Q802W2 · A9A1B_DANRE
- Protein4-trimethylaminobutyraldehyde dehydrogenase B
- Genealdh9a1b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids518 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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.
Catalytic activity
- 4-(trimethylamino)butanal + NAD+ + H2O = 4-(trimethylamino)butanoate + NADH + 2 H+
Pathway
Amine and polyamine biosynthesis; carnitine biosynthesis.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | 4-trimethylammoniobutyraldehyde dehydrogenase activity | |
Molecular Function | aminobutyraldehyde dehydrogenase (NAD+) activity | |
Biological Process | carnitine biosynthetic process | |
Biological Process | cellular aldehyde metabolic process | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name4-trimethylaminobutyraldehyde dehydrogenase B
- EC number
- Short namesTMABA-DH; TMABADH
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ802W2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000300625 | 1-518 | 4-trimethylaminobutyraldehyde dehydrogenase B | |||
Sequence: MALMRCLLPPGFYRTLYHPWTRCASSGTLQIKDPLNFWCGARVDLKDVKTKSEPVFEPATGRVLCRLQTCGSAEVDAAVRNASAAFKVWRKLSGMERARVMLEAARLIEKRREEIAEMEVINNGKSITEARLDVDSARLSIEYFAGQATTLSGQHVQLPGGSFAYTRREPFGVCVGIGAWNYPFQIAAWKSAPAIACGNSMVFKPSPLTPVTAVLLAEIYRQAGAPEGLFNVVQGGQETGSLLCLHPSVEKVSFTGSVPTGKKIMEMASRGVKAVTLELGGKSPLIIFEDTDLENAVRGALMANFLSQGQVCSNGTRVFVQSSIVPQFLKEVVRRTKAISIGDPLLDETRMGALVSKAHLDKVLRYVEQAKNEGAQVLCGGEPFSPADPKLKDGYYMTPCVLDSCTDDMTCVKEEIFGPVMSVLTFDTEDEVLRRANDSDLGLAAGVFTKDVKRAHRVIENLQAGSCFINNYNITPVEVPFGGFKASGIGRENGQVTIEFYSQLKTVVVEMGDVDSLF |
Proteomic databases
Expression
Gene expression databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length518
- Mass (Da)56,438
- Last updated2007-10-23 v2
- Checksum105AB1667E4199FF
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8M3AVP0 | A0A8M3AVP0_DANRE | aldh9a1b | 539 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 18-20 | in Ref. 2; AAH47176 | ||||
Sequence: HPW → NPG | ||||||
Sequence conflict | 84 | in Ref. 2; AAH47176 | ||||
Sequence: A → V | ||||||
Sequence conflict | 87 | in Ref. 2; AAH47176 | ||||
Sequence: K → T | ||||||
Sequence conflict | 102 | in Ref. 2; AAH47176 | ||||
Sequence: L → M | ||||||
Sequence conflict | 140 | in Ref. 2; AAH47176 | ||||
Sequence: S → C | ||||||
Sequence conflict | 167 | in Ref. 2; AAH47176 | ||||
Sequence: R → H | ||||||
Sequence conflict | 227 | in Ref. 2; AAH47176 | ||||
Sequence: E → D | ||||||
Sequence conflict | 342 | in Ref. 2; AAH47176 | ||||
Sequence: G → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL954171 EMBL· GenBank· DDBJ | CAM14219.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC047176 EMBL· GenBank· DDBJ | AAH47176.1 EMBL· GenBank· DDBJ | mRNA |