A0A6B8JPX6 · A0A6B8JPX6_9GAMM

  • 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.

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
Site95Transition state stabilizer
Active site99Proton acceptor
Binding site267Fe (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
      GJ672_06100

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 2438
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Ectothiorhodospiraceae > Spiribacter

Accessions

  • Primary accession
    A0A6B8JPX6

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for cross-link.

TypeIDPosition(s)Description
Cross-link226↔252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-98)

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.

TypeIDPosition(s)Description
Region106-125Disordered
Compositional bias110-125Polar residues
Domain132-426Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    725
  • Mass (Da)
    80,821
  • Last updated
    2020-06-17 v1
  • Checksum
    E8F64658D54FC450
MAAADMDKAGKCPVMHGGATTEGSDNMEWWPNALNLDILHQHDSKTNPLGEHFNYREEVKKLDHQALWNDMHALLKDSQSWWPADWGHYGGLMIRMAWHAAGSYRTSDGRGGGGTGNQRFAPLNSWPDNTNLDKARRLLWPLKQKYGNQVSWADLIILAGTVSYESMGLKVFGFGYGREDIWHPEKDIYWGSEKEWLAPSEERYEDVEQPETMENPLAAVQMGLIYVNPEGVNGNPDPLKTAEQVRVTFARMAMNDEETVALTAGGHTVGKCHGNGDAELLGPDPEAADVEEQGLGWNNHSTRGVGRDTVTSGIEGAWTTHPTQWDNGYFDLLFNYDWELKKSPAGAWQWEPVDIKEEDKPVDVEDPSIRLNPIMTDADMAMIKDPAYRKISERFYNDPEYFSEVFARAWFKLTHRDMGPKARYIGPHVPDEDLIWQDPVPAGSTDYDVDAVKAKIADSGLSVSEMVATAWDSARTFRGSDLRGGANGARIRLAPQKDWEGNEPQRLQKVLGVLEPIARESGASLADVIVLAGNVGVEQAARAAGLSTDVPFAPGRGDASEEQTDAESFEVLEPEADGFRNWMKKDYVVSAEELMLDRAQLLGLTGPEMTVLVGGMRAMGTNHGGSKHGVFTDREGALTNDFFVNLCDMGNTWKPVASNRYEVRDRQTDELKWTATRADLVFGSNSILRSYSELYAQNDNQEKFVKDFVNAWTKVMNADRFDLEA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias110-125Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP046046
EMBL· GenBank· DDBJ
QGM21878.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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