A0A3G6T1E5 · A0A3G6T1E5_9FLAO
- ProteinPyridoxine/pyridoxamine 5'-phosphate oxidase
- GenepdxH
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids213 (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: RKVY | ||||||
Binding site | 62-67 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RMVLLK | ||||||
Binding site | 67 | substrate | ||||
Sequence: K | ||||||
Binding site | 77-78 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT | ||||||
Binding site | 83 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
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 > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium
Accessions
- Primary accessionA0A3G6T1E5
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-118 | Pyridoxamine 5'-phosphate oxidase putative | ||||
Sequence: EVSEANAMALSTVEEDGCPRTRMVLLKAYTHEGFIFYTNYNSRKGKAIQNNHKACLHFFWPSLERQIIIKADLEKVAE | ||||||
Domain | 173-213 | Pyridoxine 5'-phosphate oxidase dimerisation C-terminal | ||||
Sequence: WGGYIAKPYEIEFWQGRPNRLHDRIIYQLEDLDWKISRLAP |
Sequence similarities
Belongs to the pyridoxamine 5'-phosphate oxidase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length213
- Mass (Da)25,096
- Last updated2019-02-13 v1
- Checksum790FB08B75B197E6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP033932 EMBL· GenBank· DDBJ | AZB23172.1 EMBL· GenBank· DDBJ | Genomic DNA |