A0A2U8QS91 · A0A2U8QS91_9FLAO
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids739 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Catalytic activity
- 2 H2O2 = 2 H2O + O2
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Features
Showing features for site, active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | catalase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to hydrogen peroxide | |
Biological Process | hydrogen peroxide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCatalase-peroxidase
- EC number
- Short namesCP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Flavobacteriaceae > Flavobacterium
Accessions
- Primary accessionA0A2U8QS91
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Cross-link | 229↔255 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-101) | ||||
Sequence: YVNPEGPDGNPDPIAAAKDIRETFARM |
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.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MEHSKNGNGKCPFTGAANSHSAGGGGTRNRD | ||||||
Compositional bias | 11-25 | Polar residues | ||||
Sequence: CPFTGAANSHSAGGG | ||||||
Domain | 135-414 | Plant heme peroxidase family profile | ||||
Sequence: LDKARRLLWPIKQKYGKKISWADLMILAGNVALESMGFKTFGFAGGREDVWEPEEDIYWGSEQTWLAPSEAPKSRYSGERDLENPLAAVQMGLIYVNPEGPDGNPDPIAAAKDIRETFARMAMNDEETVALIAGGHTFGKTHGAGDPALVGAEPEAAGIEEQGLGWKSSFGSGKASDVITGGPEVTWTQTPTKWSNFFFENLFENEWELTKSPAGAYQWVAKATTESIPDAFDLTRRHRPTMLTTDLSLRLDPAYEKISRRFYENPDEFADAFARAWFKL |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length739
- Mass (Da)81,832
- Last updated2018-09-12 v1
- Checksum3B8AA82694DD1659
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-25 | Polar residues | ||||
Sequence: CPFTGAANSHSAGGG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP029463 EMBL· GenBank· DDBJ | AWM12724.1 EMBL· GenBank· DDBJ | Genomic DNA |