3-ketoacyl-CoA thiolase (P21151)

Identification
Name:3-ketoacyl-CoA thiolase
Synonyms:
  • Acetyl-CoA acyltransferase
  • Beta-ketothiolase
  • Fatty acid oxidation complex subunit beta
Gene Name:fadA
Enzyme Class:
Biological Properties
General Function:Involved in acetyl-CoA C-acyltransferase activity
Specific Function:Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Benzoate degradation via hydroxylation ec00362
  • Biosynthesis of unsaturated fatty acids ec01040
  • Ethylbenzene degradation ec00642
  • Fatty acid elongation in mitochondria ec00062
  • Fatty acid metabolism ec00071
  • Geraniol degradation ec00281
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
  • Valine, leucine and isoleucine degradation ec00280
  • alpha-Linolenic acid metabolism ec00592
KEGG Reactions:
2.0Thumb ↔ 1.0Thumb+1.0Thumb
2.0Acetyl-CoA ↔ 1.0Acetoacetyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Octanoyl-CoA ↔ 1.03-Oxodecanoyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Tetradecanoyl-CoA ↔ 1.03-Oxohexadecanoyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Hexanoyl-CoA ↔ 1.03-Oxooctanoyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Lauroyl-CoA ↔ 1.03-Oxotetradecanoyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Decanoyl-CoA (N-C10:0CoA) ↔ 1.03-Oxododecanoyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Coenzyme A + 1.03-Oxoadipyl-CoA ↔ 1.0Acetyl-CoA + 1.0Succinyl-CoA
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Succinyl-CoA + 1.0Acetyl-CoA ↔ 1.0Coenzyme A + 1.03-Oxoadipyl-CoA
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Propionyl-CoA + 1.0Acetyl-CoA ↔ 1.0Coenzyme A + 1.02-Methylacetoacetyl-CoA
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1.0Thumb+1.0Butanoyl-CoA ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Butanoyl-CoA ↔ 1.0Coenzyme A + 1.03-Oxohexanoyl-CoA
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1.0Thumb+1.0Chenodeoxycholoyl-CoA ↔ 1.0Thumb+1.0Thumb
1.0Propionyl-CoA + 1.0Chenodeoxycholoyl-CoA ↔ 1.0Coenzyme A + 1.03alpha,7alpha-Dihydroxy-5beta-cholestanoyl-CoA
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.07-Methyl-3-oxo-6-octenoyl-CoA + 1.0Coenzyme A ↔ 1.05-Methylhex-4-enoyl-CoA + 1.0Acetyl-CoA
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05-Methyl-3-oxo-4-hexenoyl-CoA + 1.0Coenzyme A ↔ 1.03-Methylcrotonyl-CoA + 1.0Acetyl-CoA
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1.0Acyl-CoA+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acyl-CoA + 1.0Acetyl-CoA ↔ 1.0Coenzyme A + 1.03-Oxoacyl-CoA
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SMPDB Reactions:
1.03-oxo-opc8-coa → 1.0OPC6-CoA
1.03-oxo-opc8-coa → 1.0OPC6-CoA
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1.03-Oxo-OPC6-CoA → 1.0OPC4-CoA
1.03-Oxo-OPC6-CoA → 1.0OPC4-CoA
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1.03-oxo-opc4-coa → 1.0(+)-7-Isojasmonic acid CoA
1.03-oxo-opc4-coa → 1.0(+)-7-Isojasmonic acid CoA
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1.0a 3-oxoacyl-CoA +1.0Thumb → 1.0Thumb+1.0a 2,3,4-saturated fatty acyl CoA 
1.0a 3-oxoacyl-CoA  + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0a 2,3,4-saturated fatty acyl CoA 
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1.0Acetoacetyl-CoA+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Succinyl-CoA+1.0Thumb
1.0Acetoacetyl-CoA + 1.0Coenzyme A + 1.0Acetoacetyl-CoA → 1.0Acetyl-CoA + 1.0Succinyl-CoA + 1.0Succinyl-CoA
