Q5I3F3 · Q5I3F3_TRIMO

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
Site4Transition state stabilizer
Active site8Proton acceptor
Binding site9Ca2+ 1 (UniProtKB | ChEBI)
Binding site12Ca2+ 1 (UniProtKB | ChEBI)
Binding site14Ca2+ 1 (UniProtKB | ChEBI)
Binding site16Ca2+ 1 (UniProtKB | ChEBI)
Binding site18Ca2+ 1 (UniProtKB | ChEBI)
Binding site25Ca2+ 1 (UniProtKB | ChEBI)
Binding site100substrate
Binding site130Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site131Ca2+ 2 (UniProtKB | ChEBI)
Binding site177Ca2+ 2 (UniProtKB | ChEBI)
Binding site180Ca2+ 2 (UniProtKB | ChEBI)
Binding site185Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

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

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Submitted names
    • Peroxidase 5

Gene names

    • Name
      POX5

Organism names

Accessions

  • Primary accession
    Q5I3F3

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond10↔15
Disulfide bond58↔255
Disulfide bond137↔162

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-259Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    259
  • Mass (Da)
    27,551
  • Last updated
    2005-02-15 v1
  • Checksum
    45D346728E13CAF3
SLLRLHFHDCFVQGCDASVLLSGMEQNAFPNVMSLRGFEVIDSIKAKLETMCKQTVSCADILTVAARDSVVALGGPSWTVPLGRRDSTNANEAVANSDLPPPFFDLVNLTQSFGDKGFTVTDMVALSGAHTIGQAQCLNFRDRLYNETNINSGFATSLKANCPQPTGSGDRNLANLDVLTPYSFDNAYYSNLKSQKGLLHSDQVLFTGTGGGTDNTVNNFASNPAAFSSAFASAMVKMGNLSPLTGSQGQVRLSCSKVN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY857759
EMBL· GenBank· DDBJ
AAW52719.1
EMBL· GenBank· DDBJ
mRNA

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