A0A3A2IV93 · A0A3A2IV93_STAAU
- ProteinL-threonine dehydratase catabolic TdcB
- GenetdcB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids346 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
Catalytic activity
- L-threonine = 2-oxobutanoate + NH4+
Cofactor
Pathway
Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 1/4.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | L-serine ammonia-lyase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | threonine deaminase activity | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | L-serine catabolic process | |
Biological Process | L-threonine catabolic process to propionate |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-threonine dehydratase catabolic TdcB
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A3A2IV93
- Secondary accessions
Proteomes
Interaction
Subunit
In the native structure, TdcB is in a dimeric form, whereas in the TdcB-AMP complex, it exists in a tetrameric form (dimer of dimers).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 27-319 | Tryptophan synthase beta chain-like PALP | |||
Sequence similarities
Belongs to the serine/threonine dehydratase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length346
- Mass (Da)37,147
- Last updated2018-12-05 v1
- Checksum4435206B7E89CC10
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CAIHOM010000001 EMBL· GenBank· DDBJ | CAC6984673.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CAIIGN010000001 EMBL· GenBank· DDBJ | CAC8215438.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BDVT01000001 EMBL· GenBank· DDBJ | GBV19314.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WPRH01000733 EMBL· GenBank· DDBJ | MVI56942.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WPVZ01000535 EMBL· GenBank· DDBJ | MVL45785.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAAJIY010000025 EMBL· GenBank· DDBJ | NGK21606.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAALTR010000315 EMBL· GenBank· DDBJ | NGW68432.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JAANDN010000049 EMBL· GenBank· DDBJ | NUY67989.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QNXH01000001 EMBL· GenBank· DDBJ | TXL38881.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QNXF01000002 EMBL· GenBank· DDBJ | TXL46869.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP152420 EMBL· GenBank· DDBJ | XAJ30630.1 EMBL· GenBank· DDBJ | Genomic DNA |