A0A0N7KM90 · A0A0N7KM90_ORYSJ

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

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.
heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.

Features

Showing features for site, active site, binding site.

Type
IDPosition(s)Description
Site62Transition state stabilizer
Active site66Proton acceptor
Binding site67Ca2+ 1 (UniProtKB | ChEBI)
Binding site70Ca2+ 1 (UniProtKB | ChEBI)
Binding site72Ca2+ 1 (UniProtKB | ChEBI)
Binding site74Ca2+ 1 (UniProtKB | ChEBI)
Binding site76Ca2+ 1 (UniProtKB | ChEBI)
Binding site88Ca2+ 1 (UniProtKB | ChEBI)
Binding site163substrate
Binding site193Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site194Ca2+ 2 (UniProtKB | ChEBI)
Binding site238Ca2+ 2 (UniProtKB | ChEBI)
Binding site241Ca2+ 2 (UniProtKB | ChEBI)
Binding site246Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionheme binding
Molecular Functionlactoperoxidase activity
Molecular Functionmetal ion binding
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxidase
  • EC number

Gene names

    • ORF names
      OSJNBa0016D02.15
    • Ordered locus names
      Os06g0546500

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Nipponbare
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    A0A0N7KM90

Proteomes

Genome annotation databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-23
ChainPRO_503973415824-318Peroxidase
Disulfide bond35↔115
Disulfide bond68↔73
Disulfide bond121↔314
Disulfide bond200↔225

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-318Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    318
  • Mass (Da)
    33,181
  • Last updated
    2020-02-26 v1
  • Checksum
    4B6318AD3923B072
MATQWVLVVVAVMAVLFAGGAAGGQLSTRYYDGKCPNVQSIVRAGMAQAVAAEPRMGASILRMFFHDCFVNGCDASILLDDTANFTGEKNAGPNANSVRGYEVIDAIKTQVEASCNATVSCADILALAARDAVNLLGGPTWTVQLGRRDALTASQSAANGNLPGPGSDLATLVTMFGNKGLSPRDMTALSGAHTLGQARCATFRSRIFGDGNVDAAFAALRQQACPQSGGDTTLAPIDVQTPDAFDNAYYANLVKKQGLFHSDQELFNGGSQDALVRKYAGNAGMFAADFAKAMVRMGALLPAAGTPTEVRLNCRKVN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP004731
EMBL· GenBank· DDBJ
BAD54114.1
EMBL· GenBank· DDBJ
Genomic DNA
AP008212
EMBL· GenBank· DDBJ
BAF19734.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp