyl-CoA + coenzyme A (2.3.1.155)

i25: acetyl-CoA + myristoyl-CoA ← 3-oxo-palmitoyl-CoA + coenzyme A (2.3.1.155)

i26: decanoyl-CoA + acetyl-CoA = 3-oxododecanoyl-CoA + coenzyme A (2.3.1.16)

Instance reactions of [a (3S)-3-hydroxyacyl-CoA ← a trans-2-enoyl-CoA + H2O] (4.2.1.17):
i11: (S)-3-hydroxybutanoyl-CoA ↔ crotonyl-CoA + H2O (4.2.1.150)

i12: (S)-3-hydroxyhexanoyl-CoA → trans-hex-2-enoyl-CoA + H2O (4.2.1.74)

i13: (3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA ← (2E,6Z,9Z,12Z,15Z,18Z,21Z)-tetracosaheptaenoyl-CoA + H2O (4.2.1.17)

i14: (3R)-3-hydroxy-lignoceroyl-CoA → trans-lignocer-2-enoyl-CoA + H2O (4.2.1.134)

i15: (S)-3-hydroxydecanoyl-CoA ← trans-dec-2-enoyl-CoA + H2O (4.2.1.17)

i16: a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2,3-dehydroacyl-CoA + H2O (4.2.1.150)

i17: a long-chain (3S)-3-hydroxyacyl-CoA = a long-chain trans-2,3-dehydroacyl-CoA + H2O (4.2.1.74)

Instance reactions of [a (3S)-3-hydroxyacyl-CoA + NAD+ → a 3-oxoacyl-CoA + NADH + H+] (1.1.1.35):
i1: (S)-3-hydroxybutanoyl-CoA + NAD+ ↔ acetoacetyl-CoA + NADH + H+ (1.1.1.35)

i2: (S)-3-hydroxyoctanoyl-CoA + NAD+ = 3-oxooctanoyl-CoA + NADH + H+ (1.1.1.35)

i3: (S)-3-hydroxyhexanoyl-CoA + NAD+ ← 3-oxohexanoyl-CoA + NADH + H+ (1.1.1.35)

i4: (11Z)-(S)-3-hydroxyhexadec-11-enoyl-CoA + NAD+ → (11Z)-3-oxo-hexadecenoyl-CoA + NADH + H+ (1.1.1.211)

i5: (3S)-hydroxy-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NAD+ → 3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NADH + H+ (1.1.1.-)

i6: 3-hydroxy-5-cis-tetradecenoyl-CoA + NAD+ = 3-keto-5-cis-tetradecenoyl-CoA + NADH + H+ (1.1.1.211)

i7: (S)-3-hydroxytetradecanoyl-CoA + NAD+ → 3-oxo-myristoyl-CoA + NADH + H+ (no EC#)

i8: (S)-3-hydroxyhexadecanoyl-CoA + NAD+ → 3-oxo-palmitoyl-CoA + NADH + H+ (1.1.1.211)

i9: (S)-3-hydroxydecanoyl-CoA + NAD+ → 3-oxodecanoyl-CoA + NADH + H+ (1.1.1.35)

i10: a long-chain (3S)-3-hydroxyacyl-CoA + NAD+ = a long-chain 3-oxoacyl-CoA + NADH + H+ (1.1.1.211)

GO Terms:

Biological Process: GO:0006635 - fatty acid beta-oxidation Inferred from experiment Inferred by computational analysis [UniProtGOA12, Campbell03a]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0016042 - lipid catabolic process Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
Molecular Function: GO:0003988 - acetyl-CoA C-acyltransferase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Pramanik79]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11]
GO:0016747 - transferase activity, transferring acyl groups other than amino-acyl groups Inferred by computational analysis [GOA01]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, GOA01]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization fatty acids

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International


Enzymatic reaction of: 3-ketoacyl-CoA thiolase (fatty acid oxidation complex, β component)

EC Number: 2.3.1.16

3-cis-dodecenoyl-CoA + acetyl-CoA <=> 3-keto-5-cis-tetradecenoyl-CoA + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Summary:
Experimental work reported in [Ren04] was conducted using E. coli strain B


Enzymatic reaction of: 3-ketoacyl-CoA thiolase (fatty acid oxidation complex, β component)

Synonyms: acetyl-CoA C-acyltransferase, β-ketothiolase, acetyl-CoA acyltransferase, acyl-CoA:acetyl-CoA C-acyltransferase

EC Number: 2.3.1.16

a 2,3,4-saturated fatty acyl CoA + acetyl-CoA <=> a 3-oxoacyl-CoA + coenzyme A

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: pyruvate fermentation to hexanol , fatty acid β-oxidation I

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Inhibitors (Unknown Mechanism): tris [Pramanik79] , iodoacetamide [Yang83a] , N-ethylmaleimide [Pawar81]


Subunit of: aerobic fatty acid oxidation complex

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of aerobic fatty acid oxidation complex = [(FadB)2][(FadA)2]
         fatty acid oxidation complex, α component = (FadB)2 (summary available)
                 dodecenoyl-CoA δ-isomerase, enoyl-CoA hydratase, 3-hydroxybutyryl-CoA epimerase, 3-hydroxyacyl-CoA dehydrogenase = FadB
         fatty acid oxidation complex, β component = (FadA)2
                 3-ketoacyl-CoA thiolase = FadA

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 37
[Daniels92, Nakahigashi90, UniProt10]
UniProt: (in Ref. 3; CAB40810 and 4; AAA67642);
Active-Site 91
[UniProt10a]
UniProt: Acyl-thioester intermediate; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 119
[Nakahigashi90, UniProt10]
UniProt: (in Ref. 3; CAB40810);
Active-Site 343
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 371 -> 374
[Yang90a, UniProt10]
UniProt: (in Ref. 2; AA sequence);
Active-Site 373
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;

History:
10/20/97 Gene b3845 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10278; confirmed by SwissProt match.


References

Binstock81: Binstock JF, Schulz H (1981). "Fatty acid oxidation complex from Escherichia coli." Methods Enzymol 1981;71 Pt C;403-11. PMID: 7024730

Campbell03a: Campbell JW, Morgan-Kiss RM, E Cronan J (2003). "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Mol Microbiol 47(3);793-805. PMID: 12535077

Daniels92: Daniels DL, Plunkett G, Burland V, Blattner FR (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 1992;257(5071);771-8. PMID: 1379743

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Nakahigashi90: Nakahigashi K, Inokuchi H (1990). "Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nucleic Acids Res 18(16);4937. PMID: 2204034

Pawar81: Pawar S, Schulz H (1981). "The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli." J Biol Chem 1981;256(8);3894-9. PMID: 7012144

Pramanik79: Pramanik A, Pawar S, Antonian E, Schulz H (1979). "Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli." J Bacteriol 1979;137(1);469-73. PMID: 368024

Ren04: Ren Y, Aguirre J, Ntamack AG, Chu C, Schulz H (2004). "An alternative pathway of oleate beta-oxidation in Escherichia coli involving the hydrolysis of a dead end intermediate by a thioesterase." J Biol Chem 279(12);11042-50. PMID: 14707139

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Yang83a: Yang SY, Schulz H (1983). "The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli." J Biol Chem 1983;258(16);9780-5. PMID: 6350283

Yang90a: 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 1990;265(18);10424-9. PMID: 2191949


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Mon Jul 27, 2015, BIOCYC13A.