A0A1B3CVH2 · A0A1B3CVH2_PSEFL
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids215 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic activity
- H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4+ + pyridoxal 5'-phosphate
Cofactor
Note: Binds 1 FMN per subunit.
Pathway
Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9-12 | substrate | ||||
Sequence: RRNY | ||||||
Binding site | 64-69 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RILLLK | ||||||
Binding site | 69 | substrate | ||||
Sequence: K | ||||||
Binding site | 86 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 108 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 126 | substrate | ||||
Sequence: Y | ||||||
Binding site | 130 | substrate | ||||
Sequence: R | ||||||
Binding site | 134 | substrate | ||||
Sequence: S | ||||||
Binding site | 143-144 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 188 | FMN (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 194-196 | substrate | ||||
Sequence: RLH | ||||||
Binding site | 198 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FMN binding | |
Molecular Function | pyridoxamine phosphate oxidase activity | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxine/pyridoxamine 5'-phosphate oxidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A1B3CVH2
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-117 | Pyridoxamine 5'-phosphate oxidase putative | ||||
Sequence: EANSMALATVDSQGHAHCRILLLKGFSAEGFFFFGHYQSAKGEELASNPHAAMTFFWPGLERQVRIEGPVVR | ||||||
Domain | 175-215 | Pyridoxine 5'-phosphate oxidase dimerisation C-terminal | ||||
Sequence: WGGYRLQPQRIEFWQGRPDRLHDRLDYRLHAGTWQRTRLAP |
Sequence similarities
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length215
- Mass (Da)24,604
- Last updated2016-11-02 v1
- Checksum6866A6915B4ECBDA