A0A4Q3Z1N0 · A0A4Q3Z1N0_9RHOB
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids732 (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 > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Salipiger
Accessions
- Primary accessionA0A4Q3Z1N0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Cross-link | 226↔252 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-99) | ||||
Sequence: YVNPEGPDGNPDPAASAHDIRDTFGRM |
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 | 1-28 | Disordered | ||||
Sequence: MDGSDTSGGCPVIHGATTHTTNRGRSNR | ||||||
Compositional bias | 11-28 | Polar residues | ||||
Sequence: PVIHGATTHTTNRGRSNR | ||||||
Domain | 133-427 | Plant heme peroxidase family profile | ||||
Sequence: LDKARRLLWPIKQKYGNALSWADLFILTGNVAMETMGFKTFGFGGGREDIYEPEEDIYWGMEDTWLDGAARYGDQAEGRYLENPLAAVQMGLIYVNPEGPDGNPDPAASAHDIRDTFGRMAMGDEETVALIAGGHTFGKAHGNGDATILGAEPEGGAMEDMGFGWKNPFETGHGEHTVTSGLEGAWTQKPTAWDNGYFETLFGYEWELTKSPAGAHQWKPKGDAGAGTVPDAHNPGKSHQPMMFTSDLALLADPVYREIAERFRNDPQAFADAYARAWFKLTHRDMGPKVRYLGD | ||||||
Region | 348-370 | Disordered | ||||
Sequence: HQWKPKGDAGAGTVPDAHNPGKS | ||||||
Region | 558-581 | Disordered | ||||
Sequence: FTPGRADATEEQTDAESFEPLEPK | ||||||
Compositional bias | 566-580 | Basic and acidic residues | ||||
Sequence: TEEQTDAESFEPLEP |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length732
- Mass (Da)80,305
- Last updated2019-07-31 v1
- Checksum4D893819C8870497
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 11-28 | Polar residues | ||||
Sequence: PVIHGATTHTTNRGRSNR | ||||||
Compositional bias | 566-580 | Basic and acidic residues | ||||
Sequence: TEEQTDAESFEPLEP |
Keywords
- Technical term