Summary: Alcohol dehydrogenase GroES-like domain
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Alcohol dehydrogenase GroES-like domain Provide feedback
This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure [1-2].
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013154
This is the catalytic domain of alcohol dehydrogenases (EC). Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure; a name derived from the superfamily of proteins with a GroES fold. Proteins with a GroES fold structure have a highly conserved hydrophobic core and a glycyl-aspartate dipeptide which is thought to maintain the fold [PUBMED:10556240, PUBMED:8804825].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxidoreductase activity (GO:0016491)|
|Biological process||oxidation-reduction process (GO:0055114)|
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We make a range of alignments for each Pfam-A family:
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Key: available, not generated, — not available.
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Curation and family details
|Seed source:||Pfam-B_7 (Release17.0)|
|Number in seed:||92|
|Number in full:||42970|
|Average length of the domain:||101.00 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||23.28 %|
|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:||7|
|Download:||download the raw HMM for this family|
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The tree shows the occurrence of this domain across different species. More...
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 ADH_N domain has been found. There are 455 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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