A0A0F6RIY6 · A0A0F6RIY6_MICAE
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids214 (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
- pyridoxamine 5'-phosphate + O2 + H2O = pyridoxal 5'-phosphate + H2O2 + NH4+
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: RLDY | ||||||
Binding site | 62-67 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RMVLLK | ||||||
Binding site | 67 | substrate | ||||
Sequence: K | ||||||
Binding site | 77-78 | FMN (UniProtKB | ChEBI) | ||||
Sequence: FT | ||||||
Binding site | 84 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 106 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 124 | substrate | ||||
Sequence: Y | ||||||
Binding site | 128 | substrate | ||||
Sequence: R | ||||||
Binding site | 132 | substrate | ||||
Sequence: S | ||||||
Binding site | 141-142 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 186 | FMN (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 192-194 | substrate | ||||
Sequence: RLH | ||||||
Binding site | 196 | 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 > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Chroococcales > Microcystaceae > Microcystis
Accessions
- Primary accessionA0A0F6RIY6
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-120 | Pyridoxamine 5'-phosphate oxidase putative | ||||
Sequence: LEPNAMTLATISPEGKPRARMVLLKDFDPRGFVLFTNYQSAKGQELIANPNAALVFWWGELQRQIRIEGTVEKISEEE | ||||||
Domain | 173-214 | Pyridoxine 5'-phosphate oxidase dimerisation C-terminal | ||||
Sequence: WGGFRLIPSLIEFWQGRPSRLHDRLCYYRQEDGSWQRQRLAP |
Sequence similarities
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length214
- Mass (Da)24,929
- Last updated2015-07-22 v1
- ChecksumE48886A6137FABB3
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP011304 EMBL· GenBank· DDBJ | AKE62445.1 EMBL· GenBank· DDBJ | Genomic DNA |