E3ZM36 · E3ZM36_LISSE
- ProteinMalonate-semialdehyde dehydrogenase
- GeneiolA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids488 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. Is involved in a myo-inositol catabolic pathway. Bicarbonate, and not CO2, is the end-product of the enzymatic reaction.
Catalytic activity
- 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = H+ + hydrogencarbonate + NADH + propanoyl-CoA
Pathway
Polyol metabolism; myo-inositol degradation into acetyl-CoA; acetyl-CoA from myo-inositol: step 7/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 150 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 152 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 176 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 179 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 180 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 251 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 284 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 382 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | malonate-semialdehyde dehydrogenase (acetylating) activity | |
Molecular Function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity | |
Biological Process | inositol catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMalonate-semialdehyde dehydrogenase
- EC number
- Short namesMSA dehydrogenase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Listeriaceae > Listeria
Accessions
- Primary accessionE3ZM36
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-477 | Aldehyde dehydrogenase | ||||
Sequence: WVASKTEKYENVINPATGEILCQVPISTRAELDEAAEISEKAFEKWSQVAVPRRARILFSFQQLLIQHKEELARLITLENGKNLSEARGEVQRGIENVEFAAGAPTLMMGDSLASIATDVEAANYRYPVGVVGGIAPFNFPMMVPCWMFPIAIALGNSFILKPSERTPLLMEKLVELFTEAGLPNGVFNVVYGAHDVVNGILKNDKIKAVSFVGSKPVGEYVYKTGSANLKRVQALTGAKNHTIVLNDADLEDTVINVISAAFGSAGERCMACAVVTVEEGIADEFLEALRIAARNVKIGNGLDDGVFLGPVIREENQKRTLAYIEKGVEEGAKLTVDGRETGISKGHFVGPTILEEVTTDMTIWKEEIFAPVLSVIRVKNLQEAVKIANKSEFANGACIFTNNAKAIRYFREKIDAGMLGVNLGVPAPMAFFPFSGWKSSFYGTLHANGKDSVDFYTHKKVV |
Sequence similarities
Belongs to the aldehyde dehydrogenase family. IolA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length488
- Mass (Da)53,442
- Last updated2011-02-08 v1
- Checksum6D46D5D57EF380DD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ADXJ01000195 EMBL· GenBank· DDBJ | EFS01311.1 EMBL· GenBank· DDBJ | Genomic DNA |