A0A223NVS7 · A0A223NVS7_9SPHI

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 site40L-glutamate (UniProtKB | ChEBI)
Binding site74-75pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site100pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site148pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site167pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site190pyridoxal 5'-phosphate (UniProtKB | ChEBI)
Binding site232-233pyridoxal 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
    • ORF names
      MuYL_2091

Organism names

  • Taxonomic identifier
  • Strain
    • BJC16-A31
  • Taxonomic lineage
    Bacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Mucilaginibacter

Accessions

  • Primary accession
    A0A223NVS7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue191N6-(pyridoxal phosphate)lysine

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-334Aminotransferase class V

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    355
  • Mass (Da)
    38,965
  • Last updated
    2017-10-25 v1
  • Checksum
    C0236A860F61B5BE
MKHNFGAGPGILPHEVLKQAAAAVVDFGGIGLSILEISHRSPEFESVLDEAVKLVKELFSVPEGYSVLFLQGGASTQFALAPYNLLPEGGKAAYLETGVWANKALKEAKFFGDVEIVASSKDKNFTYIPKDYKIPADAAYFHITSNNTIYGTQLQQFPKSPVPMVCDMSSDIFSRKIDVADFGLIYAGAQKNMGPAGVTLVIVKDSLLGKTGRKIPAMFNYQVQVEGGSMYNTPPVFAIYVSMLTLNWLKSKGGVEAIEKENIAKARVLYEEIDRNPLFKPVCEVEDRSHMNVCFVMENPELEKPFLKLCDDKGIVGIKGHRSVGGFRASIYNALPITSVYVLIDAMQEFAEKNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP022743
EMBL· GenBank· DDBJ
ASU33983.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp