A0A940DKY5 · A0A940DKY5_9BACT
- ProteinPhosphoserine aminotransferase
- GeneserC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids357 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic activity
- 4-(phosphooxy)-L-threonine + 2-oxoglutarate = (R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate
Cofactor
Note: Binds 1 pyridoxal phosphate per subunit.
Pathway
Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 42 | L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 76-77 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 100 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 148 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 167 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 190 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 232-233 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Biological Process | L-serine biosynthetic process | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoserine aminotransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Candidatus Cryptobacteroides
Accessions
- Primary accessionA0A940DKY5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 191 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length357
- Mass (Da)39,446
- Last updated2023-02-22 v1
- MD5 ChecksumC90841E07767D3D95CC008A942CD4869
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JADIMJ010000006 EMBL· GenBank· DDBJ | MBO8453132.1 EMBL· GenBank· DDBJ | Genomic DNA |