A0A5C8KNH4 · A0A5C8KNH4_9GAMM
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids741 (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 = O2 + 2 H2O
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 > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Alkalisalibacterium
Accessions
- Primary accessionA0A5C8KNH4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Cross-link | 223↔249 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-95) | ||||
Sequence: YVNPQGPDGNPDPLASARDIRDTFARM |
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 compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | ||||
Sequence: MSDEAKCPFNGDAGKKPKGRRTN | ||||||
Region | 1-24 | Disordered | ||||
Sequence: MSDEAKCPFNGDAGKKPKGRRTNR | ||||||
Domain | 129-425 | Plant heme peroxidase family profile | ||||
Sequence: LDKARRLLWPIKKKYGRKLSWADLFILTGNVALESMGFKTFGFGGGREDIWEPREDIHWGPEEEWLATSDTENSRYSGDRELANPLAAVQMGLIYVNPQGPDGNPDPLASARDIRDTFARMAMDDEETVALVAGGHTFGKCHGAGEPDHVGAEPEGGDIVDQGFGWKNTFQSGVGTHAITSGLEGAWTNHPTKWDMGYFENLFGYEWELTKSPAGAHQWKPKGDAGKDSVPDAYDPNKRHQPMMSTADMAMRMDPAYEKISRRFKDNPQEFADAFARAWFKLTHRDMGPIARYLGPL | ||||||
Region | 344-369 | Disordered | ||||
Sequence: AHQWKPKGDAGKDSVPDAYDPNKRHQ | ||||||
Compositional bias | 349-363 | Basic and acidic residues | ||||
Sequence: PKGDAGKDSVPDAYD |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length741
- Mass (Da)81,968
- Last updated2019-11-13 v1
- ChecksumB8E199CF3835DCC6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Basic and acidic residues | ||||
Sequence: MSDEAKCPFNGDAGKKPKGRRTN | ||||||
Compositional bias | 349-363 | Basic and acidic residues | ||||
Sequence: PKGDAGKDSVPDAYD |
Keywords
- Technical term