D7M726 · D7M726_ARALL
- Proteinpyridoxal 5'-phosphate synthase (glutamine hydrolyzing)
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids309 (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 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 = 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 | 40 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 97 | Schiff-base intermediate with D-ribose 5-phosphate | ||||
Sequence: K | ||||||
Binding site | 169 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 181 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 230 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 251-252 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endomembrane system | |
Cellular Component | plasma membrane | |
Molecular Function | amine-lyase activity | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | protein homodimerization activity | |
Biological Process | amino acid metabolic process | |
Biological Process | chlorophyll metabolic process | |
Biological Process | hyperosmotic salinity response | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxine biosynthetic process | |
Biological Process | response to lipid hydroperoxide | |
Biological Process | response to non-ionic osmotic stress | |
Biological Process | response to UV-B |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namepyridoxal 5'-phosphate synthase (glutamine hydrolyzing)
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionD7M726
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-228 | PdxS/SNZ N-terminal | ||||
Sequence: FSVKVGLAQMLRGGVIMDVVNAEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPQMIKEIKQAVTIPVMAKARIGHFVEAQILEAIGIDYIDESEVLTLADEDHHINKHNFRIPFVCGCRNLGEALRRIREGAAMIRTKGEAGTGNIIEAVRHVRSVNGDIRVLRNMDDDEVFTFAKKLAAPYDLVMQTKQLGRLPVVQFAA |
Sequence similarities
Belongs to the PdxS/SNZ family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)33,216
- Last updated2010-08-10 v1
- ChecksumE74EBBCD4F124456
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GL348718 EMBL· GenBank· DDBJ | EFH47181.1 EMBL· GenBank· DDBJ | Genomic DNA |