M2PR90 · M2PR90_9PSEU
- 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
- 2-oxoglutarate + 4-(phosphooxy)-L-threonine = (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 | 48 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 106 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 152 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 174 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 197 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 249-250 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: NT |
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 > Pseudonocardiales > Pseudonocardiaceae > Amycolatopsis
Accessions
- Primary accessionM2PR90
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 198 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 141-333 | Aminotransferase class V | ||||
Sequence: GADLVGWAHNETSTGVAVPVRRPEGSDGALVAIDATSGAGGLPVKAEDFDVYYFAPQKSFASDGGLWIALASPAAVERIGEIGASDRWIPEFLSLTTALDNSRKDQTYNTPAVSTLFLLADQIEWMNSNGGLEWTTARTRDSSTRLYEWAEKTSYTTPFVSDPSLRSQVVGTIDFADEVDAAAVAKVLRANGI |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)40,233
- Last updated2013-05-01 v1
- ChecksumEB79DB2834363118
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ANMG01000025 EMBL· GenBank· DDBJ | EMD27088.1 EMBL· GenBank· DDBJ | Genomic DNA |