A1A3A5 · PDXS_BIFAA
- ProteinPyridoxal 5'-phosphate synthase subunit PdxS
- GenepdxS
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids291 (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 | 23 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 80 | Schiff-base intermediate with D-ribose 5-phosphate | ||||
Sequence: K | ||||||
Binding site | 152 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 164 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 213 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 234-235 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS |
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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionA1A3A5
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000070365 | 1-291 | Pyridoxal 5'-phosphate synthase subunit PdxS | |||
Sequence: MANNRNELNKNLAQMLKGGVIMDVTTPEQAKIAQDAGACAVMALERIPADIRAAGGVSRMSDPAMIKGIQEAVSIPVMAKVRIGHIAEARILQAIEIDYIDESEVLSPADDVYHIDKNRFDVPFVCGAKNLGEALRRVAEGASMIRTKGEPGTGDVIQAVRHMRTMNKQIRELVSLRDDEVYEAAKQLAVPYDLAKYVHDNGRLPVVNFAAGGVATPADAALMMELGAEGVFVGSGIFKSGDPAKRAAAIVQATANWQDAELLARLSENLGEAMVGINEDEIETIMAARGE |
Proteomic databases
Interaction
Subunit
In the presence of PdxT, forms a dodecamer of heterodimers.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length291
- Mass (Da)31,180
- Last updated2007-01-23 v1
- Checksum65AC5BC41B75930E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP009256 EMBL· GenBank· DDBJ | BAF40188.1 EMBL· GenBank· DDBJ | Genomic DNA |