A0A2R6W6E3 · A0A2R6W6E3_MARPO

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.

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
Site154Transition state stabilizer
Active site158Proton acceptor
Binding site159Ca2+ 1 (UniProtKB | ChEBI)
Binding site162Ca2+ 1 (UniProtKB | ChEBI)
Binding site164Ca2+ 1 (UniProtKB | ChEBI)
Binding site166Ca2+ 1 (UniProtKB | ChEBI)
Binding site168Ca2+ 1 (UniProtKB | ChEBI)
Binding site180Ca2+ 1 (UniProtKB | ChEBI)
Binding site255substrate
Binding site285Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site286Ca2+ 2 (UniProtKB | ChEBI)
Binding site337Ca2+ 2 (UniProtKB | ChEBI)
Binding site346Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplant-type cell wall
Molecular Functionheme binding
Molecular Functionlactoperoxidase activity
Molecular Functionmetal ion binding
Molecular Functionperoxidase activity
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to oxidative stress
Biological Processresponse to stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peroxidase
  • EC number

Gene names

    • ORF names
      MARPO_0141s0008

Organism names

Accessions

  • Primary accession
    A0A2R6W6E3

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_501521212231-419Peroxidase
Disulfide bond127↔207
Disulfide bond160↔165
Disulfide bond213↔415
Disulfide bond292↔324

Keywords

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias29-49Basic and acidic residues
Region29-117Disordered
Compositional bias61-117Pro residues
Domain121-419Plant 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
    419
  • Mass (Da)
    44,128
  • Last updated
    2018-06-20 v1
  • Checksum
    1729246C136385F9
MSITRRRVHAVTTVCIAFLLVSAVLTKADGRGDRNRDSNDSRDRGRNGRGGWGGRSPWRGGRTPPSPPPPIRAPASPTPPIRAPASPPPPIRAPASPPPAATPPPASPPPPPPPAVNDPVSFYSSACPAARNLVASTVQSAVQNDRGLPAALLRMQFHDCFVRGCDASILLDSTQSSLAEKDGVGNAFSVRGYEVIDAVKSAVENVCPGVVSCADIVALATRDAIVSIGGPSWKVVSGRRDGLVSLATETPSNLPPPNADYAFLVNRFTRKGLTEKEMVVLSGAHTIGVTHCGMIAGRLYNNTGPNGVDPTLDPTYGAALQQQCPFGQNVMTEVELDPTNGGNAFDSVYYTNIQDKKVLFSSDATLITTAAGRSLVQAEATGSTVPFFADFAAAMENMINIQVLRAPAGEIRQNCRFRN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias29-49Basic and acidic residues
Compositional bias61-117Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KZ772812
EMBL· GenBank· DDBJ
PTQ29425.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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