A0A7K7Y7B9 · A0A7K7Y7B9_THRLU
- Protein4-trimethylaminobutyraldehyde dehydrogenase
- GeneAldh9a1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids463 (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
Pathway
Amine and polyamine biosynthesis; carnitine biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 223 | |||||
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Passeriformes > Certhiidae > Troglodytinae > Thryothorus
Accessions
- Primary accessionA0A7K7Y7B9
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-452 | Aldehyde dehydrogenase | ||||
Sequence: GRVLCKVPCSGEKEVDLAVQSAKAAFKIWSQMSGMERCRVMLEAARIIREQRDEIATMETINNGKSIFEARVDIDISWQCLEYYAGLAGSLAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIACWKSGPALACGNAMVFKPSPFTPISVVRLAEIFTEAGVPKGLFNVVQGGAATGQFLCQHPDVAKISFTGSVPTGMKIMEMASKGIKPVTLELGGKSPLIIFSDADLENAVKGALMANFLTQGEVCCNGTRVFVERKILDTFTKEVVKRTQKIKIGDPLLEDTRMGALINRPHLNRVQGFIKQAKEQGAEVLCGGDLYVPDDPKLKNGYYMRPCVLGNCKDDMTCVKEEIFGPVMAILPFDTEEEVVERANATKFGLAGGVFTRDIQKAHRVVAALKAGMCFINNYNVSPVELPFGGYKFSGFGRENGRAAIEYYSQLKTV |
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length463
- Mass (Da)50,546
- Last updated2021-04-07 v1
- Checksum6F2EC537CB260C68
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: F | ||||||
Non-terminal residue | 463 | |||||
Sequence: F |
Keywords
- Technical term