A0A5A7QUL5 · A0A5A7QUL5_STRAF

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.

TypeIDPosition(s)Description
Site61Transition state stabilizer
Active site65Proton acceptor
Binding site66Ca2+ 1 (UniProtKB | ChEBI)
Binding site69Ca2+ 1 (UniProtKB | ChEBI)
Binding site71Ca2+ 1 (UniProtKB | ChEBI)
Binding site73Ca2+ 1 (UniProtKB | ChEBI)
Binding site75Ca2+ 1 (UniProtKB | ChEBI)
Binding site87Ca2+ 1 (UniProtKB | ChEBI)
Binding site160substrate
Binding site190Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site191Ca2+ 2 (UniProtKB | ChEBI)
Binding site235Ca2+ 2 (UniProtKB | ChEBI)
Binding site237Ca2+ 2 (UniProtKB | ChEBI)
Binding site242Ca2+ 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
      STAS_26259

Organism names

  • Taxonomic identifier
  • Strain
    • cv. UVA1
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Orobanchaceae > Buchnereae > Striga

Accessions

  • Primary accession
    A0A5A7QUL5

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_502315334023-314Peroxidase
Disulfide bond34↔113
Disulfide bond67↔72
Disulfide bond119↔310
Disulfide bond197↔224

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain24-314Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    314
  • Mass (Da)
    34,498
  • Last updated
    2019-11-13 v1
  • Checksum
    9CA42BE042B188F4
MKMAIFNLKVLAIVALLANTMADGLSMNYYVITCPIADIIIKNTVRTALISDPTLSGPLLRMHFHDCFVEGCDGSILIDSTKNNTAEKDSPANLSLRGYEIIDAAKEALERQCPGVVSCADILAMAARDAVFFSGGPYYEIPKGRKDGWRSKIEDTVRLPPPNLNSTELIDMFSRRGFSAREMVALSGAHTLGVARCLSFKSRLNRNADPTLDPQFAKTLSATCSKGDMAEQPFDSTRTVFDGQYYRALQRGTGVLFSDQTLFVGPATRAFVNGYAMNPASFFLDFQRSMVKMGTLDVKEGPNGEVRDNCRRVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BKCP01008404
EMBL· GenBank· DDBJ
GER49053.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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