A0A3R7IQC9 · A0A3R7IQC9_9EURY

Function

function

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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

TypeIDPosition(s)Description
Site74Transition state stabilizer
Active site78Proton acceptor
Binding site243Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Molecular Functioncatalase activity
Molecular Functionheme binding
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
    Catalase-peroxidase
  • EC number
  • Short names
    CP
  • Alternative names
    • Peroxidase/catalase

Gene names

    • Name
      katG
    • ORF names
      DVK01_03320

Organism names

  • Taxonomic identifier
  • Strain
    • Atlit-120R
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloarculaceae > Haloarcula

Accessions

  • Primary accession
    A0A3R7IQC9

Proteomes

PTM/Processing

Features

Showing features for cross-link.

TypeIDPosition(s)Description
Cross-link202↔228Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-77)

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, domain, compositional bias.

TypeIDPosition(s)Description
Region1-29Disordered
Domain111-390Plant heme peroxidase family profile
Region161-190Disordered
Compositional bias172-189Basic and acidic residues

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    715
  • Mass (Da)
    79,472
  • Last updated
    2019-04-10 v1
  • Checksum
    72E44AF81C8160D7
MAKRDHYRSPNQLSLDVLDQNARDADPRGDDFDYAEEFQKLDLDAVKADLEEVMTSSQDWWPADYGHYGPLFIRMAWHSAGTYRTTDGRGGASGGRQRFAPLNSWPDNANLDKARRLLWPIKKKYGRKLSWADLIVLAGNHAIESMGFETFGWAGGREDAFEPDEAVDWGPEDEMEAHQSERRNEDGTLREPLGAAVMGLIYVDPEGPNGNPDPLASAENIRESFGRMAMNDEETAALIAGGHTFGKVHGADDPEENLGAVPEDAPIEQMGLGWENDHGSGKAGDTITSGIEGPWTQAPTEWDSGYIDNLLDYEWEPEKGPGGAWQWTPTDEALENTVPDAHDPDEKRTPMMLTTDIALKRDPDYRDIMERFQDNPMEFGINFARAWYKLIHRDMGPPERFLGPDAPDEELIWQDPVPDADYDLVGDEEIADLKAEILDSGLSVTQLIKTAWASASTYRDSDKRGGANGARIRLEPQRSWEVNEPEQLETVLDTLEGIQEEFNGARDDDTRVSLADLIVLGGNAAVEQAAADAGYDVTVPFEPGRTDATPDQTDVESFEALKPRADGFRNYVRDDVEAPAEELLVDKADLLDLTPGEMTALVGGMRSLGATYQDSDLGVFTDEPGTLTNDFFQVVLGMDTEWEPVTEARDVFEGYDRDTGEQTWTASRVDLLFGSHARLRALAEVYGADDAEAELVDDFVDAWSKVMRLDRFDLE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias172-189Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QPLN01000001
EMBL· GenBank· DDBJ
RLM39604.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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