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1610  structures 8683  species 0  interactions 124152  sequences 719  architectures

Family: Aldedh (PF00171)

Summary: Aldehyde dehydrogenase family

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This is the Wikipedia entry entitled "Aldehyde dehydrogenase". More...

Aldehyde dehydrogenase Edit Wikipedia article

Aldehyde Dehydrogenase

Aldehyde dehydrogenases are a group of enzymes that catalyse the oxidation (dehydrogenation) of aldehydes. Multiple forms exist in mammals in the cytosol, mitochondria and microsomes. They have been classified as Class 1 (cytosolic), Class 2 (mitochondrial) and Class 3 (tumour and other isozymes). In all three classes constitutive and inducible forms exist.

The overall reaction catalysed by the aldehyde dehydrogenases is:

RCHO + NAD(P)+ + H2O ↔ RCOOH + NAD(P)+ + H+

Aldehyde dehydrogenases have a broad substrate specificity. Oxidation of aldehydes is considered to be generally a detoxification reaction, removing the electrophilic products of alcohol oxidation.

For example, alcohol dehydrogenase oxidizes ethanol to acetaldehyde, responsible for some “hangover” symptoms, and aldehyde dehydrogenase detoxifies this to acetic acid. Similarly aldehyde dehydrogenase detoxifies acrolein, the hepatotoxic metabolite formed from allyl alcohol. However, in the case of 2-butoxyethanol, alcohol and aldehyde dehydrogenases sequentially catalyse the formation of the hematotoxic metabolite, 2-butoxyacetic acid.

Aldehyde dehydrogenases can also behave as esterases, hydrolyzing esters such as para-nitrophenyl acetate.

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Aldehyde dehydrogenase family Provide feedback

This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases P00352 EC: Succinate-semialdehyde dehydrogenase P25526 EC: Lactaldehyde dehydrogenase P25553 EC: Benzaldehyde dehydrogenase P43503 EC: Methylmalonate-semialdehyde dehydrogenase Q02252 EC: Glyceraldehyde-3-phosphate dehydrogenase P81406 EC: Delta-1-pyrroline-5-carboxylate dehydrogenase P30038 EC: Acetaldehyde dehydrogenase P17547 EC: Glutamate-5-semialdehyde dehydrogenase P07004 EC: This family also includes omega crystallin P30842 an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.

Literature references

  1. Steinmetz CG, Xie P, Weiner H, Hurley TD; , Structure 1997;5:701-711.: Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. PUBMED:9195888 EPMC:9195888

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR015590

Aldehyde dehydrogenases ( EC and EC ) are enzymes that oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor. In mammals at least four different forms of the enzyme are known [ PUBMED:2713359 ]: class-1 (or Ald C) a tetrameric cytosolic enzyme, class-2 (or Ald M) a tetrameric mitochondrial enzyme, class- 3 (or Ald D) a dimeric cytosolic enzyme, and class IV a microsomal enzyme. Aldehyde dehydrogenases have also been sequenced from fungal and bacterial species. A number of enzymes are known to be evolutionary related to aldehyde dehydrogenases. A glutamic acid and a cysteine residue have been implicated in the catalytic activity of mammalian aldehyde dehydrogenase. These residues are conserved in all the enzymes of this entry.

Some of the proteins in this entry are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation.

The allergens in this family include allergens with the following designations: Alt a 10 and Cla h 3.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan ALDH-like (CL0099), which has the following description:

The aldehyde dehydrogenases (ALDHs) are a superfamily of multimeric enzymes which catalyse the oxidation of a broad range of aldehydes into their corresponding carboxylic acids with the reduction of their cofactor, NAD(P) into NAD(P)H. The way that the NAD is bound is distinct from other NAD(P)-dependent oxidoreductases. The domain represented by this clan consists of two similar subdomains.

The clan contains the following 4 members:

Aldedh DUF1487 Histidinol_dh LuxC


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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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.

Representative proteomes UniProt
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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Representative proteomes UniProt

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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.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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...


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 View help on the curation process

Seed source: Prosite
Previous IDs: aldedh;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A , Sonnhammer ELL
Number in seed: 89
Number in full: 124152
Average length of the domain: 406.1 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 83.05 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 23.0 23.0
Trusted cut-off 23.0 23.0
Noise cut-off 22.9 22.9
Model length: 462
Family (HMM) version: 25
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 Aldedh domain has been found. There are 1610 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044R6E3 View 3D Structure Click here
A0A044UEP7 View 3D Structure Click here
A0A044UTH7 View 3D Structure Click here
A0A077YZA6 View 3D Structure Click here
A0A077Z029 View 3D Structure Click here
A0A077Z0V3 View 3D Structure Click here
A0A077Z1A2 View 3D Structure Click here
A0A077ZAM5 View 3D Structure Click here
A0A077ZGE9 View 3D Structure Click here
A0A077ZH52 View 3D Structure Click here
A0A077ZHK5 View 3D Structure Click here
A0A077ZKY4 View 3D Structure Click here
A0A077ZLX1 View 3D Structure Click here
A0A0B4K6I6 View 3D Structure Click here
A0A0C4DHC8 View 3D Structure Click here
A0A0D2DAY4 View 3D Structure Click here
A0A0D2DC55 View 3D Structure Click here
A0A0D2DDF9 View 3D Structure Click here
A0A0D2DLR0 View 3D Structure Click here
A0A0D2DLU5 View 3D Structure Click here
A0A0D2DS70 View 3D Structure Click here
A0A0D2DSK0 View 3D Structure Click here
A0A0D2DU32 View 3D Structure Click here
A0A0D2DWQ3 View 3D Structure Click here
A0A0D2DXF0 View 3D Structure Click here
A0A0D2E0P5 View 3D Structure Click here
A0A0D2E2B8 View 3D Structure Click here
A0A0D2E4S4 View 3D Structure Click here
A0A0D2E4T5 View 3D Structure Click here
A0A0D2ELZ6 View 3D Structure Click here
A0A0D2EX05 View 3D Structure Click here
A0A0D2EY66 View 3D Structure Click here
A0A0D2FED2 View 3D Structure Click here
A0A0D2FIQ7 View 3D Structure Click here
A0A0D2G1I0 View 3D Structure Click here
A0A0D2G4M9 View 3D Structure Click here
A0A0D2G736 View 3D Structure Click here
A0A0D2G894 View 3D Structure Click here
A0A0D2G8D0 View 3D Structure Click here
A0A0D2GA90 View 3D Structure Click here