M2PR90 · M2PR90_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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site174pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site197pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site249-250pyridoxal 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
      C791_2596

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 43854
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Pseudonocardiales > Pseudonocardiaceae > Amycolatopsis

Accessions

  • Primary accession
    M2PR90

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue198N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain141-333Aminotransferase class V

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    375
  • Mass (Da)
    40,233
  • Last updated
    2013-05-01 v1
  • Checksum
    EB79DB2834363118
MTDAPELTLPADLKPADGRFGCGPSKVRDEQLANLAKSGATYLGTSHRQKPVKSLVGRVRAGLSELFSLPEGYEVVLGNGGTTAFWDAAAFGLVRERSQHFTYGEFSSKFATVTKGAPFLADPIVVKSDPGSAPEIAYEAGADLVGWAHNETSTGVAVPVRRPEGSDGALVAIDATSGAGGLPVKAEDFDVYYFAPQKSFASDGGLWIALASPAAVERIGEIGASDRWIPEFLSLTTALDNSRKDQTYNTPAVSTLFLLADQIEWMNSNGGLEWTTARTRDSSTRLYEWAEKTSYTTPFVSDPSLRSQVVGTIDFADEVDAAAVAKVLRANGIVDTEPYRKLGRNQLRVGLFPAIDPDDITKLTQSIEYVVERLG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ANMG01000025
EMBL· GenBank· DDBJ
EMD27088.1
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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