A0AAD7KTQ5 · A0AAD7KTQ5_QUISA

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.

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.

Type
IDPosition(s)Description
Site101Transition state stabilizer
Active site105Proton acceptor
Binding site106Ca2+ 1 (UniProtKB | ChEBI)
Binding site109Ca2+ 1 (UniProtKB | ChEBI)
Binding site111Ca2+ 1 (UniProtKB | ChEBI)
Binding site113Ca2+ 1 (UniProtKB | ChEBI)
Binding site115Ca2+ 1 (UniProtKB | ChEBI)
Binding site127Ca2+ 1 (UniProtKB | ChEBI)
Binding site202substrate
Binding site232Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site284Ca2+ 2 (UniProtKB | ChEBI)
Binding site286Ca2+ 2 (UniProtKB | ChEBI)
Binding site291Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular Functionperoxidase activity
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
      O6P43_030488

Organism names

  • Taxonomic identifier
  • Strain
    • S10
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Quillajaceae > Quillaja

Accessions

  • Primary accession
    A0AAD7KTQ5

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond74↔154
Disulfide bond107↔112
Disulfide bond160↔357
Disulfide bond239↔271

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain64-361Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    390
  • Mass (Da)
    43,940
  • Last updated
    2024-05-29 v1
  • MD5 Checksum
    87108E85B1B9476DAA6B171535A981B0
MKWGKWQSFCTSIQKKFKEAPHESQKPNTTIQFLADPSKFNTTSQMAPLFLLFLLHVTTLSAADLRPGFYSETCPEAEFIVRDVMKKALIREPRSVASVMRFQFHDCFVNGCDASMLLDDTPTMLGEKFALSNINSLRSYEVVDDVKEALESVCPGIVSCADIIIMASRDAVALTGGPYWEVRLGRLDSLSASQEDSNNIMPSPRSNASYLIDLFQKYSLSVKDLVALSGSHSIGQGRCFSIMFRLYNQSGSGQPDPAIEPKFREKLDKLCPLNVDQNVTGDLDATPQVFDNQYFKDLVAGRGFLNSDQTLFTFPHTKKFVKLYSKDQGEFFKDFVEGMLKMGDLQSGRPGEVRKNCRVVTGHQANSFWELTKEREENYKVIKSTTRFCC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JARAOO010000013
EMBL· GenBank· DDBJ
KAJ7945428.1
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