A0A7J0GF25 · A0A7J0GF25_9ERIC

  • Protein
    Peroxidase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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
Site55Transition state stabilizer
Active site59Proton acceptor
Binding site60Ca2+ 1 (UniProtKB | ChEBI)
Binding site63Ca2+ 1 (UniProtKB | ChEBI)
Binding site65Ca2+ 1 (UniProtKB | ChEBI)
Binding site67Ca2+ 1 (UniProtKB | ChEBI)
Binding site69Ca2+ 1 (UniProtKB | ChEBI)
Binding site81Ca2+ 1 (UniProtKB | ChEBI)
Binding site153substrate
Binding site183Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site184Ca2+ 2 (UniProtKB | ChEBI)
Binding site233Ca2+ 2 (UniProtKB | ChEBI)
Binding site236Ca2+ 2 (UniProtKB | ChEBI)
Binding site241Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplant-type cell wall
Cellular Componentplasmodesma
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
      Acr_20g0011970

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • cv. Fuchu
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Actinidiaceae > Actinidia

Accessions

  • Primary accession
    A0A7J0GF25

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_502993665318-355Peroxidase
Disulfide bond28↔107
Disulfide bond61↔66
Disulfide bond113↔309
Disulfide bond190↔222

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain18-313Plant heme peroxidase family profile
Region309-355Disordered
Compositional bias329-346Basic and acidic residues

Sequence similarities

Belongs to the peroxidase family. Ascorbate peroxidase subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    355
  • Mass (Da)
    38,900
  • Last updated
    2021-04-07 v1
  • Checksum
    FF1AB337CA0D333D
MKIAFVFICLVVPLVTAQLRVGFYNPTCPRAEKIVRDVVLKRFRTDRSITAALLRMHFHDCFVRGCDASILIDSTKNKSSEKDAGPNLTVRGYELIDEAKKALEIACPETVSCADIITIATRDSVALAGGQNYNVTTGRRDGLVSDPSLVNLPGPTASVSQALSFFTAKKMTLNDMVTLLGAHTVGVAHCSFFQDRLSNFQGTGRPDPTMDPALVSKLSTICGRPNNPTAFLDQNTSFVVDNEFYRQIRSNRGVMQIDQELASDKASAPIVANFANNAFGFQQSFANAMVKMGGIEVLVGKAGEIRKNCRVVNPPPTQKKSSQKRSRVPHVLRKGEVKRDNAKKLMDPNELNAYQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias329-346Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BJWL01000020
EMBL· GenBank· DDBJ
GFZ09389.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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