A0A0D2GXJ8 · A0A0D2GXJ8_9EURO
- Protein4-trimethylaminobutyraldehyde dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids498 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency. Catalyzes the oxidation of aldehydes arising from biogenic amines and polyamines.
Catalytic activity
- (5-hydroxyindol-3-yl)acetaldehyde + H2O + NAD+ = (5-hydroxyindol-3-yl)acetate + 2 H+ + NADH
- 3,4-dihydroxyphenylacetaldehyde + H2O + NAD+ = 3,4-dihydroxyphenylacetate + 2 H+ + NADH
- H2O + NAD+ + pentanal = 2 H+ + NADH + pentanoate
- H2O + NAD+ + propanal = 2 H+ + NADH + propanoate
- H2O + NAD+ + spermine monoaldehyde = 2 H+ + N-(2-carboxyethyl)spermidine + NADH
- H2O + hexanal + NAD+ = 2 H+ + hexanoate + NADH
- H2O + imidazole-4-acetaldehyde + NAD+ = 2 H+ + imidazole-4-acetate + NADH
- acrolein + H2O + NAD+ = acrylate + 2 H+ + NADH
- butanal + H2O + NAD+ = butanoate + 2 H+ + NADH
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 252 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aldehyde dehydrogenase (NAD+) activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-trimethylaminobutyraldehyde dehydrogenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Fonsecaea
Accessions
- Primary accessionA0A0D2GXJ8
Proteomes
Organism-specific databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MRLPERHTFYAGKPQPSSTSPGTFSSVDPST | ||||||
Compositional bias | 12-31 | Polar residues | ||||
Sequence: GKPQPSSTSPGTFSSVDPST | ||||||
Domain | 20-482 | Aldehyde dehydrogenase | ||||
Sequence: SPGTFSSVDPSTGKDVCTVHTSSPSAIDSAVVSAKAAFPSWSSTPPIERARILHKAVSILRSRNDELAKIETIDTGKPYSETSTVDIVTGADVLEYFASLVASGGLNGESFRLRDSAWVYTSKEPLGVCVGIGAWNYPIQIALWKSAPCLAAGNTMVYKPSEVTPLHGQFLAEVYKEAGLPDGVFNVVYGAGDVGAYLTKHPVIAKVSFTGQVSTGRKVAGSAAGEMKYVTMELGGKSPVIVLPDVDIEQAVDGAIMANFFSTGQVCTNGTRVFVPKQLKSEFERVLLQKLKYVRPGELMDMNTNFGPLVSKVHYDKVTSYIRHGIEVDKATLLHGGLDQPAHLPAHLRSGYWVQPTVFTDCTDAMRIVKEEIFGPVMAILPYDSLDEAVSRANDTELGLAAGVFGKDINQCHTVIKQLQAGITWVNTWGESPAEMAVGGWKQSGVGVENGRRGLEAWVRNKS |
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length498
- Mass (Da)53,587
- Last updated2015-04-29 v1
- ChecksumA02DE5BB4EDA7C6A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 12-31 | Polar residues | ||||
Sequence: GKPQPSSTSPGTFSSVDPST |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KN846974 EMBL· GenBank· DDBJ | KIW77064.1 EMBL· GenBank· DDBJ | Genomic DNA |