Q8W3D0 · PDX12_ORYSJ
- ProteinProbable pyridoxal 5'-phosphate synthase subunit PDX1.2
- GenePDX12
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids313 (go to sequence)
- Protein existenceEvidence at transcript level
- 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.
Miscellaneous
Vitamin B6 is an essential quencher of singlet oxygen in plants, that can protect cellular membranes from lipid peroxidation.
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 | 42 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 99 | Schiff-base intermediate with D-ribose 5-phosphate | ||||
Sequence: K | ||||||
Binding site | 171 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 183 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 232 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 253-254 | D-ribose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: GS |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | amine-lyase activity | |
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 nameProbable pyridoxal 5'-phosphate synthase subunit PDX1.2
- EC number
- Short namesPLP synthase subunit PDX1.2
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ8W3D0
- Secondary accessions
Proteomes
Genome annotation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000270628 | 1-313 | UniProt | Probable pyridoxal 5'-phosphate synthase subunit PDX1.2 | |||
Sequence: MASDGTDVVALYGGANGLSHKSGSFSVKVGLAQMLRGGVIMDVVTPEQARIAEEAGACAVMALERVPADIRAQGGVARMSDPGLIRDIKRSVTIPVMAKARIGHLVEAQILEAIGVDYVDESEVLTLADDAHHINKNNFRVPFVCGCRDLGEALRRIREGAAMIRTKGEAGTGNVVEAVRHVRSVMGDIRALRSMDDDEVFSYAKRIAAPYDLVMQTKQLGRLPVVQFAAGGVATPADAALMMQLGCDGVFVGSGIFKSGDPALRARAIVQAVTHYSDPKILAEVSSGLGEAMVGINLSDPKIHVERFAARSD | |||||||
Modified residue (large scale data) | 24 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length313
- Mass (Da)33,149
- Last updated2002-03-01 v1
- Checksum62A60E7A039FAAD9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC079632 EMBL· GenBank· DDBJ | AAL73561.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC108883 EMBL· GenBank· DDBJ | AAM08638.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DP000086 EMBL· GenBank· DDBJ | AAP51743.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008216 EMBL· GenBank· DDBJ | BAF25924.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014966 EMBL· GenBank· DDBJ | BAT09558.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK060323 EMBL· GenBank· DDBJ | BAG87405.1 EMBL· GenBank· DDBJ | mRNA |