Summary: Zinc-binding dehydrogenase
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Zinc-binding dehydrogenase Provide feedback
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Internal database links
|Similarity to PfamA using HHSearch:||AlaDh_PNT_C Methyltransf_11 Methyltransf_18 ADH_zinc_N_2 Methyltransf_31|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013149Alcohol dehydrogenase (EC) (ADH) catalyzes the reversible oxidation of alcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD:
- Zinc-containing 'long-chain' alcohol dehydrogenases.
- Insect-type, or 'short-chain' alcohol dehydrogenases.
- Iron-containing alcohol dehydrogenases.
- Sorbitol dehydrogenase (EC)
- L-threonine 3-dehydrogenase (EC)
- Glutathione-dependent formaldehyde dehydrogenase (EC)
- Mannitol dehydrogenase (EC)
In addition, this family includes NADP-dependent quinone oxidoreductase (EC), an enzyme found in bacteria (gene qor), in yeast and in mammals where, in some species such as rodents, it has been recruited as an eye lens protein and is known as zeta-crystallin [PUBMED:8486156]. The sequence of quinone oxidoreductase is distantly related to that other zinc-containing alcohol dehydrogenases and it lacks the zinc-ligand residues. The torpedo fish and mammalian synaptic vesicle membrane protein vat-1 is related to qor.
This entry represents the cofactor-binding domain of these enzymes, which is normally found towards the C terminus. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) [PUBMED:12962626, PUBMED:12627956, PUBMED:7602590].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||zinc ion binding (GO:0008270)|
|oxidoreductase activity (GO:0016491)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Number in seed:||108|
|Number in full:||42002|
|Average length of the domain:||125.70 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||28.57 %|
|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:||21|
|Download:||download the raw HMM for this family|
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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 ADH_zinc_N domain has been found. There are 463 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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