Long-chain-fatty-acid--CoA ligase (P69451)

Identification
Name:Long-chain-fatty-acid--CoA ligase
Synonyms:
  • Long-chain acyl-CoA synthetase
  • Acyl-CoA synthetase
Gene Name:fadD
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids
Cellular Location:Membrane; Peripheral membrane protein.
SMPDB Pathways:
KEGG Pathways:
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
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Palmitic acid + 1.0Coenzyme A ↔ 1.0Adenosine monophosphate + 1.0Palmityl-CoA + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Long-chain fatty acid+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Acyl-CoA
1.0Adenosine triphosphate + 1.0Long-chain fatty acid + 1.0Coenzyme A ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Acyl-CoA
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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 
ReactionCard
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
ReactionCard
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
ReactionCard
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
ReactionCard
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
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB03945(2E)-Hexadecenoyl-CoAMetaboCard
ECMDB03946(2E)-Tetradecenoyl-CoAMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00482Caprylic acidMetaboCard
ECMDB01423Coenzyme AMetaboCard
ECMDB21204Decanoate (N-C10:0)MetaboCard
ECMDB06404Decanoyl-CoA (N-C10:0CoA)MetaboCard
ECMDB21209Dodecanoate (N-C12:0)MetaboCard
ECMDB21229Hexanoate (N-C6:0)MetaboCard
ECMDB02845Hexanoyl-CoAMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB03571Lauroyl-CoAMetaboCard
ECMDB21427Myristic acidMetaboCard
ECMDB21347Octadecanoate (N-C18:0)MetaboCard
ECMDB21348Octadecenoate (N-C18:1)MetaboCard
ECMDB21260Octadecenoyl-CoA (N-C18:1CoA)MetaboCard
ECMDB01070Octanoyl-CoAMetaboCard
ECMDB00220Palmitic acidMetaboCard
ECMDB21442Palmitoleic acidMetaboCard
ECMDB01338Palmityl-CoAMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB21428Stearic acidMetaboCard
ECMDB21284Stearoyl-CoAMetaboCard
ECMDB21361tetradecanoate (n-C14:0)MetaboCard
ECMDB01521Tetradecanoyl-CoAMetaboCard
ECMDB21362Tetradecenoate (N-C14:1)MetaboCard
ECMDB21443Vaccenic acidMetaboCard
GO Classification:
Function
catalytic activity
Process
metabolic process
Gene Properties
Blattner:b1805
Gene OrientationCounterclockwise
Centisome Percentage:40.65
Left Sequence End1886085
Right Sequence End1887770
Gene Sequence:
>1686 bp
TTGAAGAAGGTTTGGCTTAACCGTTATCCCGCGGACGTTCCGACGGAGATCAACCCTGAC
CGTTATCAATCTCTGGTAGATATGTTTGAGCAGTCGGTCGCGCGCTACGCCGATCAACCT
GCGTTTGTGAATATGGGGGAGGTAATGACCTTCCGCAAGCTGGAAGAACGCAGTCGCGCG
TTTGCCGCTTATTTGCAACAAGGGTTGGGGCTGAAGAAAGGCGATCGCGTTGCGTTGATG
ATGCCTAATTTATTGCAATATCCGGTGGCGCTGTTTGGCATTTTGCGTGCCGGGATGATC
GTCGTAAACGTTAACCCGTTGTATACCCCGCGTGAGCTTGAGCATCAGCTTAACGATAGC
GGCGCATCGGCGATTGTTATCGTGTCTAACTTTGCTCACACACTGGAAAAAGTGGTTGAT
AAAACCGCCGTTCAGCACGTAATTCTGACCCGTATGGGCGATCAGCTATCTACGGCAAAA
GGCACGGTAGTCAATTTCGTTGTTAAATACATCAAGCGTTTGGTGCCGAAATACCATCTG
CCAGATGCCATTTCATTTCGTAGCGCACTGCATAACGGCTACCGGATGCAGTACGTCAAA
CCCGAACTGGTGCCGGAAGATTTAGCTTTTCTGCAATACACCGGCGGCACCACTGGTGTG
GCGAAAGGCGCGATGCTGACTCACCGCAATATGCTGGCGAACCTGGAACAGGTTAACGCG
ACCTATGGTCCGCTGTTGCATCCGGGCAAAGAGCTGGTGGTGACGGCGCTGCCGCTGTAT
CACATTTTTGCCCTGACCATTAACTGCCTGCTGTTTATCGAACTGGGTGGGCAGAACCTG
CTTATCACTAACCCGCGCGATATTCCAGGGTTGGTAAAAGAGTTAGCGAAATATCCGTTT
ACCGCTATCACGGGCGTTAACACCTTGTTCAATGCGTTGCTGAACAATAAAGAGTTCCAG
CAGCTGGATTTCTCCAGTCTGCATCTTTCCGCAGGCGGTGGGATGCCAGTGCAGCAAGTG
GTGGCAGAGCGTTGGGTGAAACTGACCGGACAGTATCTGCTGGAAGGCTATGGCCTTACC
GAGTGTGCGCCGCTGGTCAGCGTTAACCCATATGATATTGATTATCATAGTGGTAGCATC
GGTTTGCCGGTGCCGTCGACGGAAGCCAAACTGGTGGATGATGATGATAATGAAGTACCA
CCAGGTCAACCGGGTGAGCTTTGTGTCAAAGGACCGCAGGTGATGCTGGGTTACTGGCAG
CGTCCCGATGCTACCGATGAAATCATCAAAAATGGCTGGTTACACACCGGCGACATCGCG
GTAATGGATGAAGAAGGATTCCTGCGCATTGTCGATCGTAAAAAAGACATGATTCTGGTT
TCCGGTTTTAACGTCTATCCCAACGAGATTGAAGATGTCGTCATGCAGCATCCTGGCGTA
CAGGAAGTCGCGGCTGTTGGCGTACCTTCCGGCTCCAGTGGTGAAGCGGTGAAAATCTTC
GTAGTGAAAAAAGATCCATCGCTTACCGAAGAGTCACTGGTGACTTTTTGCCGCCGTCAG
CTCACGGGATACAAAGTACCGAAGCTGGTGGAGTTTCGTGATGAGTTACCGAAATCTAAC
GTCGGAAAAATTTTGCGACGAGAATTACGTGACGAAGCGCGCGGCAAAGTGGACAATAAA
GCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:561
Protein Molecular Weight:62332
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Long-chain-fatty-acid--CoA ligase
MKKVWLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRA
FAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDS
GASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYHL
PDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA
TYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPF
TAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLT
ECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQ
RPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGV
QEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSN
VGKILRRELRDEARGKVDNKA
References
External Links:
ResourceLink
Uniprot ID:P69451
Uniprot Name:LCFA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1736438
Ecogene ID:EG11530
Ecocyc:EG11530
ColiBase:b1805
Kegg Gene:b1805
EchoBASE ID:EB1492
CCDB:LCFA_ECOLI
BacMap:16129759
General Reference:
  • Black, P. N., DiRusso, C. C., Metzger, A. K., Heimert, T. L. (1992). "Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase." J Biol Chem 267:25513-25520. Pubmed: 1460045
  • 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
  • Fulda, M., Heinz, E., Wolter, F. P. (1994). "The fadD gene of Escherichia coli K12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family." Mol Gen Genet 242:241-249. Pubmed: 8107670
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., 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., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Weimar, J. D., DiRusso, C. C., Delio, R., Black, P. N. (2002). "Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids. Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport." J Biol Chem 277:29369-29376. Pubmed: 12034706