Q9NVS9 · PNPO_HUMAN
- ProteinPyridoxine-5'-phosphate oxidase
- GenePNPO
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids261 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Catalytic activity
- O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 FMN per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.1 μM | pyridoxine 5'-phosphate | |||||
6.2 μM | pyridoxamine 5'-phosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.1 μmol/min/mg | toward pyridoxine 5'-phosphate | ||||
0.05 μmol/min/mg | toward pyridoxamine 5'-phosphate |
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 | 42-45 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: RGDR | ||||||
Binding site | 95-98 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RMLL | ||||||
Binding site | 100 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 110-111 | FMN (UniProtKB | ChEBI) | ||||
Sequence: FT | ||||||
Binding site | 116-117 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RK | ||||||
Binding site | 139 | FMN (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 157 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 161 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 165 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 174-175 | FMN (UniProtKB | ChEBI) | ||||
Sequence: QS | ||||||
Binding site | 219 | FMN (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 225-227 | pyridoxal 5'-phosphate (UniProtKB | ChEBI) | ||||
Sequence: RLH | ||||||
Binding site | 229 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | FMN binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | pyridoxal phosphate binding | |
Molecular Function | pyridoxamine phosphate oxidase activity | |
Biological Process | pyridoxal phosphate biosynthetic process | |
Biological Process | pyridoxamine metabolic process | |
Biological Process | pyridoxine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyridoxine-5'-phosphate oxidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NVS9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Involvement in disease
Pyridoxine-5'-phosphate oxidase deficiency (PNPOD)
- Note
- DescriptionThe main feature of neonatal epileptic encephalopathy is the onset within hours of birth of a severe seizure disorder that does not respond to anticonvulsant drugs and can be fatal. Seizures can cease with the administration of PLP, being resistant to treatment with pyridoxine,.
- See alsoMIM:610090
Natural variants in PNPOD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078229 | 225 | R>H | in PNPOD; dbSNP:rs550423482 | |
VAR_078643 | 229 | R>Q | in PNPOD; dbSNP:rs773450573 | |
VAR_029360 | 229 | R>W | in PNPOD; strong activity decrease; dbSNP:rs104894629 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1-56 | Has no effect on the catalytic activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 1-72 | Loss of catalytic activity. | ||||
Sequence: Missing | ||||||
Natural variant | VAR_029358 | 50 | in dbSNP:rs549477447 | |||
Sequence: E → K | ||||||
Natural variant | VAR_029359 | 116 | in dbSNP:rs17679445 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_078229 | 225 | in PNPOD; dbSNP:rs550423482 | |||
Sequence: R → H | ||||||
Natural variant | VAR_078643 | 229 | in PNPOD; dbSNP:rs773450573 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_029360 | 229 | in PNPOD; strong activity decrease; dbSNP:rs104894629 | |||
Sequence: R → W | ||||||
Mutagenesis | 238-261 | Loss of catalytic activity. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 298 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000167783 | 1-261 | UniProt | Pyridoxine-5'-phosphate oxidase | |||
Sequence: MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP | |||||||
Modified residue (large scale data) | 40 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 238 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 241 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 241 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Expressed in liver, brain, lung, prostate and stomach (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NVS9 | AGTRAP Q6RW13-2 | 6 | EBI-11030787, EBI-11522760 | |
BINARY | Q9NVS9 | CMTM5 Q96DZ9-2 | 3 | EBI-11030787, EBI-11522780 | |
BINARY | Q9NVS9 | LIME1 Q9H400 | 3 | EBI-11030787, EBI-2830566 | |
BINARY | Q9NVS9 | MTERF1 Q99551 | 3 | EBI-11030787, EBI-2690033 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q9NVS9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length261
- Mass (Da)29,988
- Last updated2000-10-01 v1
- Checksum2C74E9F962FE2A95
Q9NVS9-2
- Name2
- NoteMay be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Q9NVS9-3
- Name3
- Differences from canonical
- 122-139: Missing
Q9NVS9-4
- Name4
- Differences from canonical
- 140-182: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A286YF16 | A0A286YF16_HUMAN | PNPO | 34 | ||
A0A286YF38 | A0A286YF38_HUMAN | PNPO | 72 | ||
A0A286YFL3 | A0A286YFL3_HUMAN | PNPO | 151 | ||
A0A286YFA1 | A0A286YFA1_HUMAN | PNPO | 46 | ||
J3QQV6 | J3QQV6_HUMAN | PNPO | 165 | ||
J3QQZ9 | J3QQZ9_HUMAN | PNPO | 238 |
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_058769 | 47-69 | in isoform 2 | |||
Sequence: AFEETHLTSLDPVKQFAAWFEEA → RWKTLCSHVAAEGLRERWLPLLH | ||||||
Alternative sequence | VSP_058770 | 70-261 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_056410 | 122-139 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_056411 | 140-182 | in isoform 4 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF468030 EMBL· GenBank· DDBJ | AAM76918.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001397 EMBL· GenBank· DDBJ | BAA91668.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303536 EMBL· GenBank· DDBJ | BAG64562.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AK303665 EMBL· GenBank· DDBJ | BAG64664.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303792 EMBL· GenBank· DDBJ | BAG64749.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94770.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94771.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC006525 EMBL· GenBank· DDBJ | AAH06525.1 EMBL· GenBank· DDBJ | mRNA |