Short-chain-fatty-acid--CoA ligase (P38135)

Identification
Name:Short-chain-fatty-acid--CoA ligase
Synonyms:
  • Acyl-CoA synthetase
Gene Name:fadK
Enzyme Class:Not Available
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It has a low activity on medium or long chain fatty acids and is maximally active on C6 and C8 substrates
Cellular Location:Membrane; Peripheral membrane protein.
SMPDB Pathways:
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0Palmitic acid → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Palmityl-CoA + 1.0Pyrophosphate
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SMPDB Reactions:
1.0Thumb+1.0a 2,3,4- saturated fatty acid+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0a 2,3,4-saturated fatty acyl CoA 
1.0Coenzyme A + 1.0a 2,3,4- saturated fatty acid + 1.0Adenosine triphosphate → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0a 2,3,4-saturated fatty acyl CoA 
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Butyryl-CoA+1.0Thumb
1.0Butyric acid + 1.0Coenzyme A + 1.0Adenosine triphosphate → 1.0Adenosine triphosphate + 1.0Butyryl-CoA + 1.0Butyryl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Decanoyl-CoA (n-C10:0CoA)+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Capric acid → 1.0Adenosine monophosphate + 1.0Decanoyl-CoA (n-C10:0CoA) + 1.0Decanoyl-CoA (N-C10:0CoA)
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Hexanyl-CoA
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Caproic acid → 1.0Adenosine monophosphate + 1.0Hexanyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Dodecanoic acid + 1.0Coenzyme A + 1.0Adenosine triphosphate → 1.0Adenosine monophosphate + 1.0Lauroyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Myristic acid + 1.0Coenzyme A + 1.0Adenosine triphosphate → 1.0Adenosine monophosphate + 1.0Tetradecanoyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Octanoyl-CoA+1.0Thumb
1.0Caprylic acid + 1.0Adenosine triphosphate + 1.0Coenzyme A → 1.0Adenosine monophosphate + 1.0Octanoyl-CoA + 1.0Octanoyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Palmitic acid + 1.0Coenzyme A + 1.0Adenosine triphosphate → 1.0Adenosine monophosphate + 1.0Palmityl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Stearoyl-CoA+1.0Thumb
1.0Stearic acid + 1.0Adenosine triphosphate + 1.0Coenzyme A → 1.0Adenosine monophosphate + 1.0Stearoyl-CoA + 1.0Stearoyl-CoA
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Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Dodecanoate (N-C12:0) + 1.0Hydrogen ion → 1.0Adenosine monophosphate + 1.0Lauroyl-CoA + 1.0Hydrogen ion + 1.0Pyrophosphate
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0Octadecanoate (N-C18:0) → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate + 1.0Stearoyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0tetradecanoate (n-C14:0) → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate + 1.0Tetradecanoyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0Tetradecenoate (N-C14:1) → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate + 1.0(2E)-Tetradecenoyl-CoA
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Decanoate (N-C10:0) + 1.0Hydrogen ion → 1.0Adenosine monophosphate + 1.0Decanoyl-CoA (N-C10:0CoA) + 1.0Hydrogen ion + 1.0Pyrophosphate
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0Caprylic acid → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Octanoyl-CoA + 1.0Pyrophosphate
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0Hexanoate (N-C6:0) → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Hexanoyl-CoA + 1.0Pyrophosphate
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1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Coenzyme A + 1.0Hydrogen ion + 1.0Octadecenoate (N-C18:1) → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0Octadecenoyl-CoA (N-C18:1CoA) + 1.0Pyrophosphate
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Metabolites:
ECMDB IDNameView
ECMDB03945(2E)-Hexadecenoyl-CoAMetaboCard
ECMDB03946(2E)-Tetradecenoyl-CoAMetaboCard
ECMDB214183-Hydroxybutyric acidMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00039Butyric acidMetaboCard
ECMDB01088Butyryl-CoAMetaboCard
ECMDB24048Capric acidMetaboCard
ECMDB24049Caproic acidMetaboCard
ECMDB00482Caprylic acidMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21204Decanoate (N-C10:0)MetaboCard
