Domain

Aldehyde dehydrogenase N-terminal domain (IPR016162)

Short name: Ald_DH_N

Domain relationships

None.

Description

This entry represents a structural domain found at the N-terminal of aldehyde dehydrogenases [PMID: 12795606]. These proteins contain two similar domains, each with a 3-layer alpha/beta/alpha structure, which probably arose from a duplication; this entry covers the N-terminal a/b/a domain. These enzymes binds NAD differently from other NAD(P)-dependent oxidoreductases.

Aldehyde dehydrogenases (EC:1.2.1.3 and EC:1.2.1.5) 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 [PMID: 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.

This domain is also found in gamma-glutamyl phosphate reductases, also known as glutamate-5-semialdehyde dehydrogenases.

GO terms

Biological Process

GO:0008152 metabolic process
GO:0055114 oxidation-reduction process

Molecular Function

GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
GENE3D