P48534 · APX1_PEA
- ProteinL-ascorbate peroxidase, cytosolic
- GeneAPX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids250 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a key role in hydrogen peroxide removal.
Miscellaneous
Binds one cation per subunit; probably K+, but might also be Ca2+.
Catalytic activity
- H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 38 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 42 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 163 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 164 | K+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 180 | K+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 182 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 185 | K+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 187 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | heme binding | |
Molecular Function | L-ascorbate peroxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to oxidative stress | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to reactive oxygen species |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameL-ascorbate peroxidase, cytosolic
- EC number
- Short namesAP
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > Hologalegina > IRL clade > Fabeae > Pisum
Accessions
- Primary accessionP48534
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000055597 | 2-250 | L-ascorbate peroxidase, cytosolic | |||
Sequence: GKSYPTVSPDYQKAIEKAKRKLRGFIAEKKCAPLILRLAWHSAGTFDSKTKTGGPFGTIKHQAELAHGANNGLDIAVRLLEPIKEQFPIVSYADFYQLAGVVAVEITGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGLSDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLTGEKDGLLQLPSDKALLTDSVFRPLVEKYAADEDVFFADYAEAHLKLSELGFAEA |
Expression
Induction
By stress.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 113-137 | Disordered | ||||
Sequence: VPFHPGREDKPEPPPEGRLPDATKG | ||||||
Compositional bias | 115-137 | Basic and acidic residues | ||||
Sequence: FHPGREDKPEPPPEGRLPDATKG |
Sequence similarities
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length250
- Mass (Da)27,193
- Last updated2007-01-23 v2
- Checksum6F51006D0A13B42C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 115-137 | Basic and acidic residues | ||||
Sequence: FHPGREDKPEPPPEGRLPDATKG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M93051 EMBL· GenBank· DDBJ | AAA33645.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X62077 EMBL· GenBank· DDBJ | CAA43992.1 EMBL· GenBank· DDBJ | mRNA |