A0A432G3V3 · A0A432G3V3_9DELT
- ProteinL-carnitine dehydrogenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids497 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the NAD+-dependent oxidation of L-carnitine to 3-dehydrocarnitine.
Catalytic activity
- carnitine + NAD+ = 3-dehydrocarnitine + NADH + H+
Pathway
Amine and polyamine metabolism; carnitine metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 12-17 | NAD+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | carnitine 3-dehydrogenase activity | |
Molecular Function | L-gulonate 3-dehydrogenase activity | |
Molecular Function | NAD+ binding | |
Biological Process | carnitine metabolic process | |
Biological Process | catabolic process | |
Biological Process | fatty acid metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-carnitine dehydrogenase
- EC number
- Short namesCDH ; L-CDH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Deltaproteobacteria > SAR324 cluster
Accessions
- Primary accessionA0A432G3V3
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 8-182 | 3-hydroxyacyl-CoA dehydrogenase NAD binding | |||
Domain | 187-254 | 3-hydroxyacyl-CoA dehydrogenase C-terminal | |||
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length497
- Mass (Da)56,044
- Last updated2019-05-08 v1
- Checksum0045436A3AB3632B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QNZM01000290 EMBL· GenBank· DDBJ | RTZ78416.1 EMBL· GenBank· DDBJ | Genomic DNA |