A0A0D2YD52 · A0A0D2YD52_FUSOF
- ProteinCatalase-peroxidase
- Gene28955419
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids781 (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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium > Fusarium oxysporum species complex
Accessions
- Primary accessionA0A0D2YD52
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MHVQSLLLASGLVPLAAS | ||||||
Chain | PRO_5010593853 | 19-781 | Catalase-peroxidase | |||
Sequence: QGCPFAKRATDNNLVPPREIPEDFGICRVASNQAGGGTRSKDFWPCALRLDVLRQFSPQYSPLGADFDYTEAFKSLDYESLKKDLKALLTDSQDWWPADHGSYGGLFIRMSWHSAGTYRAMDGRGGAGMGQQRFAPLDSWPDNQNLDKARRLLWPIKQKYGSKISWADLVVLAGNVALEHSGFETLGFAGGRADTWEADESIYWGAESTFVPKGNDVRYNGSTDIYERADKLEKPLGATHFGLIYVNPEGPDGSSDPKASALDIRTAFGRMGMDDEETAALIIGGHTLGKTHGAVSSKNIGPEPMAADLGGMGLGWHNSVNEGNGPDQMTSGLEVIWSTTPTKWSNHFLKSLLGNNWTLVESPAGHKQWEALDGKLEYPDPFVKGKFRRPTMLTSDLALINDPAYLKICKRWHDHPKEMNQAFARAWYKLLHRDLGPVSRYLGPEVAKEKFIWQDPLPERKGDIISEGDISSLKSAILSTDGLTVSKLVSTAWNSASTFRGTDKRGGANGARIALEPQVNWASNNPKQLKQVLSALKKVQKNFNSKSSSKQVSLADLIVLGGVAAVEKAAQDAGFKDVKVPFTPGRVAATQNQTDLVQFGYLEPLADGFRNYGHGTARARTEEILVDRAALLTLTPPEMTVLVGGLRALNANYDGSSNGILTEKKGQLTNDFFVNLLSPAFVWTKKDDRGELWTGTDRATKSAKWTATRADLVFGSHAELRAISEVYGSADAKEKFVKDFISAWTKVMNLDRFDVKTEKETKY | ||||||
Cross-link | 130↔263 | Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with Met-289) | ||||
Sequence: WHSAGTYRAMDGRGGAGMGQQRFAPLDSWPDNQNLDKARRLLWPIKQKYGSKISWADLVVLAGNVALEHSGFETLGFAGGRADTWEADESIYWGAESTFVPKGNDVRYNGSTDIYERADKLEKPLGATHFGLIY | ||||||
Cross-link | 263↔289 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-130) | ||||
Sequence: YVNPEGPDGSSDPKASALDIRTAFGRM |
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
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length781
- Mass (Da)85,717
- Last updated2015-04-29 v1
- Checksum02ABB334D21110C1
Keywords
- Technical term