A0A5E4EH34 · A0A5E4EH34_PRUDU

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

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
Site68Transition state stabilizer
Active site72Proton acceptor
Binding site73Ca2+ 1 (UniProtKB | ChEBI)
Binding site76Ca2+ 1 (UniProtKB | ChEBI)
Binding site78Ca2+ 1 (UniProtKB | ChEBI)
Binding site80Ca2+ 1 (UniProtKB | ChEBI)
Binding site82Ca2+ 1 (UniProtKB | ChEBI)
Binding site94Ca2+ 1 (UniProtKB | ChEBI)
Binding site169substrate
Binding site199Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site200Ca2+ 2 (UniProtKB | ChEBI)
Binding site247Ca2+ 2 (UniProtKB | ChEBI)
Binding site250Ca2+ 2 (UniProtKB | ChEBI)
Binding site255Ca2+ 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
      ALMOND_2B026039

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Texas
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus

Accessions

  • Primary accession
    A0A5E4EH34

Proteomes

Genome annotation databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-30
ChainPRO_502315331431-327Peroxidase
Disulfide bond41↔121
Disulfide bond74↔79
Disulfide bond127↔323
Disulfide bond206↔232

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain31-327Plant 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
    327
  • Mass (Da)
    35,336
  • Last updated
    2019-11-13 v1
  • Checksum
    1C5839960020BA45
MTKSFSFTSHANVAFAMLLLFFIMSTASQAQLSSTFYDRTCPNALATIKSSISRAVSQERRMAASLMRLHFHDCFVQGCDASLLLNDSASIVSEKNAFQNRGSARGFEVIDDAKAQVEKICPGVVSCADILAVAARDASVAVSGPSWTVKLGRRDATKASQAQAESDLPLFTDSLDRLISRFGDRGLSPRDLVALSGAHTIGQAQCFTFRDRIYNNGSDIDSNFATTRRRRCPAAAPNGNTNLAPLDLVTPNSFDYNYFKNLIQKKGLLESDQVLFSGGSTDSIVSEYSSKPATFRSDFGIAMIKMGDVSPLTGSAGEIRRICTAVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CABIKO010000011
EMBL· GenBank· DDBJ
VVA14686.1
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.
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