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PROSITE documentation PDOC00070

Acyl-CoA dehydrogenases signatures

Description:

Acyl-CoA dehydrogenases [1,2,3] are enzymes that catalyze the α,β-dehydrogenation of acyl-CoA esters and transfer electrons to ETF, the electron transfer protein. Acyl-CoA dehydrogenases are FAD flavoproteins. This family currently includes:

We have selected two conserved regions as signature patterns. The first is located in the center of these enzymes, the second in the C-terminal section.

Last update:

December 2004 / Pattern and text revised.

Technical section:

PROSITE methods (with tools and information) covered by this documentation:

ACYL_COA_DH_1, PS00072Acyl-CoA dehydrogenases signature 1  (PATTERN)
Consensus pattern: [GAC] - [LIVM] - [ST] - E - x(2) - [GSAN] - G - [ST] - D - x(2) - [GSA]
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00072
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00072
Scan Swiss-Prot/TrEMBL entries against PS00072
view ligand binding statistics
Matching PDB structures: 1BUC 1EGC 1EGD 1EGE ... [ALL]
ACYL_COA_DH_2, PS00073Acyl-CoA dehydrogenases signature 2  (PATTERN)
Consensus pattern: [QDE] - x - {P} - G - [GS] - x - G - [LIVMFY] - x(2) - [DEN] - x(4) - [KR] - x(3) - [DEN]
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00073
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00073
Scan Swiss-Prot/TrEMBL entries against PS00073
view ligand binding statistics
Matching PDB structures: 1BUC 1EGC 1EGD 1EGE ... [ALL]

References:

1 AuthorsTanaka K., Ikeda Y., Matsubara Y., Hyman D.B.
TitleMolecular basis of isovaleric acidemia and medium-chain acyl-CoA dehydrogenase deficiency.
SourceEnzyme 38:91-107(1987).
PubMed ID3326738
2 AuthorsMatsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
TitleMolecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family.
SourceJ. Biol. Chem. 264:16321-16331(1989).
PubMed ID2777793
3 AuthorsAoyama T., Ueno I., Kamijo T., Hashimoto T.
TitleRat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial acyl-CoA dehydrogenase gene product, is a rate-limiting enzyme in long-chain fatty acid beta-oxidation system. cDNA and deduced amino acid sequence and distinct specificities of the cDNA-expressed protein.
SourceJ. Biol. Chem. 269:19088-19094(1994).
PubMed ID8034667
4 AuthorsEichler K., Bourgis F., Buchet A., Kleber H.-P., Mandrand-Berthelot M.-A.
TitleMolecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli.
SourceMol. Microbiol. 13:775-786(1994).
PubMed ID7815937

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