B0CHH2 · PDXJ_BRUSI
- ProteinPyridoxine 5'-phosphate synthase
- GenepdxJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids246 (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 | 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 | 76 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 106 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 157 | Transition state stabilizer | ||||
Sequence: E | ||||||
Active site | 198 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 199 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 221-222 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionB0CHH2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000078814 | 1-246 | Pyridoxine 5'-phosphate synthase | |||
Sequence: MPAKLSVNLNAIAMLRNRRDLPWPSVTGLGRAALAAGAAGLTVHPRPDQRHIRFSDLGDIRALIDDEYPQAEFNIEGFPSEAFLDLVEKHEPEQVTLVPDDPMQATSDHGWDFMSKADFLAPIVARLKGRGMRVSLFADPDSLGYERAKAIGADHVELYTGPYGATHDDPAAAARELDRLEKAARAATALGLAVNAGHDLTVDNLPALVKRIPQLAEVSIGHGLTADALMYGIPVTVSRYITALAG |
Interaction
Subunit
Homooctamer; tetramer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length246
- Mass (Da)26,447
- Last updated2008-02-26 v1
- Checksum6E44F12BD0FC15CF
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000911 EMBL· GenBank· DDBJ | ABY38473.1 EMBL· GenBank· DDBJ | Genomic DNA |