A0A2G6FGD6 · A0A2G6FGD6_UNCDU
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids731 (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 | |
---|---|---|
Molecular Function | catalase activity | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | response to oxidative stress |
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 > Thermodesulfobacteriota > Desulfobacteria > Desulfobacterales
Accessions
- Primary accessionA0A2G6FGD6
Proteomes
PTM/Processing
Features
Showing features for cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Cross-link | 219↔245 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-96) | ||||
Sequence: YVNPEGPSGNPDVLASGRDVRETFARM |
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 | 1-20 | Polar residues | ||||
Sequence: MNDKSRCPVTGKSGSQAAGG | ||||||
Region | 1-25 | Disordered | ||||
Sequence: MNDKSRCPVTGKSGSQAAGGGASNR | ||||||
Domain | 130-422 | Plant heme peroxidase family profile | ||||
Sequence: LDKARRLLWPVKQKYGRKISWADLIIFAGNCAIESMGLKPFGFGGGREDVWEPERDIYWGAEDTWLGDDRYKGDRELDNPLAAVQMGLIYVNPEGPSGNPDVLASGRDVRETFARMAMNDEETVALVAGGHTFGKCHGAGDAARVGPEPEGAGLSEQGLGWKSSHGSGSGDDTISSGIEGAWTPNPIKWDNAYFDMLFGYDWNLEKSPAGAWQWVPVNPEEKDFAPAAHDAARKVKTIMTTADLSLRMDPIYKPIAKRFQENPEEFADAFVRAWFKLTHRDMGPRSRYLGGMV | ||||||
Region | 269-307 | Disordered | ||||
Sequence: GDAARVGPEPEGAGLSEQGLGWKSSHGSGSGDDTISSGI | ||||||
Compositional bias | 289-307 | Polar residues | ||||
Sequence: GWKSSHGSGSGDDTISSGI |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length731
- Mass (Da)80,359
- Last updated2018-01-31 v1
- ChecksumFB3655AC5FBA9E2D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Polar residues | ||||
Sequence: MNDKSRCPVTGKSGSQAAGG | ||||||
Compositional bias | 289-307 | Polar residues | ||||
Sequence: GWKSSHGSGSGDDTISSGI |