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InterPro: IPR003361 Acetaldehyde dehydrogenase

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UniProtKB

Matches:

333 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR003361 Acetaldehyde_dehydrogenase

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF015689	Actaldh_dh_actl	313
PANTHER	PTHR21123	Acetylald_dh	330
TIGRFAMs	TIGR03215	ac_ald_DH_ac	319
Signatures in BioMart

InterPro Relationships Help

Contains

IPR000534 Semialdehyde dehydrogenase, NAD-binding
IPR015426 Acetaldehyde dehydrogenase, C-terminal

GO Term annotation Help

Process

GO:0019439 aromatic compound catabolic process
GO:0055114 oxidation reduction

Function

GO:0008774 acetaldehyde dehydrogenase (acetylating) activity

InterPro annotation

Entry Details in BioMart

Abstract

The acetaldehyde dehydrogenase family (EC:1.2.1.10) of bacterial enzymes catalyse the formation of acetyl-CoA from acetaldehyde in the 3-hydroxyphenylpropinoate degradation pathway. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate [1].

Members of this entry heterodimerise with members of IPR000891 to form a bifunctional aldolase-dehydrogenase [2].

Members of this protein family are acetaldehyde dehydrogenase (acetylating), EC:1.2.1.10. This enzyme oxidizes acetaldehyde, using NAD(+), and attaches coenzyme A (CoA), yielding acetyl-CoA., etc.

Structural links Help

PDB - click here

SCOP: c.2.1.3 , d.81.1.1

CATH: 3.30.360.10 , 3.40.50.720

Database links Help

CluSTr: ALLvsALL:8381:51.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003361

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A0PR19 Acetaldehyde dehydrogenase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015426	Acetaldehyde dehydrogenase, C-terminal
IPR016040	NAD(P)-binding domain
IPR003361	Acetaldehyde dehydrogenase
IPR000534	Semialdehyde dehydrogenase, NAD-binding
	SWISS-MODEL

Publications Open in usermanual
1.	Shingler V, Powlowski J, Marklund U. Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600. J. Bacteriol. 174 711-24 1992 [PubMed: 1732207] http://jb.asm.org/cgi/content/abstract/174/3/711
2.	Manjasetty BA, Powlowski J, Vrielink A. Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate. Proc. Natl. Acad. Sci. U.S.A. 100 6992-7 2003 [PubMed: 12764229] http://dx.doi.org/10.1073/pnas.1236794100

InterPro 23.1