A0A8R7PGU3 · A0A8R7PGU3_TRIUA
- ProteinPlant heme peroxidase family profile domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids488 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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. These functions might be dependent on each isozyme/isoform in each plant tissue.
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 | 228 | Transition state stabilizer | ||||
Sequence: R | ||||||
Active site | 232 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 233 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 238 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 240 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 242 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 251 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 355 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 356 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 407 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | peroxidase activity | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended namePlant heme peroxidase family profile domain-containing protein
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Triticodae > Triticeae > Triticinae > Triticum
Accessions
- Primary accessionA0A8R7PGU3
Proteomes
Genome annotation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MDRGRRRQWGVVCSALLLSALLAVASA | ||||||
Chain | PRO_5035722680 | 28-488 | Plant heme peroxidase family profile domain-containing protein | |||
Sequence: QSPSPARAPKPAPSLPAALRAAPRPSSPAVPAPKAPAASPAPKQTPSPSASPVPKPPTPRAPAQAPKPSSPAAPSASPVPKPPAPRAPAQAPKPPSPPSASPPPAAPPLPKPSPPPPAPSAPKPSPVAPAPAQKPSPPTTTPPPQKPSAPPSPTNSSPPTPSLALSPNFYAASCPSVELAVNDVVRSASTLDPSIPGKLLRMVFHDCFVEGCDASVLIQGSGTERTDPANLSLGGFNVIDEAKRLLEAVCPATVSCSDIIVLAARDAVTFTGGPSVPVSLGRRDSLVSLASNVRANIIDTGFSVDAMAASFASKGLSLDDLVTLSGGHTIGSAHCGTFRERFRPDANGSMVPVDGTMNAEYATELMRACAASGSAAVGCDDGSAAAFDNRYFSNLLDGRGLLRTDAVLVQNATTRARVAAFAQSQDSFFSSWAGSFARLTSLGVKTGSAGEVRRLCSSVNG | ||||||
Disulfide bond | 201↔277 | |||||
Sequence: CPSVELAVNDVVRSASTLDPSIPGKLLRMVFHDCFVEGCDASVLIQGSGTERTDPANLSLGGFNVIDEAKRLLEAVC | ||||||
Disulfide bond | 234↔239 | |||||
Sequence: CFVEGC | ||||||
Disulfide bond | 283↔483 | |||||
Sequence: CSDIIVLAARDAVTFTGGPSVPVSLGRRDSLVSLASNVRANIIDTGFSVDAMAASFASKGLSLDDLVTLSGGHTIGSAHCGTFRERFRPDANGSMVPVDGTMNAEYATELMRACAASGSAAVGCDDGSAAAFDNRYFSNLLDGRGLLRTDAVLVQNATTRARVAAFAQSQDSFFSSWAGSFARLTSLGVKTGSAGEVRRLC | ||||||
Disulfide bond | 362↔396 | |||||
Sequence: CGTFRERFRPDANGSMVPVDGTMNAEYATELMRAC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-191 | Disordered | ||||
Sequence: ASAQSPSPARAPKPAPSLPAALRAAPRPSSPAVPAPKAPAASPAPKQTPSPSASPVPKPPTPRAPAQAPKPSSPAAPSASPVPKPPAPRAPAQAPKPPSPPSASPPPAAPPLPKPSPPPPAPSAPKPSPVAPAPAQKPSPPTTTPPPQKPSAPPSPTNSSPPTPSLA | ||||||
Compositional bias | 53-187 | Pro residues | ||||
Sequence: SSPAVPAPKAPAASPAPKQTPSPSASPVPKPPTPRAPAQAPKPSSPAAPSASPVPKPPAPRAPAQAPKPPSPPSASPPPAAPPLPKPSPPPPAPSAPKPSPVAPAPAQKPSPPTTTPPPQKPSAPPSPTNSSPPT | ||||||
Domain | 191-487 | Plant heme peroxidase family profile | ||||
Sequence: ALSPNFYAASCPSVELAVNDVVRSASTLDPSIPGKLLRMVFHDCFVEGCDASVLIQGSGTERTDPANLSLGGFNVIDEAKRLLEAVCPATVSCSDIIVLAARDAVTFTGGPSVPVSLGRRDSLVSLASNVRANIIDTGFSVDAMAASFASKGLSLDDLVTLSGGHTIGSAHCGTFRERFRPDANGSMVPVDGTMNAEYATELMRACAASGSAAVGCDDGSAAAFDNRYFSNLLDGRGLLRTDAVLVQNATTRARVAAFAQSQDSFFSSWAGSFARLTSLGVKTGSAGEVRRLCSSVN |
Sequence similarities
Belongs to the peroxidase family. Ascorbate peroxidase subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length488
- Mass (Da)49,382
- Last updated2022-10-12 v1
- Checksum3EC398891B72F00F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 53-187 | Pro residues | ||||
Sequence: SSPAVPAPKAPAASPAPKQTPSPSASPVPKPPTPRAPAQAPKPSSPAAPSASPVPKPPAPRAPAQAPKPPSPPSASPPPAAPPLPKPSPPPPAPSAPKPSPVAPAPAQKPSPPTTTPPPQKPSAPPSPTNSSPPT |
Keywords
- Technical term