Q62CH7 · BETB_BURMA
- ProteinBetaine aldehyde dehydrogenase
- GenebetB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids489 (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 + H2O + NAD+ = glycine betaine + 2 H+ + NADHThis reaction proceeds in the forward direction.
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 | 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 | 176-179 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: KPSE | ||||||
Binding site | 180 | K+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 229-232 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GVET | ||||||
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 | 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 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > pseudomallei group
Accessions
- Primary accessionQ62CH7
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056539 | 1-489 | Betaine aldehyde dehydrogenase | |||
Sequence: MSVYGLQRLYIAGAHADATSGKTFDTFDPATGELLARVQQASADDVDRAVASAREGQREWAAMTAMQRSRILRRAVELLRERNDALAELEMRDTGKPIAETRAVDIVTGADVIEYYAGLATAIEGLQVPLRPESFVYTRREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLSALKLAEIYTEAGVPAGVFNVVQGDGSVGALLSAHPGIAKVSFTGGVETGKKVMSLAGASSLKEVTMELGGKSPLIVFDDADLDRAADIAVTANFFSAGQVCTNGTRVFVQQAVKDAFVERVLARVARIRAGKPSDPDTNFGPLASAAQLDKVLGYIDSGKAEGAKLLAGGARLVNDHFASGQYVAPTVFGDCRDDMRIVREEIFGPVMSILSFETEDEAIARANATDYGLAAGVVTENLSRAHRAIHRLEAGICWINTWGESPAEMPVGGYKQSGVGRENGITTLEHYTRIKSVQVELGRYQPVF | ||||||
Modified residue | 285 | Cysteine sulfenic acid (-SOH) | ||||
Sequence: C |
Keywords
- PTM
Interaction
Subunit
Dimer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)52,173
- Last updated2004-10-25 v1
- Checksum53E483722690674A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000011 EMBL· GenBank· DDBJ | AAU46695.1 EMBL· GenBank· DDBJ | Genomic DNA |