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.03-Oxodecanoyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Lauroyl-CoA
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Octanoyl-CoA+1.0Thumb
1.03-Oxohexanoyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Octanoyl-CoA + 1.0Octanoyl-CoA
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.03-Oxododecanoyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Tetradecanoyl-CoA
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.03-Oxotetradecanoyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Palmityl-CoA
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Decanoyl-CoA (n-C10:0CoA)+1.0Thumb
1.03-Oxooctanoyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Decanoyl-CoA (n-C10:0CoA) + 1.0Decanoyl-CoA (N-C10:0CoA)
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Stearoyl-CoA+1.0Thumb
1.03-Oxohexadecanoyl-CoA + 1.0Coenzyme A → 1.0Acetyl-CoA + 1.0Stearoyl-CoA + 1.0Stearoyl-CoA
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1.03-Oxooctadecanoyl-CoA+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Stearoyl-CoA+1.0Thumb
1.03-Oxooctadecanoyl-CoA + 1.0Coenzyme A + 1.03-Oxooctadecanoyl-CoA → 1.0Acetyl-CoA + 1.0Stearoyl-CoA + 1.0Stearoyl-CoA
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EcoCyc Reactions:
2.0Thumb ↔ 1.0Thumb+1.0Thumb
2.0Acetyl-CoA ↔ 1.0Acetoacetyl-CoA + 1.0Coenzyme A
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Coenzyme A + 1.03-Oxoadipyl-CoA ↔ 1.0Acetyl-CoA + 1.0Succinyl-CoA
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Acetyl-CoA + 1.0Butyryl-CoA ↔ 1.03-Oxohexanoyl-CoA + 1.0Coenzyme A
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.03-Oxooctadecanoyl-CoA + 1.0Coenzyme A ↔ 1.0Acetyl-CoA + 1.0Palmityl-CoA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB011572-Methylacetoacetyl-CoAMetaboCard
ECMDB014933-Methylcrotonyl-CoAMetaboCard
ECMDB200743-Oxo-OPC4-CoAMetaboCard
ECMDB200753-Oxo-OPC6-CoAMetaboCard
ECMDB200773-Oxoadipyl-CoAMetaboCard
ECMDB039393-Oxodecanoyl-CoAMetaboCard
ECMDB039373-Oxododecanoyl-CoAMetaboCard
ECMDB064023-Oxohexadecanoyl-CoAMetaboCard
ECMDB039433-Oxohexanoyl-CoAMetaboCard
ECMDB211703-Oxooctadecanoyl-CoAMetaboCard
ECMDB039413-Oxooctanoyl-CoAMetaboCard
ECMDB039353-Oxotetradecanoyl-CoAMetaboCard
ECMDB021593alpha,7alpha-Dihydroxy-5beta-cholestanoyl-CoAMetaboCard
ECMDB201045-Methyl-3-oxo-4-hexenoyl-CoAMetaboCard
ECMDB201055-Methylhex-4-enoyl-CoAMetaboCard
ECMDB201087-Methyl-3-oxo-6-octenoyl-CoAMetaboCard
ECMDB01484Acetoacetyl-CoAMetaboCard
ECMDB01206Acetyl-CoAMetaboCard
ECMDB20120Benzoyl acetyl-CoAMetaboCard
ECMDB01088Butyryl-CoAMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB06404Decanoyl-CoA (N-C10:0CoA)MetaboCard
ECMDB02845Hexanoyl-CoAMetaboCard
ECMDB03571Lauroyl-CoAMetaboCard
ECMDB01070Octanoyl-CoAMetaboCard
ECMDB01338Palmityl-CoAMetaboCard
ECMDB01275Propionyl-CoAMetaboCard
ECMDB21284Stearoyl-CoAMetaboCard
ECMDB01022Succinyl-CoAMetaboCard
ECMDB01521Tetradecanoyl-CoAMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
acetyl-CoA C-acyltransferase activity
acyltransferase activity
C-acyltransferase activity
catalytic activity
transferase activity
transferase activity, transferring acyl groups
transferase activity, transferring acyl groups other than amino-acyl groups
Process
carboxylic acid metabolic process
cellular metabolic process
fatty acid metabolic process
