A9M007 · PDXH_NEIM0
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids210 (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 | 7-10 | substrate | ||||
Sequence: REDY | ||||||
Binding site | 60-65 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RMVLLK | ||||||
Binding site | 65 | substrate | ||||
Sequence: K | ||||||
Binding site | 75-76 | FMN (UniProtKB | ChEBI) | ||||
Sequence: FT | ||||||
Binding site | 81 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 82 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 104 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 122 | substrate | ||||
Sequence: Y | ||||||
Binding site | 126 | substrate | ||||
Sequence: R | ||||||
Binding site | 130 | substrate | ||||
Sequence: S | ||||||
Binding site | 139-140 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 183 | FMN (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 189-191 | substrate | ||||
Sequence: RLH | ||||||
Binding site | 193 | 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 > Betaproteobacteria > Neisseriales > Neisseriaceae > Neisseria
Accessions
- Primary accessionA9M007
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000186321 | 1-210 | Pyridoxine/pyridoxamine 5'-phosphate oxidase | |||
Sequence: MDLHNIREDYSKRELSEGDCADNPIEQFERWLDEAVRAEVNEPTAVNVAAVDGRGRPNSRMVLLKEVNSEGFVFFTNYHSRKGRSLDAHPFAAMTFFWPELERQVRVEGRVERLAEKLSDEYFESRPYQSRLGAWASAQSEVIPNKAVLVAKAAAVGLKHPLHVPRPPHWGGYIVIPDLLEFWQGRPSRLHDRIQYRLLDGGWIRERLSP |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length210
- Mass (Da)24,202
- Last updated2008-02-05 v1
- Checksum190FF6406877CB89
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000381 EMBL· GenBank· DDBJ | ABX73443.1 EMBL· GenBank· DDBJ | Genomic DNA |