Q3TG52 · Q3TG52_MOUSE
- Protein4-trimethylaminobutyraldehyde dehydrogenase
- GeneAldh9a1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids518 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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
Pathway
Amine and polyamine biosynthesis; carnitine biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 278 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
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 > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3TG52
Organism-specific databases
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MILGAVGSVLTSLLRIHRAAA | ||||||
Chain | PRO_5004229467 | 22-518 | 4-trimethylaminobutyraldehyde dehydrogenase | |||
Sequence: VAAMSTGTFVVSQPLNYRGGARVEPVDASGTEKAFEPATGRVIATFACSGEKEVNLAVENAKAAFKLWSKKSGLERCQVLLEAARIIKERKDEIATVETINNGKSIFEARLDVDTCWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIACWKSAPALACGNAMIFKPSPFTPVSALLLAEIYTKAGAPPGLFNVVQGGAATGQFLCHHREVAKISFTGSVPTGVKIMEMSAKGVKPITLELGGKSPLIIFSDCNMENAVKGALMANFLTQGQVCCNGTRVFVQKEIADKFINEVVKQTQKIKLGDPLLEDTRMGPLINAPHLERVLGFVKLAKEQGATVLCGGEVYVPEDPKLKHGYYMTPCVLTNCRDDMTCVKEEIFGPVMSILTFGTEAEVLERANDTTFGLAAGVFTRDIQRAHRVAAELQAGTCYINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF |
Proteomic databases
2D gel databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 52-507 | Aldehyde dehydrogenase | ||||
Sequence: TEKAFEPATGRVIATFACSGEKEVNLAVENAKAAFKLWSKKSGLERCQVLLEAARIIKERKDEIATVETINNGKSIFEARLDVDTCWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIACWKSAPALACGNAMIFKPSPFTPVSALLLAEIYTKAGAPPGLFNVVQGGAATGQFLCHHREVAKISFTGSVPTGVKIMEMSAKGVKPITLELGGKSPLIIFSDCNMENAVKGALMANFLTQGQVCCNGTRVFVQKEIADKFINEVVKQTQKIKLGDPLLEDTRMGPLINAPHLERVLGFVKLAKEQGATVLCGGEVYVPEDPKLKHGYYMTPCVLTNCRDDMTCVKEEIFGPVMSILTFGTEAEVLERANDTTFGLAAGVFTRDIQRAHRVAAELQAGTCYINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTV |
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length518
- Mass (Da)55,874
- Last updated2005-10-11 v1
- Checksum5A754A6FAF8E1EFC