spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR012394 Aldehyde dehydrogenase NAD(P)-dependent

Protein matchesHelp
UniProtKB
Matches:
1093 proteins
AccessionHelp IPR012394 Aldehyde_DH_NAD(P)
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR015590 Aldehyde dehydrogenase
IPR016160 Aldehyde dehydrogenase, conserved site
IPR016162 Aldehyde dehydrogenase, N-terminal
GO Term annotationHelp
Process GO:0006081 cellular aldehyde metabolic process
GO:0055114 oxidation reduction
Function GO:0004030 aldehyde dehydrogenase [NAD(P)+] activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Aldehydes are produced as intermediates during the metabolism of many different compounds including amino acids, carbohydrates, lipids vitamins and steroids [1]. They are highly reactive compounds whose buildup to excess levels can cause cytotoxic, genotoxic and carcinogenic effects. Aldehyde dehydrogenases oxidise these compounds to their respective carboxylic acids. This is necessary both for the operation of these metabolic pathways, and to prevent the concentration of aldehydes within the cell from reaching toxic levels. Proteins in this entry are NAD(P)-dependent aldehyde dehydrogenases, found in a variety of organisms, including general aldehyde dehydrogensases (EC:1.2.1.5), fatty aldehyde dehydrogenases (EC:1.2.1.3), and coniferyl aldehyde dehydrogenase (EC:1.2.1.68). Structural studies of the Rattus norvegicus protein (P11883) show that this enzyme is a homodimer where each subunit consists of two alpha-beta-alpha domains [2]. The mode of NAD binding differs substantially from that commonly associated with the Rossman fold.

Structural linksHelp
SCOP: c.82.1.1
Database linksHelp
Enzyme: EC:1.2.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012394 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O86447 Coniferyl aldehyde dehydrogenase

P30838 Aldehyde dehydrogenase, dimeric NADP-preferring

P47739 Aldehyde dehydrogenase, dimeric NADP-preferring

Q04458 Putative fatty aldehyde dehydrogenase HFD1

Q70DU8 Aldehyde dehydrogenase family 3 member H1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR015590 Aldehyde dehydrogenase
IPR016162 Aldehyde dehydrogenase, N-terminal
IPR016161 Aldehyde/histidinol dehydrogenase
IPR016160 Aldehyde dehydrogenase, conserved site
IPR012394 Aldehyde dehydrogenase NAD(P)-dependent
SWISS-MODEL
ModBase

PublicationsHelp
1. Vasiliou V, Pappa A, Petersen DR.
Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism.
Chem. Biol. Interact. 129 1-19 2000 [PubMed: 11154732]
http://dx.doi.org/10.1016/S0009-2797(00)00211-8
2. Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC.
The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold.
Nat. Struct. Biol. 4 317-26 1997 [PubMed: 9095201]
http://dx.doi.org/10.1038/nsb0497-317

spacer
spacer
InterPro 23.1