A0A7J0GF25 · A0A7J0GF25_9ERIC
- ProteinPeroxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Removal of H2O2, oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress.
Catalytic activity
- 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 calcium ions per subunit.
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 | 55 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 59 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 60 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 63 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 65 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 67 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 69 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 81 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 153 | substrate | ||||
Sequence: P | ||||||
Binding site | 183 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 184 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 233 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 241 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Cellular Component | plasmodesma | |
Molecular Function | heme binding | |
Molecular Function | lactoperoxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeroxidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Actinidiaceae > Actinidia
Accessions
- Primary accessionA0A7J0GF25
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MKIAFVFICLVVPLVTA | ||||||
Chain | PRO_5029936653 | 18-355 | Peroxidase | |||
Sequence: QLRVGFYNPTCPRAEKIVRDVVLKRFRTDRSITAALLRMHFHDCFVRGCDASILIDSTKNKSSEKDAGPNLTVRGYELIDEAKKALEIACPETVSCADIITIATRDSVALAGGQNYNVTTGRRDGLVSDPSLVNLPGPTASVSQALSFFTAKKMTLNDMVTLLGAHTVGVAHCSFFQDRLSNFQGTGRPDPTMDPALVSKLSTICGRPNNPTAFLDQNTSFVVDNEFYRQIRSNRGVMQIDQELASDKASAPIVANFANNAFGFQQSFANAMVKMGGIEVLVGKAGEIRKNCRVVNPPPTQKKSSQKRSRVPHVLRKGEVKRDNAKKLMDPNELNAYQ | ||||||
Disulfide bond | 28↔107 | |||||
Sequence: CPRAEKIVRDVVLKRFRTDRSITAALLRMHFHDCFVRGCDASILIDSTKNKSSEKDAGPNLTVRGYELIDEAKKALEIAC | ||||||
Disulfide bond | 61↔66 | |||||
Sequence: CFVRGC | ||||||
Disulfide bond | 113↔309 | |||||
Sequence: CADIITIATRDSVALAGGQNYNVTTGRRDGLVSDPSLVNLPGPTASVSQALSFFTAKKMTLNDMVTLLGAHTVGVAHCSFFQDRLSNFQGTGRPDPTMDPALVSKLSTICGRPNNPTAFLDQNTSFVVDNEFYRQIRSNRGVMQIDQELASDKASAPIVANFANNAFGFQQSFANAMVKMGGIEVLVGKAGEIRKNC | ||||||
Disulfide bond | 190↔222 | |||||
Sequence: CSFFQDRLSNFQGTGRPDPTMDPALVSKLSTIC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-313 | Plant heme peroxidase family profile | ||||
Sequence: QLRVGFYNPTCPRAEKIVRDVVLKRFRTDRSITAALLRMHFHDCFVRGCDASILIDSTKNKSSEKDAGPNLTVRGYELIDEAKKALEIACPETVSCADIITIATRDSVALAGGQNYNVTTGRRDGLVSDPSLVNLPGPTASVSQALSFFTAKKMTLNDMVTLLGAHTVGVAHCSFFQDRLSNFQGTGRPDPTMDPALVSKLSTICGRPNNPTAFLDQNTSFVVDNEFYRQIRSNRGVMQIDQELASDKASAPIVANFANNAFGFQQSFANAMVKMGGIEVLVGKAGEIRKNCRVVN | ||||||
Region | 309-355 | Disordered | ||||
Sequence: CRVVNPPPTQKKSSQKRSRVPHVLRKGEVKRDNAKKLMDPNELNAYQ | ||||||
Compositional bias | 329-346 | Basic and acidic residues | ||||
Sequence: PHVLRKGEVKRDNAKKLM |
Sequence similarities
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)38,900
- Last updated2021-04-07 v1
- ChecksumFF1AB337CA0D333D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 329-346 | Basic and acidic residues | ||||
Sequence: PHVLRKGEVKRDNAKKLM |
Keywords
- Technical term