Summary
Enoyl-CoA hydratase/isomerase family
This family contains a diverse set of enzymes including: Enoyl-CoA hydratase (Q13011). Napthoate synthase (P27290). Carnitate racemase (P31551). 3-hydoxybutyryl-CoA dehydratase (P52046). Dodecanoyl-CoA delta-isomerase (P42126).
InterPro entry IPR001753
The crotonase superfamily is comprised of mechanistically diverse proteins that share a conserved trimeric quaternary structure (sometimes a hexamer consisting of a dimer of trimers), the core of which consists of 4 turns of a (beta/beta/alpha)n superhelix. Some enzymes in the superfamily have been shown to display dehalogenase, hydratase, and isomerase activities, while others have been implicated in carbon-carbon bond formation and cleavage as well as the hydrolysis of thioesters PUBMED:11263873. However, these different enzymes share the need to stabilise an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two structurally conserved peptidic NH groups that provide hydrogen bonds to the carbonyl moieties of the acyl-CoA substrates and form an "oxyanion hole". The CoA thioester derivatives bind in a characteristic hooked shape and a conserved tunnel binds the pantetheine group of CoA, which links the 3'-phosphate ADP binding site to the site of reaction PUBMED:17198383. Enzymes in the crotonase superfamily include:
- Enoyl-CoA hydratase (crotonase; ), which catalyses the hydratation of 2-trans-enoyl-CoA into 3-hydroxyacyl-CoA PUBMED:12445775.
- 3-2trans-enoyl-CoA isomerase (or dodecenoyl-CoA isomerise; ), which shifts the 3-double bond of the intermediates of unsaturated fatty acid oxidation to the 2-trans position PUBMED:1958319.
- 3-hydroxbutyryl-CoA dehydratase (crotonase; ), a bacterial enzyme involved in the butyrate/butanol-producing pathway.
- 4-Chlorobenzoyl-CoA dehalogenase (), a Pseudomonas enzyme which catalyses the conversion of 4-chlorobenzoate-CoA to 4-hydroxybenzoate-CoA PUBMED:8679561.
- Dienoyl-CoA isomerise, which catalyses the isomerisation of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA PUBMED:9739087.
- Naphthoate synthase (MenB, or DHNA synthetase; ), a bacterial enzyme involved in the biosynthesis of menaquinone (vitamin K2) PUBMED:16131752.
- Carnitine racemase (gene caiD), which catalyses the reversible conversion of crotonobetaine to L-carnitine in Escherichia coli PUBMED:11551212.
- Methylmalonyl CoA decarboxylase (MMCD; ), which has a hexameric structure (dimer of trimers) PUBMED:10769118.
- Carboxymethylproline synthase (CarB), which is involved in carbapenem biosynthesis PUBMED:16096274.
- 6-oxo camphor hydrolase, which catalyses the desymmetrisation of bicyclic beta-diketones to optically active keto acids PUBMED:15138275.
- The alpha subunit of fatty oxidation complex, a multi-enzyme complex that catalyses the last three reactions in the fatty acid beta-oxidation cycle PUBMED:5229654.
- AUH protein, a bifunctional RNA-binding homologue of enoyl-CoA hydratase PUBMED:11738050.
This entry represents the core domain found in crotonase superfamily members.
Clan
This family is a member of clan ClpP_crotonase (CL0127), which contains the following 9 members:
ACCA Carboxyl_trans CLP_protease ECH MdcE Peptidase_S41 Peptidase_S49 Peptidase_S49_N SDH_sahGene Ontology
| Molecular function | catalytic activity (GO:0003824) |
| Biological process | metabolic process (GO:0008152) |
External database links
| HOMSTRAD: | ech |
| PANDIT: | PF00378 |
| PROSITE: | PDOC00150 |
| SCOP: | 1dub |
| SYSTERS: | ECH |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Family |
| Author: | Finn RD |
| Number in seed: | 13 |
| Number in full: | 10821 |
| Average length of the domain: | 166.70 aa |
| Average identity of full alignment: | 27 % |
| Average coverage of the sequence by the domain: | 47.07 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 170 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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 ECH domain has been found.
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