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InterPro: IPR006092 Acyl-CoA dehydrogenase, N-terminal
Protein matches
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UniProtKB Matches: 10500 proteins |
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Accession
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IPR006092 Acyl-CoA_DH_N |
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Secondary
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IPR001552
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Type
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Domain |
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Signatures
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InterPro Relationships
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Parent
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IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal
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Found in
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IPR009100 Acyl-CoA dehydrogenase/oxidase
IPR017616 Pimeloyl-CoA dehydrogenase, small subunit
IPR017617 Pimeloyl-CoA dehydrogenase, large subunit
IPR017620 Cyclohexanecarboxyl-CoA dehydrogenase
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GO Term annotation
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Process
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GO:0055114 oxidation reduction
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Function
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GO:0003995 acyl-CoA dehydrogenase activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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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). These enzymes are homodimers containing one molecule of FAD. The monomeric enzyme is folded into three domains of approximately equal size. The N-terminal and the C-terminal are mainly alpha-helices packed together, and the middle domain consists of two orthogonal beta-sheets. The flavin ring is buried in the crevise between two alpha-helical domains and the beta-sheet of one subunit, and the adenosine pyrophosphate moiety is stretched into the subunit junction with one formed by two C-terminal domains [4]. The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain, on dimerisation, the N-terminal of one molecule extends into the other dimer and lies on the surface of the molecule.
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Structural links
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Database links
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Example proteins
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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 |
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| IPR009075 |
Acyl-CoA dehydrogenase/oxidase C-terminal |
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| IPR013786 |
Acyl-CoA dehydrogenase/oxidase, N-terminal |
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| IPR006092 |
Acyl-CoA dehydrogenase, N-terminal |
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| IPR006090 |
Acyl-CoA oxidase/dehydrogenase, type 1 |
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| IPR006091 |
Acyl-CoA oxidase/dehydrogenase, central domain |
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| IPR013764 |
Acyl-CoA oxidase/dehydrogenase, type1/2, C-terminal |
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| IPR006089 |
Acyl-CoA dehydrogenase, conserved site |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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Publications
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1.
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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]
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2.
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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
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3.
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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
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4.
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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
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Additional Reading
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Fitzpatrick PF, Bozinovski DM, Heroux A, Shaw PG, Valley MP, Orville AM.
Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase.
Biochemistry 46 2007 13800-8
[PubMed: 17994768]
http://dx.doi.org/10.1021/bi701557k
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Nagpal A, Valley MP, Fitzpatrick PF, Orville AM.
Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover.
Biochemistry 45 2006 1138-50
[PubMed: 16430210]
http://dx.doi.org/10.1021/bi051966w
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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
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Fitzpatrick PF, Orville AM, Nagpal A, Valley MP.
Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase.
Arch. Biochem. Biophys. 433 2005 157-65
[PubMed: 15581574]
http://dx.doi.org/10.1016/j.abb.2004.08.021
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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
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Djordjevic S, Pace CP, Stankovich MT, Kim JJ.
Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii.
Biochemistry 34 1995 2163-71
[PubMed: 7857927]
http://dx.doi.org/10.1021/bi00007a009
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InterPro 23.1
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