A0A0N0V4S6 · A0A0N0V4S6_FUSLA
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids780 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H2O2 in hyphae. May play an antioxidative role in fungal defense against the host-produced H2O2 (oxidative burst) at the early stage of plant infection.
Catalytic activity
- 2 H2O2 = 2 H2O + O2
Cofactor
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
Features
Showing features for site, active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
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 lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium
Accessions
- Primary accessionA0A0N0V4S6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MHAKTLLLATGLVPLVAG | ||||||
Chain | PRO_5006987270 | 19-780 | Catalase-peroxidase | |||
Sequence: DCPFAAKRDTQQNLLPPREISEDFGRCRVASNQAGGGSRTKDFWPCQLRLDVLRQFSPQINPLGEEFDYAEAFQSLDFEALKKDIHDLLTDSQDWWPADFGHYGGLFIRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLAGNIALESSNFKTLGFAGGRPDTWQADESIYWGAETTFVPKGNDVRYNGSTDIYERANKLEKPLGATHFGLIYVNPEGPDGSSDPKASALDIREAFGRMGMDDEETAALIIGGHTLGKTHGAVPGKNIGPEPEAADLGEMGLGWHNSVGEGNGPNQQTSGLEVVWSKTPTKWSNHFLESLLGNKWTLVESPAGAHQWEAVNGTLDYPDPFDNTKFRRATMLTSDLALINDESYLKICKRWLKNPEEMNEAFAKAWFKLLHRDLGPTSRYLGPDVPKEKFIWQDPLPERKGDVITDEDVSSLKTAILAADGLDVSKLVSTAWASASTFRGTDKRGGANGARIALEPQVSWASNNPKQLKQVLSALKSVQKEFNAKSESKQVSLADLIVLGGVAAVEKAAKDAGFKDIEVPFTPGRVDATQEQTDITQFNYLEPLADGFRNYGHGTARARTEEILVDKAALLTLTPPEMTVLVGGLRALNANFDGSSNGVLTEKKGQLTNDFFVNLLSPAFKWSKKDQRGELWTATDRKTKSTKWTATRADLVFGSHAELRAISEVYGSADANEKFAKDFVAAWTKVMNLDRFDVKVNKESK | ||||||
Cross-link | 130↔263 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met-289) | ||||
Sequence: WHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLAGNIALESSNFKTLGFAGGRPDTWQADESIYWGAETTFVPKGNDVRYNGSTDIYERANKLEKPLGATHFGLIY | ||||||
Cross-link | 263↔289 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-130) | ||||
Sequence: YVNPEGPDGSSDPKASALDIREAFGRM |
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.
Keywords
- PTM
Interaction
Subunit
Homodimer; disulfide-linked.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 164-448 | Plant heme peroxidase family profile | ||||
Sequence: LDKARRLIWPIKQKYGNKISWADLMLLAGNIALESSNFKTLGFAGGRPDTWQADESIYWGAETTFVPKGNDVRYNGSTDIYERANKLEKPLGATHFGLIYVNPEGPDGSSDPKASALDIREAFGRMGMDDEETAALIIGGHTLGKTHGAVPGKNIGPEPEAADLGEMGLGWHNSVGEGNGPNQQTSGLEVVWSKTPTKWSNHFLESLLGNKWTLVESPAGAHQWEAVNGTLDYPDPFDNTKFRRATMLTSDLALINDESYLKICKRWLKNPEEMNEAFAKAWFKL |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length780
- Mass (Da)85,923
- Last updated2015-12-09 v1
- Checksum8AEDFE94365185C5
Keywords
- Technical term