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InterPro: IPR016162 Aldehyde dehydrogenase, N-terminal

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16829 proteins

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Accession

IPR016162 Ald_DH_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.605.10	Aldehyde_dehydrogenase_N	16829
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000965 Gamma-glutamyl phosphate reductase GPR
IPR005766 Delta l-pyrroline-5-carboxylate synthetase
IPR005931 Delta-1-pyrroline-5-carboxylate dehydrogenase 1
IPR005932 Delta-1-pyrroline-5-carboxylate dehydrogenase 2
IPR005933 Delta-1-pyrroline-5-carboxylate dehydrogenase 3
IPR010061 Methylmalonate-semialdehyde dehydrogenase
IPR010102 Succinic semialdehyde dehydrogenase
IPR011264 Betaine aldehyde dehydrogenase
IPR011407 10-formyltetrahydrofolate dehydrogenase
IPR011408 Aldehyde dehydrogenase predicted, duplicated domain-containing
IPR011966 Phenylacetic acid degradation protein paaN
IPR011975 Phenylacetic acid degradation protein paaN2
IPR011985 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase
IPR012079 Bifunctional aldehyde/alcohol dehydrogenase
IPR012134 Glutamate-5-semialdehyde dehydrogenase
IPR012394 Aldehyde dehydrogenase NAD(P)-dependent
IPR012408 Acetaldehyde/propionaldehyde dehydrogenase, EutE/PduP-related
IPR013357 Acetaldehyde dehydrogenase, acetylating
IPR015590 Aldehyde dehydrogenase
IPR016161 Aldehyde/histidinol dehydrogenase
IPR017628 2-hydroxymuconic semialdehyde dehydrogenase
IPR017649 Succinylglutamic semialdehyde dehydrogenase
IPR017656 Putative phosphonoacetaldehyde dehydrogenase
IPR017749 1-pyrroline dehydrogenase

Contains

IPR016160 Aldehyde dehydrogenase, conserved site

GO Term annotation Help

Process

GO:0008152 metabolic process
GO:0055114 oxidation reduction

Function

GO:0016491 oxidoreductase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents a structural domain found at the N-terminal of aldehyde dehydrogenases [1]. 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 [2]: 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.

Structural links Help

PDB - click here

SCOP: c.82.1.1

CATH: 3.40.309.10 , 3.40.605.10

Database links Help

Enzyme: EC:1.2.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR016162

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35945 Aldehyde dehydrogenase, cytosolic 1

O75891 10-formyltetrahydrofolate dehydrogenase

P46562 Putative aldehyde dehydrogenase family 7 member A1 homolog

P54885 Gamma-glutamyl phosphate reductase

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
IPR000965	Gamma-glutamyl phosphate reductase GPR
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
IPR020593	Gamma-glutamyl phosphate reductase GPR, conserved site
IPR012134	Glutamate-5-semialdehyde dehydrogenase
IPR009081	Acyl carrier protein-like
IPR010061	Methylmalonate-semialdehyde dehydrogenase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Perez-Miller SJ, Hurley TD. Coenzyme isomerization is integral to catalysis in aldehyde dehydrogenase. Biochemistry 42 7100-9 2003 [PubMed: 12795606] http://dx.doi.org/10.1021/bi034182w
2.	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 Reading Open in usermanual
	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
	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
	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
	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]

InterPro 23.1