A1VY45 · SERC_CAMJJ
- ProteinPhosphoserine aminotransferase
- GeneserC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids358 (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
- 2-oxoglutarate + O-phospho-L-serine = 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 | 41 | L-glutamate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 75-76 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: AS | ||||||
Binding site | 100 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 148 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 167 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 190 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 233-234 | 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
- Strain
- Taxonomic lineageBacteria > Campylobacterota > Epsilonproteobacteria > Campylobacterales > Campylobacteraceae > Campylobacter
Accessions
- Primary accessionA1VY45
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000058208 | 1-358 | Phosphoserine aminotransferase | |||
Sequence: MRKINFSAGPSTLPLEILEQAQKELCDYQGRGYSIMEISHRTKVFEEVHFGAQEKAKKLYGLNDDYEVLFLQGGASLQFAMIPMNLALNGVCEYANTGVWTKKAIKEAQILGVNVKTVASSEESNFNHIPRVEFRDNADYAYICSNNTIYGTQYQNYPKTKTPLIVDASSDFFSRKVDFSNIALFYGGVQKNAGISGLSCIFIRKDMLERSKNKQIPSMLNYLTHAENQSLFNTPPTFAIYMFNLEMDWLLNQGGLDKVHEKNSQKAAMLYECIDLSNGFYKGHADKKDRSLMNVSFNIAKNKDLEPLFVKEAEEAGMIGLKGHRILGGIRASIYNALNLDQIKTLCEFMKEFQGKYA | ||||||
Modified residue | 191 | N6-(pyridoxal phosphate)lysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)40,466
- Last updated2007-02-06 v1
- ChecksumD77A76B8B23473A2
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000538 EMBL· GenBank· DDBJ | EAQ72981.1 EMBL· GenBank· DDBJ | Genomic DNA |