A0A5A7QJ94 · A0A5A7QJ94_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
Site77Transition state stabilizer
Active site81Proton acceptor
Binding site82Ca2+ 1 (UniProtKB | ChEBI)
Binding site85Ca2+ 1 (UniProtKB | ChEBI)
Binding site87Ca2+ 1 (UniProtKB | ChEBI)
Binding site89Ca2+ 1 (UniProtKB | ChEBI)
Binding site101Ca2+ 1 (UniProtKB | ChEBI)
Binding site176substrate
Binding site206Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site207Ca2+ 2 (UniProtKB | ChEBI)
Binding site262Ca2+ 2 (UniProtKB | ChEBI)
Binding site265Ca2+ 2 (UniProtKB | ChEBI)
Binding site270Ca2+ 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_20859

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
    A0A5A7QJ94

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_502312857321-338Peroxidase
Disulfide bond50↔128
Disulfide bond83↔86
Disulfide bond134↔337
Disulfide bond213↔249

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain40-338Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    338
  • Mass (Da)
    36,243
  • Last updated
    2019-11-13 v1
  • Checksum
    76B699247F439BF4
MGIYLATIYLILLNFSASFANITNTTVSNEAEACVDANIVLSFNFYINSCPEAEPIVFSWVEKALSDDPRMAASLLRLHFHDCFGCDASVLLDDTLGFVGEKTAAPNANSLRGFEVIDAIKADLEYVCPQTVSCADILAIAARDSVVLSGGPGWEVEMGRKDSVGANKAAANSNIPAPNSDLSTLLSKFQNLGLSLQDMVALSGAHTMGKARCSTFAARLNNNNNTNDIISDNAPNVNLEFLQSLEQLCSQPSAGSTLADLDHSTPTTFDNQYYLNLLSGEGLLGSDQELLKEGPRGIIELYADDVDVFFEDFKKAMLKMGSLLGSGGAPGEIRRNCR

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue338

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BKCP01006815
EMBL· GenBank· DDBJ
GER43981.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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