A0A1J9NWY0 · A0A1J9NWY0_9BURK
- ProteinL-threonine 3-dehydrogenase
- Genetdh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids342 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the NAD+-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Catalytic activity
- L-threonine + NAD+ = (2S)-2-amino-3-oxobutanoate + NADH + H+
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 38 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Active site | 40 | Charge relay system | |||
Active site | 43 | Charge relay system | |||
Binding site | 63 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 64 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 93 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 96 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 99 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 107 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Site | 148 | Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom | |||
Binding site | 175 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 195 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 200 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 262-264 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 286-287 | NAD+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | L-threonine 3-dehydrogenase activity | |
Molecular Function | zinc ion binding | |
Biological Process | L-threonine catabolic process to glycine |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-threonine 3-dehydrogenase
- EC number
- Short namesTDH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionA0A1J9NWY0
Proteomes
Subcellular Location
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length342
- Mass (Da)37,376
- Last updated2017-02-15 v1
- MD5 ChecksumD3B75A88C02215E1267DB194B570B3F3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MDEQ01000011 EMBL· GenBank· DDBJ | OJD09161.1 EMBL· GenBank· DDBJ | Genomic DNA |