A0A1J4NGR6 · A0A1J4NGR6_9GAMM
- ProteinBetaine aldehyde dehydrogenase
- GenebetB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids491 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid.
Catalytic activity
- betaine aldehyde + NAD+ + H2O = glycine betaine + NADH + 2 H+
Cofactor
Note: Binds 2 potassium ions per subunit.
Pathway
Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | K+ 1 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 27 | K+ 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 93 | K+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 150-152 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAW | ||||||
Active site | 162 | Charge relay system | ||||
Sequence: K | ||||||
Binding site | 229-232 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GVAT | ||||||
Binding site | 245 | K+ 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Site | 247 | Seems to be a necessary countercharge to the potassium cations | ||||
Sequence: E | ||||||
Active site | 251 | |||||
Sequence: E | ||||||
Active site | 251 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 253 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 285 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 285 | NAD+ (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 386 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 456 | K+ 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 459 | K+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Active site | 463 | Charge relay system | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | betaine-aldehyde dehydrogenase (NAD+) activity | |
Molecular Function | metal ion binding | |
Biological Process | glycine betaine biosynthetic process from choline |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBetaine aldehyde dehydrogenase
- EC number
- Short namesBADH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter
Accessions
- Primary accessionA0A1J4NGR6
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 285 | Cysteine sulfenic acid (-SOH) | ||||
Sequence: C |
Keywords
- PTM
Interaction
Subunit
Dimer of dimers.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-478 | Aldehyde dehydrogenase | ||||
Sequence: FVDATSNSTFETINPATGEVLAEVQICSKDDIDRAVKSAQQGQKVWAEMTAIQRSRILQKAVAILRDRNDELARIETLDSGKAFSETSTVDIATGADVLEYYAGILPALEGQQIPLRETSFIYTRREPLGVVAGIGAWNYPIQIALWKSAPAMAAGNAMIFKASEVTPLTALKLAEIYTEAGVPHGVFNVVTGGSEIGAYLTSHPDIAKVSFTGGVATGKKVMAQAANSSLKEVTMELGGKSPLIICEDADLDLAADIAMMANYYSSGQVCTNGTRVFIPLALKAEFEDKILQRIPYVRMGDPLDPETNFGPVSSFSHMAKVLDYIEQGKKEGARLLCGGGRAEDEQFAQGAYVLPTVFTDCRDDMTIVRDEIFGPVMSILSYDSEEEVIQRANATEYGLAAGVVTPNLSRAHRIIHQIEAGICWINTWGESPAEMPVGGYKHSGVGRENGIVTLQQYTQTKSV |
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length491
- Mass (Da)53,275
- Last updated2017-02-15 v1
- Checksum543E21074651C2D0