A0A7J9H515 · A0A7J9H515_9ROSI

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

TypeIDPosition(s)Description
Site40Transition state stabilizer
Active site44Proton acceptor
Binding site45Ca2+ 1 (UniProtKB | ChEBI)
Binding site48Ca2+ 1 (UniProtKB | ChEBI)
Binding site50Ca2+ 1 (UniProtKB | ChEBI)
Binding site52Ca2+ 1 (UniProtKB | ChEBI)
Binding site54Ca2+ 1 (UniProtKB | ChEBI)
Binding site66Ca2+ 1 (UniProtKB | ChEBI)
Binding site144substrate
Binding site174Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site175Ca2+ 2 (UniProtKB | ChEBI)
Binding site226Ca2+ 2 (UniProtKB | ChEBI)
Binding site229Ca2+ 2 (UniProtKB | ChEBI)
Binding site234Ca2+ 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
      Gohar_004397

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 0
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Malvales > Malvaceae > Malvoideae > Gossypium

Accessions

  • Primary accession
    A0A7J9H515

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond13↔96
Disulfide bond46↔51
Disulfide bond102↔302
Disulfide bond181↔213

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-306Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    306
  • Mass (Da)
    33,251
  • Last updated
    2021-04-07 v1
  • Checksum
    F4A17613772CFB96
SAQLRQNFYANSCSNVEAIVRGEVAKKFRQTFVTVPATLRLFFHDCFVQGCDASVMIASTGSNKAEKDHPDNLSLAGDGFDTVIKAKAAVDAVPSCRNKVSCADILALATRDVIAMSGGPSYAVELGRLDGLSSTAASVNGKLPHPTFNLNQLNSLFAANGLSQTDMIALSAAHTLGFSHCDKFSNRIYNFSRQNAVDPTLNKDYATQLQQMCPRNVDPRIAINMDPNTPRTFDNVYFQNLQKGQGLFTSDQVLFTDTRSRPTVDAWASNSQAFNQAFITAMSKLGRVGVKTGRNGNIRRNCASFN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABFAD010000008
EMBL· GenBank· DDBJ
MBA0804832.1
EMBL· GenBank· DDBJ
Genomic DNA

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