CATH Domain 6qapD02

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CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.309	Aldehyde Dehydrogenase; Chain A, domain 2
	3.40.309.10	Aldehyde Dehydrogenase; Chain A, domain 2

Domain Context

CATH Clusters

Superfamily	Aldehyde Dehydrogenase; Chain A, domain 2
Functional Family	4-trimethylaminobutyraldehyde dehydrogenase isoform X1

Enzyme Information

1.2.1.3	Aldehyde dehydrogenase (NAD(+)). based on mapping to UniProt P49189 An aldehyde + NAD(+) + H(2)O = a carboxylate + NADH. -!- Wide specificity, including oxidation of D-glucuronolactone to D-glucarate. -!- Formerly EC 1.1.1.70.
1.2.1.19	Aminobutyraldehyde dehydrogenase. based on mapping to UniProt P49189 4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH. -!- The enzyme from some species exhibits broad substrate specificity and has a marked preference for straight-chain aldehydes (up to 7 carbon atoms) as substrates. -!- The plant enzyme also acts on 4-guanidinobutanal (cf. EC 1.2.1.54). -!- As 1-pyrroline and 4-aminobutanal are in equilibrium and can be interconverted spontaneously, 1-pyrroline may act as the starting substrate. -!- Formerly EC 1.5.1.35.
1.2.1.47	4-trimethylammoniobutyraldehyde dehydrogenase. based on mapping to UniProt P49189 4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate + NADH.

UniProtKB Entries (1)

AL9A1_HUMAN

Homo sapiens

4-trimethylaminobutyraldehyde dehydrogenase

PDB Structure

PDB	6QAP
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Kinetic and structural analysis of human ALDH9A1. Koncitikova, R., Vigouroux, A., Kopecna, M., Sebela, M., Morera, S., Kopecny, D. Biosci.Rep.