ECMDB06404Decanoyl-CoA (N-C10:0CoA)MetaboCard
ECMDB21209Dodecanoate (N-C12:0)MetaboCard
ECMDB24050Dodecanoic acidMetaboCard
ECMDB21229Hexanoate (N-C6:0)MetaboCard
ECMDB02845Hexanoyl-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21402Isobutyryl-CoAMetaboCard
ECMDB03571Lauroyl-CoAMetaboCard
ECMDB21427Myristic acidMetaboCard
ECMDB21347Octadecanoate (N-C18:0)MetaboCard
ECMDB21348Octadecenoate (N-C18:1)MetaboCard
ECMDB21260Octadecenoyl-CoA (N-C18:1CoA)MetaboCard
ECMDB01070Octanoyl-CoAMetaboCard
ECMDB00220Palmitic acidMetaboCard
ECMDB01338Palmityl-CoAMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB21428Stearic acidMetaboCard
ECMDB21284Stearoyl-CoAMetaboCard
ECMDB21361tetradecanoate (n-C14:0)MetaboCard
ECMDB01521Tetradecanoyl-CoAMetaboCard
ECMDB21362Tetradecenoate (N-C14:1)MetaboCard
GO Classification:
Function
catalytic activity
Process
metabolic process
Gene Properties
Blattner:b1701
Gene OrientationClockwise
Centisome Percentage:38.39
Left Sequence End1781055
Right Sequence End1782701
Gene Sequence:
>1647 bp
ATGGCAGCTAAAGACGTAAAATTCGGTAACGACGCTCGTGTGAAAATGCTGCGCGGCGTA
AACGTACTGGCAGATGCAGTGAAAGTTACCCTCGGTCCAAAAGGCCGTAACGTAGTTCTG
GATAAATCTTTCGGTGCACCGACCATCACCAAAGATGGTGTTTCCGTTGCTCGTGAAATC
GAACTGGAAGACAAGTTCGAAAATATGGGTGCGCAGATGGTGAAAGAAGTTGCCTCTAAA
GCAAACGACGCTGCAGGCGACGGTACCACCACTGCAACCGTACTGGCTCAGGCTATCATC
ACTGAAGGTCTGAAAGCTGTTGCTGCGGGCATGAACCCGATGGACCTGAAACGTGGTATC
GACAAAGCGGTTACCGCTGCAGTTGAAGAACTGAAAGCGCTGTCCGTACCATGCTCTGAC
TCTAAAGCGATTGCTCAGGTTGGTACCATCTCCGCTAACTCCGACGAAACCGTAGGTAAA
CTGATCGCTGAAGCGATGGACAAAGTCGGTAAAGAAGGCGTTATCACCGTTGAAGACGGT
ACCGGTCTGCAGGACGAACTGGACGTGGTTGAAGGTATGCAGTTCGACCGTGGCTACCTG
TCTCCTTACTTCATCAACAAGCCGGAAACTGGCGCAGTAGAACTGGAAAGCCCGTTCATC
CTGCTGGCTGACAAGAAAATCTCCAACATCCGCGAAATGCTGCCGGTTCTGGAAGCTGTT
GCCAAAGCAGGCAAACCGCTGCTGATCATCGCTGAAGATGTAGAAGGCGAAGCGCTGGCA
ACTCTGGTTGTTAACACCATGCGTGGCATCGTGAAAGTCGCTGCGGTTAAAGCACCGGGC
TTCGGCGATCGTCGTAAAGCTATGCTGCAGGATATCGCAACCCTGACTGGCGGTACCGTG
ATCTCTGAAGAGATCGGTATGGAGCTGGAAAAAGCAACCCTGGAAGACCTGGGTCAGGCT
AAACGTGTTGTGATCAACAAAGACACCACCACTATCATCGATGGCGTGGGTGAAGAAGCT
GCAATCCAGGGCCGTGTTGCTCAGATCCGTCAGCAGATTGAAGAAGCAACTTCTGACTAC
GACCGTGAAAAACTGCAGGAACGCGTAGCGAAACTGGCAGGCGGCGTTGCAGTTATCAAA
GTGGGTGCTGCTACCGAAGTTGAAATGAAAGAGAAAAAAGCACGCGTTGAAGATGCCCTG
CACGCGACCCGTGCTGCGGTAGAAGAAGGCGTGGTTGCTGGTGGTGGTGTTGCGCTGATC
CGCGTAGCGTCTAAACTGGCTGACCTGCGTGGTCAGAACGAAGACCAGAACGTGGGTATC
AAAGTTGCACTGCGTGCAATGGAAGCTCCGCTGCGTCAGATCGTATTGAACTGCGGCGAA
GAACCGTCTGTTGTTGCTAACACCGTTAAAGGCGGCGACGGCAACTACGGTTACAACGCA
GCAACCGAAGAATACGGCAACATGATCGACATGGGTATCCTGGATCCAACCAAAGTAACT
CGTTCTGCTCTGCAGTACGCAGCTTCTGTGGCTGGCCTGATGATCACCACCGAATGCATG
GTTACCGACCTGCCGAAAAACGATGCAGCTGACTTAGGCGCTGCTGGCGGTATGGGCGGC
ATGGGTGGCATGGGCGGCATGATGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:548
Protein Molecular Weight:60773
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Short-chain-fatty-acid--CoA ligase
MKVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAA
SCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVSVPLLPSWREAELVWVLNK
CQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADNTSLT
TAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGH
ATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCMLGATPFVYDLLNVLEKQPA
DLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTDGY
AAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPELTARALDEEGWYYSGDLCR
MDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMSDERLGERSCAYV
VLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTTSGKIQKFLLRKDIMRRLT
QDVCEEIE
References
External Links:
ResourceLink
Uniprot ID:P38135
Uniprot Name:FADK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676895
Ecogene ID:EG12357
Ecocyc:EG12357
ColiBase:b1701
Kegg Gene:b1701
EchoBASE ID:EB2260
CCDB:FADK_ECOLI
BacMap:145698273
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Borodovsky, M., Rudd, K. E., Koonin, E. V. (1994). "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Nucleic Acids Res 22:4756-4767. Pubmed: 7984428
  • 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
  • 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
  • Morgan-Kiss, R. M., Cronan, J. E. (2004). "The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase." J Biol Chem 279:37324-37333. Pubmed: 15213221