A0A4Q3Z1N0 · A0A4Q3Z1N0_9RHOB

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
Site96Transition state stabilizer
Active site100Proton 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
      EU805_15455

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • IMCC34102
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Salipiger

Accessions

  • Primary accession
    A0A4Q3Z1N0

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for cross-link.

TypeIDPosition(s)Description
Cross-link226↔252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-99)

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
Region1-28Disordered
Compositional bias11-28Polar residues
Domain133-427Plant heme peroxidase family profile
Region348-370Disordered
Region558-581Disordered
Compositional bias566-580Basic and acidic residues

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    732
  • Mass (Da)
    80,305
  • Last updated
    2019-07-31 v1
  • Checksum
    4D893819C8870497
MDGSDTSGGCPVIHGATTHTTNRGRSNREWWPNQLNLKILHQNLPQTQPMDEGFDYRAAFQTLDLAAVKADLAALMTDSQDWWPADYGHYGPFFVRMAWHSSGTYRTADGRGGSSSGSQRFAPLNSWPDNGNLDKARRLLWPIKQKYGNALSWADLFILTGNVAMETMGFKTFGFGGGREDIYEPEEDIYWGMEDTWLDGAARYGDQAEGRYLENPLAAVQMGLIYVNPEGPDGNPDPAASAHDIRDTFGRMAMGDEETVALIAGGHTFGKAHGNGDATILGAEPEGGAMEDMGFGWKNPFETGHGEHTVTSGLEGAWTQKPTAWDNGYFETLFGYEWELTKSPAGAHQWKPKGDAGAGTVPDAHNPGKSHQPMMFTSDLALLADPVYREIAERFRNDPQAFADAYARAWFKLTHRDMGPKVRYLGDEVPQEDLIWQDPIPAWEHEVIGDSDVKELSQQILASGLSVPDLVHAAWSSASTFRGSDKRGGANGARIRLAPQKDWEVNDPARLANTLQVLDGIRSKFGKPVSLADMIVLGGTAAVEKAARDAGFDVSVPFTPGRADATEEQTDAESFEPLEPKSDGFRNYQLKSYTASPEELLVDRAQLLTLTAPEMTVLVGGLRALDANTGGVQYGVLTDRPGQLTNDFFVNLLDMRVEWKPDGEGATTYTGRDRKTGETRWTGTRCDLVFGSNSQLRAISEVYAQSDNASKFVQDFVAAWTKVMNADRFDLA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias11-28Polar residues
Compositional bias566-580Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SELQ01000009
EMBL· GenBank· DDBJ
RYH01187.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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