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InterPro: IPR016160 Aldehyde dehydrogenase, conserved site

Protein matchesHelp
UniProtKB
Matches:
12126 proteins
AccessionHelp IPR016160 Ald_DH_CS
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011264 Betaine aldehyde dehydrogenase
IPR011407 10-formyltetrahydrofolate dehydrogenase
IPR011408 Aldehyde dehydrogenase predicted, duplicated domain-containing
IPR012394 Aldehyde dehydrogenase NAD(P)-dependent
IPR015590 Aldehyde dehydrogenase
IPR016161 Aldehyde/histidinol dehydrogenase
IPR016162 Aldehyde dehydrogenase, N-terminal
IPR017649 Succinylglutamic semialdehyde dehydrogenase
IPR017749 1-pyrroline dehydrogenase
GO Term annotationHelp
Process GO:0008152 metabolic process
GO:0055114 oxidation reduction
Function GO:0016491 oxidoreductase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 [1]: 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.

Structural linksHelp
PDB - click here
SCOP: c.82.1.1
Database linksHelp
Enzyme: EC:1.2.1
PROSITE doc: PDOC00068

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR016160 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A6ZR27 Aldehyde dehydrogenase 5, mitochondrial

O35945 Aldehyde dehydrogenase, cytosolic 1

O75891 10-formyltetrahydrofolate dehydrogenase

P46562 Putative aldehyde dehydrogenase family 7 member A1 homolog

Q7KW39 Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011407 10-formyltetrahydrofolate dehydrogenase
IPR002376 Formyl transferase, N-terminal
IPR005793 Formyl transferase, C-terminal
IPR016163 Aldehyde dehydrogenase, C-terminal
IPR016162 Aldehyde dehydrogenase, N-terminal
IPR016161 Aldehyde/histidinol dehydrogenase
IPR016160 Aldehyde dehydrogenase, conserved site
IPR015590 Aldehyde dehydrogenase
IPR001555 Phosphoribosylglycinamide formyltransferase, active site
IPR011034 Formyl transferase, C-terminal-like
IPR009081 Acyl carrier protein-like
IPR010061 Methylmalonate-semialdehyde dehydrogenase
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Hempel J, Harper K, Lindahl R.
Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria.
Biochemistry 28 1160-7 1989 [PubMed: 2713359]
http://dx.doi.org/10.1021/bi00429a034

Additional ReadingHelp
Weretilnyk EA, Hanson AD.
Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to salinity and drought.
Proc. Natl. Acad. Sci. U.S.A. 87 1990 2745-9 [PubMed: 2320587]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2320587
Cook RJ, Lloyd RS, Wagner C.
Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase.
J. Biol. Chem. 266 1991 4965-73 [PubMed: 1848231]
http://intl.jbc.org/cgi/content/abstract/266/8/4965
Steele MI, Lorenz D, Hatter K, Park A, Sokatch JR.
Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase.
J. Biol. Chem. 267 1992 13585-92 [PubMed: 1339433]
http://intl.jbc.org/cgi/reprint/267/19/13585.pdf
Guerrero FD, Jones JT, Mullet JE.
Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes.
Plant Mol. Biol. 15 1990 11-26 [PubMed: 1715781]
http://dx.doi.org/10.1007/BF00017720
Hidalgo E, Chen YM, Lin EC, Aguilar J.
Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase.
J. Bacteriol. 173 1991 6118-23 [PubMed: 1917845]
http://jb.asm.org/cgi/content/abstract/173/19/6118
Di Costanzo L, Gomez GA, Christianson DW.
Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity.
J. Mol. Biol. 366 2007 481-93 [PubMed: 17173928]
http://dx.doi.org/10.1016/j.jmb.2006.11.023
Tsybovsky Y, Donato H, Krupenko NI, Davies C, Krupenko SA.
Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases.
Biochemistry 46 2007 2917-29 [PubMed: 17302434]
http://dx.doi.org/10.1021/bi0619573
Larson HN, Zhou J, Chen Z, Stamler JS, Weiner H, Hurley TD.
Structural and functional consequences of coenzyme binding to the inactive asian variant of mitochondrial aldehyde dehydrogenase: roles of residues 475 and 487.
J. Biol. Chem. 282 2007 12940-50 [PubMed: 17327228]
http://dx.doi.org/10.1074/jbc.M607959200
Nordlund I, Shingler V.
Nucleotide sequences of the meta-cleavage pathway enzymes 2-hydroxymuconic semialdehyde dehydrogenase and 2-hydroxymuconic semialdehyde hydrolase from Pseudomonas CF600.
Biochim. Biophys. Acta 1049 1990 227-30 [PubMed: 2194577]
http://dx.doi.org/10.1016/0167-4781(90)90046-5
Lowe ED, Gao GY, Johnson LN, Keung WM.
Structure of daidzin, a naturally occurring anti-alcohol-addiction agent, in complex with human mitochondrial aldehyde dehydrogenase.
J. Med. Chem. 51 2008 4482-7 [PubMed: 18613661]
http://dx.doi.org/10.1021/jm800488j
Inagaki E, Ohshima N, Sakamoto K, Babayeva ND, Kato H, Yokoyama S, Tahirov TH.
New insights into the binding mode of coenzymes: structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 462-5 [PubMed: 17554163]
Krzywicki KA, Brandriss MC.
Primary structure of the nuclear PUT2 gene involved in the mitochondrial pathway for proline utilization in Saccharomyces cerevisiae.
Mol. Cell. Biol. 4 1984 2837-42 [PubMed: 6098824]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=6098824
Niegemann E, Schulz A, Bartsch K.
Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene.
Arch. Microbiol. 160 1993 454-60 [PubMed: 8297211]
http://dx.doi.org/10.1007/BF00245306
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InterPro 23.1