A0A6G1ZCW8 · A0A6G1ZCW8_9BACT
- ProteinPyridoxine 5'-phosphate synthase
- GenepdxJ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids239 (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
- 1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = H+ + 2 H2O + phosphate + pyridoxine 5'-phosphate
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 | 7 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 18 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 43 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 45 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 50 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 70 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 100 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 151 | Transition state stabilizer | ||||
Sequence: E | ||||||
Active site | 190 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 191 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 213-214 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: GH |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 > Bacteroidota > Bacteroidia > Bacteroidales > Tannerellaceae > Parabacteroides
Accessions
- Primary accessionA0A6G1ZCW8
Subcellular Location
Interaction
Subunit
Homooctamer; tetramer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length239
- Mass (Da)26,302
- Last updated2020-08-12 v1
- Checksum5BCBFCC69D44C297