A0A418KVF7 · A0A418KVF7_9ACTN
- ProteinPhosphoserine aminotransferase
- GeneserC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 46 | L-glutamate (UniProtKB | ChEBI) | |||
Binding site | 104 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 150 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 173 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 196 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
Binding site | 248-249 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | alanine-glyoxylate transaminase activity | |
Molecular Function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | serine-pyruvate transaminase activity | |
Biological Process | glycine biosynthetic process, by transamination of glyoxylate | |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Jiangellales > Jiangellaceae > Jiangella
Accessions
- Primary accessionA0A418KVF7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 197 | N6-(pyridoxal phosphate)lysine | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-22 | Disordered | |||
Domain | 139-332 | Aminotransferase class V | |||
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)39,619
- Last updated2019-05-08 v1
- MD5 Checksum1F78A7DCA35D9E1A440B09B45FD44420
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
QUAL01000043 EMBL· GenBank· DDBJ | RIQ32565.1 EMBL· GenBank· DDBJ | Genomic DNA |