Summary: Trans-2-enoyl-CoA reductase catalytic region
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Trans-2-enoyl-CoA reductase catalytic region Provide feedback
This family of trans-2-enoyl-CoA reductases, EC:126.96.36.199, carries the the catalytic sites of the enzyme, characterised by the conserved sequence motifs: YNThhhFxK, and YShAPxR. In Euglena where the enzyme has been characterised it catalyses the reduction of enoyl-CoA to acyl-CoA in an unusual fatty acid pathway in mitochondria. the whole path performs a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation.
Hoffmeister M, Piotrowski M, Nowitzki U, Martin W;, J Biol Chem. 2005;280:4329-4338.: Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis. PUBMED:15569691 EPMC:15569691
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|Similarity to PfamA using HHSearch:||adh_short_C2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024910
This entry represents a putative catalytic domain of trans-2-enoyl-CoA reductases, EC:188.8.131.52. In Euglena where the enzyme has been characterised it catalyses the reduction of enoyl-CoA to acyl-CoA in an unusual fatty acid pathway in mitochondria. The whole path performs a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation[PUBMED:15569691].
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Curation and family details
|Seed source:||Pfam-B_10602 (release 10.0)|
|Author:||Vella Briffa B, Coggill P|
|Number in seed:||49|
|Number in full:||655|
|Average length of the domain:||236.20 aa|
|Average identity of full alignment:||56 %|
|Average coverage of the sequence by the domain:||59.63 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Enoyl_reductase domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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