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A0A6J4IIH7 · A0A6J4IIH7_9ACTN

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 site44L-glutamate (UniProtKB | ChEBI)
Binding site102pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site148pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site171pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site194pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site246-247pyridoxal 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
      AVDCRST_MAG57-2147

Organism names

  • Taxonomic identifier
  • Strain
    • AVDCRST_MAG57
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Geodermatophilales > Geodermatophilaceae > Blastococcus > environmental samples

Accessions

  • Primary accession
    A0A6J4IIH7

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue195N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain34-330Aminotransferase class V

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    371
  • Mass (Da)
    39,035
  • Last updated
    2020-10-07 v1
  • MD5 Checksum
    DC07D26A3FE3CA0D3F5F08F7E90F5882
MSITIPAELLPSDGRFGCGPSKVRPEALQALAGDGAAIMGTSHRQAPVKTLVREIREGLSRLFDLPEGYEVVLGNGGTTAFWDAAAIGLIRDRSAFGTYGEFSAKFASGVKEAPFLADPVIAKGEPGSLALPTAEAGIDAYGWAHNETSTGVMAPVRRPAGADDDALVLIDATSGAGGLPVDVAQTDVYYFAPQKSFAADGGLWVALMSPKALARVAEIKASGRWIPGFLDLSIAVDNSGKDQTYNTPAVATLFLLADQIRWLLSLGGLSGAVARTTDSSSRLYGWAEKTEYTTPFVTDPAHRSLVVGTVDFADSVDAAALAKVLRANGVVDVEPYRKLGRNQLRVGMFPAVEPDDVTALTACIEHVVERL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CADCTI010000176
EMBL· GenBank· DDBJ
CAA9251337.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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