lipid catabolic process
lipid metabolic process
metabolic process
monocarboxylic acid metabolic process
organic acid metabolic process
oxoacid metabolic process
primary metabolic process
Gene Properties
Blattner:b3845
Gene OrientationCounterclockwise
Centisome Percentage:86.77
Left Sequence End4025632
Right Sequence End4026795
Gene Sequence:
>1164 bp
ATGAACAACTTTAATCTGCACACCCCAACCCGCATTCTGTTTGGTAAAGGCGCAATCGCT
GGTTTACGCGAACAAATTCCTCACGATGCTCGCGTATTGATTACCTACGGCGGCGGCAGC
GTGAAAAAAACCGGCGTTCTCGATCAAGTTCTGGATGCCCTGAAAGGCATGGACGTGCTG
GAATTTGGCGGTATTGAGCCAAACCCGGCTTATGAAACGCTGATGAACGCCGTGAAACTG
GTTCGCGAACAGAAAGTGACTTTCCTGCTGGCGGTTGGCGGCGGTTCTGTACTGGACGGC
ACCAAATTTATCGCCGCAGCGGCTAACTATCCGGAAAATATCGATCCGTGGCACATTCTG
CAAACGGGCGGTAAAGAGATTAAAAGCGCCATCCCGATGGGCTGTGTGCTGACGCTGCCA
GCAACCGGTTCAGAATCCAACGCAGGCGCGGTGATCTCCCGTAAAACCACAGGCGACAAG
CAGGCGTTCCATTCTGCCCATGTTCAGCCGGTATTTGCCGTGCTCGATCCGGTTTATACC
TACACCCTGCCGCCGCGTCAGGTGGCTAACGGCGTAGTGGACGCCTTTGTACACACCGTG
GAACAGTATGTTACCAAACCGGTTGATGCCAAAATTCAGGACCGTTTCGCAGAAGGCATT
TTGCTGACGCTAATCGAAGATGGTCCGAAAGCCCTGAAAGAGCCAGAAAACTACGATGTG
CGCGCCAACGTCATGTGGGCGGCGACTCAGGCGCTGAACGGTTTGATTGGCGCTGGCGTA
CCGCAGGACTGGGCAACGCATATGCTGGGCCACGAACTGACTGCGATGCACGGTCTGGAT
CACGCGCAAACACTGGCTATCGTCCTGCCTGCACTGTGGAATGAAAAACGCGATACCAAG
CGCGCTAAGCTGCTGCAATATGCTGAACGCGTCTGGAACATCACTGAAGGTTCCGATGAT
GAGCGTATTGACGCCGCGATTGCCGCAACCCGCAATTTCTTTGAGCAATTAGGCGTGCCG
ACCCACCTCTCCGACTACGGTCTGGACGGCAGCTCCATCCCGGCTTTGCTGAAAAAACTG
GAAGAGCACGGCATGACCCAACTGGGCGAAAATCATGACATTACGTTGGATGTCAGCCGC
CGTATATACGAAGCCGCCCGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:387
Protein Molecular Weight:40876
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>3-ketoacyl-CoA thiolase
MEQVVIVDAIRTPMGRSKGGAFRNVRAEDLSAHLMRSLLARNPALEAAALDDIYWGCVQQ
TLEQGFNIARNAALLAEVPHSVPAVTVNRLCGSSMQALHDAARMIMTGDAQACLVGGVEH
MGHVPMSHGVDFHPGLSRNVAKAAGMMGLTAEMLARMHGISREMQDAFAARSHARAWAAT
QSAAFKNEIIPTGGHDADGVLKQFNYDEVIRPETTVEALATLRPAFDPVNGMVTAGTSSA
LSDGAAAMLVMSESRAHELGLKPRARVRSMAVVGCDPSIMGYGPVPASKLALKKAGLSAS
DIGVFEMNEAFAAQILPCIKDLGLIEQIDEKINLNGGAIALGHPLGCSGARISTTLLNLM
ERKDVQFGLATMCIGLGQGIATVFERV
References
External Links:
ResourceLink
Uniprot ID:P21151
Uniprot Name:FADA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675815
Ecogene ID:EG10278
Ecocyc:EG10278
ColiBase:b3845
Kegg Gene:b3845
EchoBASE ID:EB0274
CCDB:FADA_ECOLI
BacMap:49176430
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Campbell, J. W., Morgan-Kiss, R. M., Cronan, J. E. Jr (2003). "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway." Mol Microbiol 47:793-805. Pubmed: 12535077
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • DiRusso, C. C. (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 172:6459-6468. Pubmed: 1699931
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Nakahigashi, K., Inokuchi, H. (1990). "Nucleotide sequence of the fadA and fadB genes from Escherichia coli." Nucleic Acids Res 18:4937. Pubmed: 2204034
  • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K., Blattner, F. R., Chaudhuri, R. R., Glasner, J. D., Horiuchi, T., Keseler, I. M., Kosuge, T., Mori, H., Perna, N. T., Plunkett, G. 3rd, Rudd, K. E., Serres, M. H., Thomas, G. H., Thomson, N. R., Wishart, D., Wanner, B. L. (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34:1-9. Pubmed: 16397293
  • Yang, S. Y., Yang, X. Y., 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 265:10424-10429. Pubmed: 2191949