A0A3A5HLC8 · A0A3A5HLC8_9EURY

  • Protein
    Catalase-peroxidase
  • Gene
    katG
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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
Site84Transition state stabilizer
Active site88Proton acceptor
Binding site251Fe (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
      CIT03_07215

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Archaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanobacterium

Accessions

  • Primary accession
    A0A3A5HLC8

Proteomes

PTM/Processing

Features

Showing features for cross-link.

TypeIDPosition(s)Description
Cross-link210↔236Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-87)

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 domain, region, compositional bias.

TypeIDPosition(s)Description
Domain121-418Plant heme peroxidase family profile
Region331-358Disordered
Compositional bias342-356Basic and acidic residues

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    724
  • Mass (Da)
    81,421
  • Last updated
    2018-12-05 v1
  • Checksum
    79185C3441C304F9
MDKKTIKRANGGMTNIDWWPERLNLDILRQHSSKSDPMGEDFNYAEEFKSLDLDSLKKDLHELMTDSKDWWPADFGHYGPLFIRMAWHSAGTYRIGDGRGGGGSGSQRFAPLNSWPDNANLDKARRLLWPIKQKYGRKISWADLMILVGNVALESMGFKTFGFGGGREDIWEPEKDIYWGSESEWLEDERYTGDRELENPLAAVQMGLIYVNPEGPDGKPDPVAAARDIRESFARMAMNDEETVALIAGGHAFGKTHGAGDPSLVGPEPEAAPIQEQGLGWKSKFGTGKGNDTITGGPEVIWTNTPIKWDNNFFRILFEFEWELTKSPAGAYQWKPKGDAGDGTVPDPHDSSKRRTPGMLTTDLSLRLDPDYEKISRRFYENPDQFADAFARAWFKLTHRDMGPLSRYLGPEVPEEELIWQDPIPAVNHELINEEDINTLKDRIMDSDLTISEMVYTAWASASTFRGSDKRGGANGARIRLEPQKNWEVNQPSQLTKVLDILEGIQLEFNQTQSGNKMVSLADLIVLAGCAGVEQAVKNAGYDMEVPFTPGRMDASQEETDVDSFIYLEPIADGFRNYQKTIYAARPEELLVDKAQLLTLTVPEMTVLVGGLRAMNSNFEQSPNGVFTKKPEALTNDFFVNLLDMSTIWDASADDENLFEGRDRITGELKWTATRVDLIFGSNSELRALAEVYACDDSSEKFINDFIMAWDKVMNLDRFDLDLS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias342-356Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NPZC01000012
EMBL· GenBank· DDBJ
RJS48617.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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