A0A0S7BY15 · A0A0S7BY15_9CHLR
- ProteinPyridoxal 5'-phosphate synthase subunit PdxS
- GenepdxS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids290 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively.
Catalytic activity
- aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H+
Pathway
Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 22 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
Active site | 79 | Schiff-base intermediate with D-ribose 5-phosphate | |||
Binding site | 151 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 163 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | |||
Binding site | 212 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 233-234 | D-ribose 5-phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity | |
Biological Process | amino acid metabolic process | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxal 5'-phosphate synthase subunit PdxS
- EC number
- Short namesPLP synthase subunit PdxS
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Chloroflexota > Anaerolineae > Anaerolineales > Anaerolineaceae > Flexilinea
Accessions
- Primary accessionA0A0S7BY15
Proteomes
Interaction
Subunit
In the presence of PdxT, forms a dodecamer of heterodimers.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length290
- Mass (Da)31,617
- Last updated2016-02-17 v1
- MD5 Checksum8B07C25B69664D37947B9D63B89642E4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DF968181 EMBL· GenBank· DDBJ | GAP41632.1 EMBL· GenBank· DDBJ | Genomic DNA |