Q10LQ5 · Q10LQ5_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 site164substrate
Binding site194Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site195Ca2+ 2 (UniProtKB | ChEBI)
Binding site242Ca2+ 2 (UniProtKB | ChEBI)
Binding site249Ca2+ 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

    • Ordered locus names
      LOC_Os03g22020

Organism names

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

Accessions

  • Primary accession
    Q10LQ5
  • Secondary accessions
    • B9F8D0

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-24
ChainPRO_500999841025-326Peroxidase
Disulfide bond35↔115
Disulfide bond68↔73
Disulfide bond122↔320
Disulfide bond201↔227

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-324Plant 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
    326
  • Mass (Da)
    34,292
  • Last updated
    2006-08-22 v1
  • Checksum
    214753E3B0DB5159
MVSSAMAAVAVAFAVVVAATMSSAQLDPHFYDGLCPAALPTIKRIVEEAVAAEPRMGASLLRLHFHDCFVNGCDGSILLDDTPFFTGEKNAAPNMNSVRGFDVIDRIKDAVNAACRRNVVSCADIVAVAARDSIVTLGGPSYHVPLGRRDARTASQAAANSSIPAPTLNLDGLVSSFAAQGLSVQDLVLLSGAHTLGFSRCTNFRDRLYNETATLDASLAASLGGTCPRTAGAGDDNLAPLDPTPARFDAAYYASLLRARGLLHSDQQLFAGGGLGATDGLVRFYAANPDAFRRDFAESMVRMASLSPLVGSQGEVRVNCRKVNYY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DP000009
EMBL· GenBank· DDBJ
ABF95843.1
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.
Help