Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A6J4H3Y7 · A0A6J4H3Y7_9ACTN

Function

function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.

Features

Showing features for site, active site, binding site.

Type
IDPosition(s)Description
Site102Transition state stabilizer
Active site106Proton acceptor
Binding site268Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncatalase activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Biological Processcellular response to hydrogen peroxide
Biological Processhydrogen peroxide catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Catalase-peroxidase
  • EC number
  • Short names
    CP
  • Alternative names
    • Peroxidase/catalase

Gene names

    • Name
      katG
    • ORF names
      AVDCRST_MAG20-239

Organism names

Accessions

  • Primary accession
    A0A6J4H3Y7

Subcellular Location

PTM/Processing

Features

Showing features for cross-link.

TypeIDPosition(s)Description
Cross-link227↔253Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-105)

Post-translational modification

Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme.

Interaction

Subunit

Homodimer or homotetramer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-34Disordered
Compositional bias20-34Polar residues
Domain139-414Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    738
  • Mass (Da)
    81,012
  • Last updated
    2020-10-07 v1
  • MD5 Checksum
    EB8BADC7D23A1EB0ABA80D0642795FF9
MSDIETGSGGEGSESENPAIDAPTVKSTRPRTNQDWWPNQLDLKVLHQHSPLSNPMGPDHKYPEAFAGLDVDALKRDVMGVMTSSQDWWPADYGHYGPLFIRMAWHSAGTYRIADGRGGAGDGSQRFAPLNSWPDNANLDKARRLLWPVKQKYGQKLSWADLIVFTGNCALESMGFETFGFAFGREDIWEPEEIFWGPEDTWLGDERYSGERELADKVGAVQMGLIYVNPEGPNGNPDPMASARDIRETFARMAMNDVETAALIVGGHTFGKCHGAVSPDYVGPEPEACPVEAQGFGWHNTAGQGNGPDTITSGLEGAWTNEPAKWDNGYLENLFKYDWELTESPAGAKQWTPKDPAAADDVPDAHIASKRHAPIMLTSDMAMKVDPTYRAIVERWHEHPEELADAFAKAWYKLLHRDMGPLARYLGPWVPEPQLWQDPVPAVDHELIGDEDVATLKARLLESGLSVSQLVSTAWRSASSFRGTDKRGGANGARIRLEPQRSWEVNEPAELGAALQVLEQVQQDFNASQSGGKKVSLADVIVLGGCAAVEEAARRAGHDVTVPFAPGRTDASQEQTDVDSFSVLEPHADGFLNYLRAGEKLQPETLLLDRANLLTLTAPEMTVLIGGMRALDTGVGGAKHGVFTEQPGTLTNDFFVNLIDMSTEWKPSVSSENVYEGRDRATGEARWTATAVDLVFGSNSQLRGLAELYAGDDAKEKFVRDFVAAWDKVMNLDRYDLV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias20-34Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CADCSY010000010
EMBL· GenBank· DDBJ
CAA9213371.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help