A0AA49JTT1 · A0AA49JTT1_9BACT
- ProteinPyridoxine 5'-phosphate synthase
- GenepdxJ
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids240 (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 | 8 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 10-11 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DH | ||||||
Binding site | 19 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 44 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 46 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 71 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 101 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 152 | Transition state stabilizer | ||||
Sequence: E | ||||||
Active site | 189 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 190 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 211-212 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: GH |
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
- Strain
- Taxonomic lineageBacteria > Gemmatimonadota > Gemmatimonadia > Gemmatimonadales > Gemmatimonadaceae
Accessions
- Primary accessionA0AA49JTT1
Subcellular Location
Interaction
Subunit
Homooctamer; tetramer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length240
- Mass (Da)26,059
- Last updated2024-01-24 v1
- Checksum1E9E234DE2BE9375