Summary: Dehydratase small subunit
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Dehydratase small subunit Provide feedback
This family contains the small subunit of the trimeric diol dehydratases and glycerol dehydratases. These enzymes are produced by some enterobacteria in response to growth substances.
Literature references
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Tobimatsu T, Azuma M, Hayashi S, Nishimoto K, Toraya T; , Biosci Biotechnol Biochem 1998;62:1774-1777.: Molecular cloning, sequencing and characterization of the genes for adenosylcobalamin-dependent diol dehydratase of Klebsiella pneumoniae. PUBMED:9805380 EPMC:9805380
Internal database links
| SCOOP: | Ferritin |
External database links
| PANDIT: | PF02287 |
| Pseudofam: | PF02287 |
| SCOP: | 1dio |
| SYSTERS: | Dehydratase_SU |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003207
Diol dehydratase (EC) and glycerol dehydratase (EC) are two iso-functional enzymes that can each catalyse the conversion of 1,2-propanediol, 1,2-ethanediol and glycerol to the corresponding deoxy aldehydes (propionaldehyde, acetaldehyde and 3-hydroxypropionaldehyde, respectively). This reaction proceeds by a radical mechanism involving coenzyme B12 (adenosylcobalamin, AdoCbl) as an essential cofactor. Even though they catalyse the same reaction, these two enzymes (1) differ in their substrate preferences (diol dehydratase has a higher affinity for 1,2-propanediol and glycerol dehydratase for glycerol [PUBMED:1267798]); (2) they participate in different pathways (dihydroxyacetone [DHA] pathway for glycerol dehydratase and 1,2-propanediol degradation pathway for diol dehydratase); and (3) in those organisms where both enzymes are produced (such as Klebsiella and Citrobacter), the genes for them are independently regulated: glycerol dehydratase is induced when Klebsiella pneumoniae grows in glycerol-containing medium, whereas diol dehydratase is fully induced when it grows in propane-1,2-diol-containing medium, but only slightly in the glycerol medium [PUBMED:210157, PUBMED:12230560].
Crystal structures, mechanism of action and structure-function relationship with the coenzyme B12 have been extensively studied for these enzymes [PUBMED:10949584]. Diol/glycerol dehydratases undergo inactivation during catalysis and require a reactivating factor. Propanediol dehydratase was found to be associated with and is believed to be encased in the proteinaceous shell of polyhedral organelles [PUBMED:10498708].
Both diol dehydratase and glycerol dehydratase comprise three subunits: PduC/PduD/PduE or PddA/PddB/PddC for propanediol dehydratase, and GldA/Gld/B/GldC or DhaB/DhaC/DhaE for glycerol dehydratase. This entry represents the small subunit PduE/PddC/GldC/DhaE.
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
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (17) |
Full (370) |
Representative proteomes | NCBI (205) |
Meta (7) |
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| RP15 (14) |
RP35 (25) |
RP55 (34) |
RP75 (44) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (17) |
Full (370) |
Representative proteomes | NCBI (205) |
Meta (7) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (14) |
RP35 (25) |
RP55 (34) |
RP75 (44) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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 HMMER3.
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's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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: | Pfam-B_6588 (release 5.2) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Mian N, Bateman A |
| Number in seed: | 17 |
| Number in full: | 370 |
| Average length of the domain: | 135.80 aa |
| Average identity of full alignment: | 66 % |
| Average coverage of the sequence by the domain: | 81.96 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 137 | ||||||||||||
| Family (HMM) version: | 10 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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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 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 Dehydratase_SU domain has been found. There are 20 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence