A3PGF5 · PDXJ_CERS1
- ProteinPyridoxine 5'-phosphate synthase
- GenepdxJ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids252 (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 | 12 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 14-15 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: DH | ||||||
Binding site | 23 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 48 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 50 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 55 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 75 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 105 | 1-deoxy-D-xylulose 5-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Site | 156 | Transition state stabilizer | ||||
Sequence: E | ||||||
Active site | 199 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 200 | 3-amino-2-oxopropyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
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 > Rhodobacterales > Paracoccaceae > Cereibacter
Accessions
- Primary accessionA3PGF5
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000022401 | 1-252 | Pyridoxine 5'-phosphate synthase | |||
Sequence: MKPLGRLRLGVNIDHVATVRNARGTSYPDPLRAGLLAEAAGADGITAHLREDRRHIRDEDITALMQGLRVPLNLEMATTPEMQAIALRHKPHAVCLVPERREERTTEGGIDVAGDIGRLKDFVAPLRAAGCRVSMFIGHDVRQIEASAEIGAAVVELHTGHYCDLVAEGRTAEAARELEALREGAALAHSLGLEVHAGHGISYDTVAEIAAFPQVMELNIGHFLIGEAIFRGLGSAIEGMRRRMDAAREAAA |
Interaction
Subunit
Homooctamer; tetramer of dimers.
Structure
Sequence
- Sequence statusComplete
- Length252
- Mass (Da)27,132
- Last updated2007-04-03 v1
- Checksum12878857ED43ECB1
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000577 EMBL· GenBank· DDBJ | ABN75421.1 EMBL· GenBank· DDBJ | Genomic DNA |