A0A265B4Y1 · A0A265B4Y1_SALET
- ProteinGamma-aminobutyraldehyde dehydrogenase
- GenepatD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids481 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidation 4-aminobutanal (gamma-aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4-aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Miscellaneous
4-aminobutanal can spontaneously cyclize to 1-pyrroline, and 5-aminopentanal to 1-piperideine.
Catalytic activity
- 4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH + 2 H+
- 5-aminopentanal + NAD+ + H2O = 5-aminopentanoate + NADH + 2 H+
Pathway
Amine and polyamine degradation; putrescine degradation; 4-aminobutanoate from 4-aminobutanal: step 1/1.
Amino-acid degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 153-155 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 179-182 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 216 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 232-235 | NAD+ (UniProtKB | ChEBI) | |||
Active site | 253 | ||||
Active site | 287 | Nucleophile | |||
Binding site | 287 | NAD+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aminobutyraldehyde dehydrogenase (NAD+) activity | |
Molecular Function | NAD binding | |
Biological Process | L-lysine catabolic process | |
Biological Process | putrescine catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGamma-aminobutyraldehyde dehydrogenase
- EC number
- Short namesABALDH
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A265B4Y1
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 19-477 | Aldehyde dehydrogenase | |||
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length481
- Mass (Da)51,948
- Last updated2017-12-20 v1
- Checksum6A44022C5049CE71
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHMQS010000006 EMBL· GenBank· DDBJ | EBX9256711.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAAKA010000002 EMBL· GenBank· DDBJ | HAA0832340.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAAKJ010000001 EMBL· GenBank· DDBJ | HAA0876753.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
RUBA01000002 EMBL· GenBank· DDBJ | MKI12708.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP043214 EMBL· GenBank· DDBJ | QEI79483.1 EMBL· GenBank· DDBJ | Genomic DNA |