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A0A0M4QAD0 · A0A0M4QAD0_9PSEU

Function

function

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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site48L-glutamate (UniProtKB | ChEBI)
Binding site106pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site152pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site175pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site198pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site250-251pyridoxal 5'-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentperoxisome
Molecular Functionalanine-glyoxylate transaminase activity
Molecular FunctionO-phospho-L-serine:2-oxoglutarate aminotransferase activity
Molecular Functionpyridoxal phosphate binding
Molecular Functionserine-pyruvate transaminase activity
Biological Processglycine biosynthetic process, by transamination of glyoxylate
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
    • ORF names
      XF36_22160

Organism names

  • Taxonomic identifier
  • Strain
    • HH130629-09
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Pseudonocardia

Accessions

  • Primary accession
    A0A0M4QAD0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue199N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain139-334Aminotransferase class V

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    377
  • Mass (Da)
    39,970
  • Last updated
    2015-12-09 v1
  • MD5 Checksum
    5454D8DC39F8AA2F7849A3D424B1AC94
MTSPADLKIPGDLLPQDGRFGCGPSKVRPEQLSALAATGDSLLGTSHRQKPVRELVGRVRSGLAELFSLPDGYEVVLGNGGSTAFWDAAAFGLVRERSLHLTYGEFSQKFADTTTGAPFLADPVVVRADPGSAPEPVSDPSVDVIAWAHNETSTGVAVPVNRPAGTTEDQLVVIDATSGAGGLPVDVTQSDVYYFAPQKGFASDGGLYLALMSPKALQRVAELAASDRWIPPFLSLATAVDNSGKDQTYNTPSLATLFLLEDQVRWMNALGGLDGCVARTRDSSDRLYTWAEKSSFATPFVTDPAHRSLVVGTIDFDDAVDAAAVATALRANGIVDTEPYRKLGRNQLRIGMFPAVEPSDVSALTACIDWVVERLGS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011868
EMBL· GenBank· DDBJ
ALE85522.1
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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