A0A0H3PIZ6 · A0A0H3PIZ6_ECO5C
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids218 (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 | 14-17 | substrate | ||||
Sequence: RREY | ||||||
Binding site | 67-72 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RIVLLK | ||||||
Binding site | 72 | substrate | ||||
Sequence: K | ||||||
Binding site | 82-83 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT | ||||||
Binding site | 88 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 89 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 111 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 129 | substrate | ||||
Sequence: Y | ||||||
Binding site | 133 | substrate | ||||
Sequence: R | ||||||
Binding site | 137 | substrate | ||||
Sequence: S | ||||||
Binding site | 146-147 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 191 | FMN (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 197-199 | substrate | ||||
Sequence: RLH | ||||||
Binding site | 201 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A0H3PIZ6
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-122 | Pyridoxamine 5'-phosphate oxidase putative | ||||
Sequence: LSQACEAKLADPTAMVVATVDEHGQPYQRIVLLKHYDEKGMVFYTNLGSRKAHQIENNPRVSLLFPWHTLERQVMVIGKAERLS | ||||||
Domain | 178-218 | Pyridoxine 5'-phosphate oxidase dimerisation C-terminal | ||||
Sequence: WGGFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP |
Sequence similarities
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length218
- Mass (Da)25,561
- Last updated2015-09-16 v1
- Checksum95582F0EA6D83923