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InterPro: IPR016160 Aldehyde dehydrogenase, conserved site
Protein matches
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UniProtKB Matches: 12126 proteins |
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Accession
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IPR016160 Ald_DH_CS |
Type
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Conserved_site |
Signatures
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InterPro Relationships
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Found in
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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
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GO Term annotation
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Process
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GO:0008152 metabolic process
GO:0055114 oxidation reduction
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Function
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GO:0016491 oxidoreductase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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.
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Structural links
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Database links
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Example proteins
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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 |
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| IPR002376 |
Formyl transferase, N-terminal |
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| IPR005793 |
Formyl transferase, C-terminal |
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| IPR016163 |
Aldehyde dehydrogenase, C-terminal |
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| IPR016162 |
Aldehyde dehydrogenase, N-terminal |
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| IPR016161 |
Aldehyde/histidinol dehydrogenase |
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| IPR016160 |
Aldehyde dehydrogenase, conserved site |
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| IPR015590 |
Aldehyde dehydrogenase |
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| IPR001555 |
Phosphoribosylglycinamide formyltransferase, active site |
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| IPR011034 |
Formyl transferase, C-terminal-like |
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| IPR009081 |
Acyl carrier protein-like |
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| IPR010061 |
Methylmalonate-semialdehyde dehydrogenase |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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Publications
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1.
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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
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Additional Reading
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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]
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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
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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
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