A0A014MHQ3 · A0A014MHQ3_9BURK
- ProteinPyridoxine 5'-phosphate synthase
- GenepdxJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids257 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
Catalytic activity
- 3-amino-2-oxopropyl phosphate + 1-deoxy-D-xylulose 5-phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O + H+
Pathway
Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 15 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 26 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | |||
Active site | 51 | Proton acceptor | |||
Binding site | 53 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Binding site | 58 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Active site | 82 | Proton acceptor | |||
Binding site | 112 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | |||
Site | 163 | Transition state stabilizer | |||
Active site | 203 | Proton donor | |||
Binding site | 204 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | |||
Binding site | 226-227 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | pyridoxine 5'-phosphate synthase activity | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxine 5'-phosphate synthase
- EC number
- Short namesPNP synthase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Comamonas
Accessions
- Primary accessionA0A014MHQ3
Proteomes
Subcellular Location
Interaction
Structure
Sequence
- Sequence statusComplete
- Length257
- Mass (Da)27,576
- Last updated2014-06-11 v1
- MD5 Checksum5ED5B8A24566494D57A339F1EF2BCDA4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JBOK01000003 EMBL· GenBank· DDBJ | EXU81246.1 EMBL· GenBank· DDBJ | Genomic DNA |