A0A5M9ZNU8 · A0A5M9ZNU8_9BIFI

  • Protein
    Phosphoserine aminotransferase
  • Gene
    serC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site46L-glutamate (UniProtKB | ChEBI)
Binding site80-81pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site104pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site150pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site174pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site197pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site255-256pyridoxal 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
      EMO89_08135

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RST7
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A5M9ZNU8

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
Domain139-345Aminotransferase class V

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    381
  • Mass (Da)
    41,350
  • Last updated
    2020-02-26 v1
  • Checksum
    5EE7D36AF2B5D252
MIEPVKIPMSMLPEDGRFGCGPSKIRHKQVKALTEAGYNLLGTSHRQAPVKHVVASIREGLSDYFSIPEGWQIALGNGGASAFWEVACASLISRRAAFGTYGSFSGKFATSAAKAPFLEEPVIYKAEYGSCAIPQYTDDVDAYCWAQNETSTGVMAPVHRVPGSVEQGALTLIDATSGAGGLPIDISQTDAYYFSPQKVFGSDGGLWFAILSPDAIKRAEDVEKSAELEGARRWVPPFLSLTQALANSRKDQTLNTPAISTLVLMDEQVRWLNEHGGLTWAQERCAKSADILYTWAEKSDYATPFVSDPSLRSNVVVTIDLDDSIKAAAVVAVLRDNGIVDTSGYRKLGRNQLRIGVFPSVKPSDVEALTYCIDYVVEHLQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RZUI01000010
EMBL· GenBank· DDBJ
KAA8829311.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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