A6WE21 · PDXH_KINRD
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids223 (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 | 8-11 | substrate | ||||
Sequence: RVDY | ||||||
Binding site | 60-65 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RTVLLK | ||||||
Binding site | 65 | substrate | ||||
Sequence: K | ||||||
Binding site | 75-76 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT | ||||||
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 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kineosporiales > Kineosporiaceae > Kineococcus
Accessions
- Primary accessionA6WE21
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000335788 | 1-223 | Pyridoxine/pyridoxamine 5'-phosphate oxidase | |||
Sequence: MEDPAGRRVDYGDRRFDEHDLAPTPLAQFQAWYSDAVEAGVVEPNAMTVATAGADGVSARTVLLKAVDGRGFVFYTNQRSRKALAIAHDPRVALLFTWHGTHRQVAVRGTAEEVPRAETEAYFASRPYGSRIGAWVSEQSRTTPSAAALHEREAQLRERWPDTGSPDDVPTPPHWGGYLVRALEVEFWQGRTSRLHDRLVLVAADGPARLDDPAPWRTERRQP |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length223
- Mass (Da)24,864
- Last updated2007-08-21 v1
- ChecksumA8EE8EF8CC392AE8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000750 EMBL· GenBank· DDBJ | ABS05060.1 EMBL· GenBank· DDBJ | Genomic DNA |