N9U269 · N9U269_9GAMM
- ProteinL-threonine dehydratase
- GeneilvA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids508 (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 biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | L-serine ammonia-lyase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | threonine deaminase activity | |
Biological Process | isoleucine biosynthetic process | |
Biological Process | L-serine catabolic process | |
Biological Process | threonine catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-threonine dehydratase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Aeromonadales > Aeromonadaceae > Aeromonas
Accessions
- Primary accessionN9U269
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 330-402 | ACT-like | ||||
Sequence: GMLAVTIPERKGAFLDFCRNLGPRMVTEFNYRYSDAEQAALFVSVRLTGGEVELGQIERQLEESGYPVVNMTE | ||||||
Domain | 425-496 | ACT-like | ||||
Sequence: RLYSFKFPEQPGALMRFLETLGCRWNISLFHYRNHGADYGRVLCAFELPDEDVAAFHDYLREIGYAWKEVSE |
Sequence similarities
Belongs to the serine/threonine dehydratase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length508
- Mass (Da)56,009
- Last updated2013-06-26 v1
- Checksum7908C1FA319047ED
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
APVG01000016 EMBL· GenBank· DDBJ | ENY72415.1 EMBL· GenBank· DDBJ | Genomic DNA |