D7M726 · D7M726_ARALL

Function

function

Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers.

Catalytic activity

Pathway

Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.

Features

Showing features for binding site, active site.

130920406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site40D-ribose 5-phosphate (UniProtKB | ChEBI)
Active site97Schiff-base intermediate with D-ribose 5-phosphate
Binding site169D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site181D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site230D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site251-252D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentendomembrane system
Cellular Componentplasma membrane
Molecular Functionamine-lyase activity
Molecular Functionprotein heterodimerization activity
Molecular Functionprotein homodimerization activity
Biological Processamino acid metabolic process
Biological Processchlorophyll metabolic process
Biological Processhyperosmotic salinity response
Biological Processpyridoxal phosphate biosynthetic process
Biological Processpyridoxine biosynthetic process
Biological Processresponse to lipid hydroperoxide
Biological Processresponse to non-ionic osmotic stress
Biological Processresponse to UV-B

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)
  • EC number

Gene names

    • ORF names
      ARALYDRAFT_908014

Organism names

  • Taxonomic identifier
  • Strain
    • cv. MN47
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    D7M726

Proteomes

Genome annotation databases

Subcellular Location

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-228PdxS/SNZ N-terminal

Sequence similarities

Belongs to the PdxS/SNZ family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    309
  • Mass (Da)
    33,216
  • Last updated
    2010-08-10 v1
  • Checksum
    E74EBBCD4F124456
MEGTGVVAVYGNGAITEAKKSPFSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPQMIKEIKQAVTIPVMAKARIGHFVEAQILEAIGIDYIDESEVLTLADEDHHINKHNFRIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNIIEAVRHVRSVNGDIRVLRNMDDDEVFTFAKKLAAPYDLVMQTKQLGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGIFKSGDPARRARAIVQAVTHYSDPEMLVEVSCGLGEAMVGINLNDEKVERFANRSE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL348718
EMBL· GenBank· DDBJ
EFH47181.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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