A0A2N7QZC7 · A0A2N7QZC7_9GAMM
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids195 (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 | 42-47 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RIVLLK | ||||||
Binding site | 47 | substrate | ||||
Sequence: K | ||||||
Binding site | 57-58 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT | ||||||
Binding site | 64 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 88 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 106 | substrate | ||||
Sequence: Y | ||||||
Binding site | 110 | substrate | ||||
Sequence: R | ||||||
Binding site | 114 | substrate | ||||
Sequence: S | ||||||
Binding site | 123-124 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 168 | FMN (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 174-176 | substrate | ||||
Sequence: RLH | ||||||
Binding site | 178 | 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 > Lysobacterales > Rhodanobacteraceae > Dyella
Accessions
- Primary accessionA0A2N7QZC7
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-100 | Pyridoxamine 5'-phosphate oxidase putative | ||||
Sequence: AGKAGEPEPTAMSLATVDAAGRVSSRIVLLKGADERGFRFYTNYESDKGSQVESHPQVALCFHWKQLRNAVQVRVEGVSRKVLP | ||||||
Domain | 155-195 | Pyridoxine 5'-phosphate oxidase dimerisation C-terminal | ||||
Sequence: WGGYVVEPDMVEFWYGAEYRLHERVRWSRHGQTWTSRLLYP |
Sequence similarities
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length195
- Mass (Da)22,538
- Last updated2018-04-25 v1
- Checksum4C1A249EA13AF661