B5F159 · SERC_SALA4
- ProteinPhosphoserine aminotransferase
- GeneserC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids362 (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
- O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + 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 | 9 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 42 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 76-77 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GR | ||||||
Binding site | 102 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 153 | 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 | 239-240 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: NT |
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionB5F159
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000203550 | 1-362 | Phosphoserine aminotransferase | |||
Sequence: MAQVFNFSSGPAMLPAEVLKLAQQELRDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKITVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETPDFGPEVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPTFAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPFQLADNALDKVFLEESFAAGLHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRHG | ||||||
Modified residue | 198 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)39,855
- Last updated2008-10-14 v1
- Checksum8A8ED1A74D313507
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001138 EMBL· GenBank· DDBJ | ACH48969.1 EMBL· GenBank· DDBJ | Genomic DNA |