A0A0M8X8V6 · A0A0M8X8V6_9ACTN
- ProteinL-threonine 3-dehydrogenase
- Genetdh
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids339 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the NAD+-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Catalyzes the oxidation of 2-deoxy-scyllo-inosamine (DOIA) with NAD+ or NADP+, forming 3-amino-2,3-dideoxy-scyllo-inosose (amino-DOI).
Catalytic activity
- 2-deoxy-scyllo-inosamine + NAD+ = 3-amino-2,3-dideoxy-scyllo-inosose + 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.
Antibiotic biosynthesis.
Metabolic intermediate biosynthesis; 2-deoxystreptamine biosynthesis; 2-deoxystreptamine from D-glucose 6-phosphate: step 3/4.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 35 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Active site | 37 | Charge relay system | ||||
Sequence: T | ||||||
Active site | 40 | Charge relay system | ||||
Sequence: H | ||||||
Binding site | 60 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 61 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 90 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 93 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 96 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 145 | Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom | ||||
Sequence: D | ||||||
Binding site | 172 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 192 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 197 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 259-261 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: LGL | ||||||
Binding site | 283-284 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: IY |
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 > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A0M8X8V6
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-335 | Enoyl reductase (ER) | ||||
Sequence: GLWLADVPEPTVGPKDVLIRVLRTGICGTDLHIRAWDGWARQAISTPLVVGHEFVGEVVETGRDVTDISVGDRVSGEGHLVCGKCRNCLAGRRHLCRATVGLGVGRDGAFAEYVALPAGNVWVHRVPVDLDVAAIFDPFGNAVHTALSFPLVGEDVLVTGAGPIGLMAAAVAKHAGARNVVITDVSEERLELARKIGVSLALNVSEATIADGQRTLGLREGFDIGLEMSGRPEAMRDMIANMTHGGRIAMLGLPAQEFPVDWARVVTSMITIKGIYGREMFETWYAMSVLLEAGLDLAPVITGRYSHRDFEAAFEDAASGRGGKVIL |
Sequence similarities
Belongs to the zinc-containing alcohol dehydrogenase family. DOIA dehydrogenase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length339
- Mass (Da)36,241
- Last updated2015-12-09 v1
- Checksum0C80869BA11E2284
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LGEA01000099 EMBL· GenBank· DDBJ | KOV99183.1 EMBL· GenBank· DDBJ | Genomic DNA |