P55900 · SERC_SALTY

Function

function

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

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.

TypeIDPosition(s)Description
Binding site9L-glutamate (UniProtKB | ChEBI)
Binding site42L-glutamate (UniProtKB | ChEBI)
Binding site76-77pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site102pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site153pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site174pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site197pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site239-240pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Biological ProcessL-serine biosynthetic process
Biological Processpyridoxine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoserine aminotransferase
  • EC number
  • Alternative names
    • Phosphohydroxythreonine aminotransferase
      (PSAT
      )

Gene names

    • Name
      serC
    • Ordered locus names
      STM0977

Organism names

Accessions

  • Primary accession
    P55900

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001502071-362Phosphoserine aminotransferase
Modified residue198N6-(pyridoxal phosphate)lysine

Proteomic databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    362
  • Mass (Da)
    39,832
  • Last updated
    2002-01-23 v2
  • Checksum
    802C026A8B4CE2C3
MAQVFNFSSGPAMLPAEVLKLAQQELCDWHGLGTSVMEISHRGKEFIQVAEEAEQDFRDLLNIPSNYKVLFCHGGGRGQFAGVPLNLLGDKTTADYVDAGYWAASAIKEAKKYCAPQIIDAKITVDGKRAVKPMREWQLSDNAAYLHYCPNETIDGIAIDETPDFGPEVVVTADFSSTILSAPLDVSRYGVIYAGAQKNIGPAGLTLVIVREDLLGKAHESCPSILDYTVLNDNDSMFNTPPTFAWYLSGLVFKWLKAQGGVAAMHKINQQKAELLYGVIDNSDFYRNDVAQANRSRMNVPFQLADNTLDKVFLEESFAAGLHALKGHRVVGGMRASIYNAMPIEGVKALTDFMIDFERRHG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict47in Ref. 1; CAA71381
Sequence conflict79in Ref. 1; CAA71381

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y10355
EMBL· GenBank· DDBJ
CAA71381.1
EMBL· GenBank· DDBJ
Genomic DNA
AE006468
EMBL· GenBank· DDBJ
AAL19911.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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