O14027 · PDX1_SCHPO
- ProteinProbable pyridoxal 5'-phosphate synthase subunit PDX1
- Genesnz1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids296 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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
- aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = H+ + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate
Pathway
Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 83 | Schiff-base intermediate with D-ribose 5-phosphate | ||||
Sequence: K | ||||||
Binding site | 155 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 167 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 216 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 237-238 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | glutaminase complex | |
Molecular Function | amine-lyase activity | |
Molecular Function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity | |
Biological Process | amino acid metabolic process | |
Biological Process | cysteine biosynthetic process from serine | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable pyridoxal 5'-phosphate synthase subunit PDX1
- EC number
- Short namesPLP synthase subunit PDX1
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionO14027
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000109364 | 1-296 | Probable pyridoxal 5'-phosphate synthase subunit PDX1 | |||
Sequence: MSAEIKGSTQVKAGLAQMLKGGVIMDVVNAEQARIAEAAGACAVMALERVPADIRAQGGVARMSDPSMIKEIQAAVSIPVMAKVRIGHFVEAQILESIGVDYIDESEVLTPADDINHIEKSKFTVPFVCGSRNLGEALRRISEGAAMIRTKGEAGTGDVVEAVRHTRQMQGELRRVKSMSPDELYTYAKEIAAPIDLVKECAQLGRLPVVNFAAGGVATPADAALMMQLGCDGVFVGSGIFLSGDPAKRARAIVRAVTHYNDPKILAEVSENLGAAMVGRSVSSLEEKEKLATRGW | ||||||
Modified residue | 178 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 180 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 283 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length296
- Mass (Da)31,403
- Last updated1998-01-01 v1
- Checksum1B31C82B8AEFB961
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329670 EMBL· GenBank· DDBJ | CAB16249.1 EMBL· GenBank· DDBJ | Genomic DNA |