Q65S80 · SERC_MANSM

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 site42L-glutamate (UniProtKB | ChEBI)
Binding site76-77pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site102pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site153pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site173pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site196pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site238-239pyridoxal 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
      MS1573

Organism names

Accessions

  • Primary accession
    Q65S80

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001501861-361Phosphoserine aminotransferase
Modified residue197N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    361
  • Mass (Da)
    39,988
  • Last updated
    2004-10-25 v1
  • Checksum
    C13EF5C92426CCFE
MSNVFNFSAGPAMMPPAVLKKAQEELLNWQGQGTSVMEVSHRGKYFMELITQADKDFRELYNIPENYKILFLQGGARGQFAAIPMNLANNKGKALYLNTGHWSATAAKEARNFTEVDELNITEQIDGLTRVNRLDFSDIAEQYDYVHYCPNETITGVEINEIPNVGNAVLVADMSSNIMARKLDISKFGIIYAGAQKNLGPAGIVIVIVREDLIGHARKATPSIWNYEVQANADSMINTPPTFAWYLCSLVFKDLLANGGIDTVEKRNAQKAALLYDYLDQTVFYHNTIAKENRSVMNVTFTTGDDQLNAKFVAQATEAGLQALKGHKVFGGMRASIYNAMPVEGVEALIAFMKKFEAENA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE016827
EMBL· GenBank· DDBJ
AAU38180.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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