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InterPro: IPR006089 Acyl-CoA dehydrogenase, conserved site

Protein matches Help

UniProtKB

Matches:

5547 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR006089 Acyl-CoA_DH_CS

Secondary

IPR001552

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00072	ACYL_COA_DH_1	3789
PROSITE pattern	PS00073	ACYL_COA_DH_2	4667
Signatures in BioMart

InterPro Relationships Help

Found in

IPR006090 Acyl-CoA oxidase/dehydrogenase, type 1
IPR006091 Acyl-CoA oxidase/dehydrogenase, central domain
IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal
IPR009100 Acyl-CoA dehydrogenase/oxidase
IPR013764 Acyl-CoA oxidase/dehydrogenase, type1/2, C-terminal

GO Term annotation Help

Process

GO:0055114 oxidation reduction

Function

GO:0003995 acyl-CoA dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

Mammalian Co-A dehydrogenases (EC:1.3.99.3) are enzymes that catalyse the first step in each cycle of beta-oxidation in mitochondion. Acyl-CoA dehydrogenases [1, 2, 3] catalyze the alpha,beta-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. Reoxidation of the flavin involves transfer of electrons to ETF (electron transfering flavoprotein) [4]. These enzymes are homodimers containing one molecule of FAD.

Structural links Help

PDB - click here

SCOP: a.29.3.1 , e.6.1.1

CATH: 1.20.140.10 , 2.40.110.10

Database links Help

PDBe-motif: PS00072 , PS00073

Enzyme: EC:1.3.99

PROSITE doc: PDOC00070

Blocks: IPB006089

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006089

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

P34275 Probable acyl coa dehydrogenase 6

P45952 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Q96329 Acyl-coenzyme A oxidase 4, peroxisomal

Q9VSA3 Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR009100	Acyl-CoA dehydrogenase/oxidase
IPR009075	Acyl-CoA dehydrogenase/oxidase C-terminal
IPR013786	Acyl-CoA dehydrogenase/oxidase, N-terminal
IPR006092	Acyl-CoA dehydrogenase, N-terminal
IPR006090	Acyl-CoA oxidase/dehydrogenase, type 1
IPR006091	Acyl-CoA oxidase/dehydrogenase, central domain
IPR013764	Acyl-CoA oxidase/dehydrogenase, type1/2, C-terminal
IPR006089	Acyl-CoA dehydrogenase, conserved site
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Tanaka K, Ikeda Y, Matsubara Y, Hyman DB. Molecular basis of isovaleric acidemia and medium-chain acyl-CoA dehydrogenase deficiency. Enzyme 38 91-107 1987 [PubMed: 3326738]
2.	Matsubara Y, Indo Y, Naito E, Ozasa H, Glassberg R, Vockley J, Ikeda Y, Kraus J, Tanaka K. Molecular 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. J. Biol. Chem. 264 16321-31 1989 [PubMed: 2777793] http://intl.jbc.org/cgi/reprint/264/27/16321.pdf
3.	Aoyama T, Ueno I, Kamijo T, Hashimoto T. Rat 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. J. Biol. Chem. 269 19088-94 1994 [PubMed: 8034667] http://intl.jbc.org/cgi/reprint/269/29/19088.pdf
4.	Kim JJ, Wang M, Paschke R. Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl. Acad. Sci. U.S.A. 90 7523-7 1993 [PubMed: 8356049] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8356049&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Eichler K, Bourgis F, Buchet A, Kleber HP, Mandrand-Berthelot MA. Molecular characterization of the cai operon necessary for carnitine metabolism in Escherichia coli. Mol. Microbiol. 13 1994 775-86 [PubMed: 7815937] http://dx.doi.org/10.1111/j.1365-2958.1994.tb00470.x
	Rao KS, Fu Z, Albro M, Narayanan B, Baddam S, Lee HJ, Kim JJ, Frerman FE. The effect of a Glu370Asp mutation in glutaryl-CoA dehydrogenase on proton transfer to the dienolate intermediate. Biochemistry 46 2007 14468-77 [PubMed: 18020372] http://dx.doi.org/10.1021/bi7009597
	Toogood HS, van Thiel A, Scrutton NS, Leys D. Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J. Biol. Chem. 280 2005 30361-6 [PubMed: 15975918] http://dx.doi.org/10.1074/jbc.M505562200
	Battaile KP, Nguyen TV, Vockley J, Kim JJ. Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases. J. Biol. Chem. 279 2004 16526-34 [PubMed: 14752098] http://dx.doi.org/10.1074/jbc.M400034200
	Fu Z, Wang M, Paschke R, Rao KS, Frerman FE, Kim JJ. Crystal structures of human glutaryl-CoA dehydrogenase with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry 43 2004 9674-84 [PubMed: 15274622] http://dx.doi.org/10.1021/bi049290c
	Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D. Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex. J. Biol. Chem. 279 2004 32904-12 [PubMed: 15159392] http://dx.doi.org/10.1074/jbc.M404884200

InterPro 23.1