O14027 · PDX1_SCHPO

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.

TypeIDPosition(s)Description
Binding site26D-ribose 5-phosphate (UniProtKB | ChEBI)
Active site83Schiff-base intermediate with D-ribose 5-phosphate
Binding site155D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site167D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site216D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site237-238D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentglutaminase complex
Molecular Functionamine-lyase activity
Molecular Functionpyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
Biological Processamino acid metabolic process
Biological Processcysteine biosynthetic process from serine
Biological Processpyridoxal phosphate biosynthetic process
Biological Processpyridoxine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable pyridoxal 5'-phosphate synthase subunit PDX1
  • EC number
  • Short names
    PLP synthase subunit PDX1

Gene names

    • Name
      snz1
    • ORF names
      SPAC29B12.04

Organism names

Accessions

  • Primary accession
    O14027

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001093641-296Probable pyridoxal 5'-phosphate synthase subunit PDX1
Modified residue178Phosphoserine
Modified residue180Phosphoserine
Modified residue283Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the PdxS/SNZ family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    296
  • Mass (Da)
    31,403
  • Last updated
    1998-01-01 v1
  • Checksum
    1B31C82B8AEFB961
MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329670
EMBL· GenBank· DDBJ
CAB16249.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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