A0A1T3CHM4 · A0A1T3CHM4_9HYPO
- ProteinCatalase-peroxidase
- GenekatG
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids793 (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 | extracellular region | |
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 lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionA0A1T3CHM4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MPLKNILAIVGALPLATA | ||||||
Chain | PRO_5011820952 | 19-793 | Catalase-peroxidase | |||
Sequence: TGCPHINGNSNVHVARSGFQHPESILETRFSPDGPDFGTCPRKSTVAGGGTRSRQWWPCELNLAVLRQFSEKSNPFGSDFDYASAFSKIDVTQLKKDITAVQTTSQDWWPADFGNYGPFFIRLAWHNAGTYRAVDGRGGAGQGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGAALSWADLFVFAGNTAMENMGFPTYGFGFGRVDTWQSDEGIYWGGEQEMFPEALNNVVRYNGSTDFTTRADELESPLGAVSMGLIYVDPRGPNGTPDTKASALDIRETFGRMGMDDEETVALIAGGHAFGKTHGAVAGSNIGPEPNAAGIELQGLGWKNSFGTGNADDAYTSGLEVIWSRTPTKWANEFLFSLLNNNFTLTKSPDGAPQWEALDANASYPDPFIPGKFRRPTMLTSDLGLRDDPVYNNISKTFLNDFDYFTEKFGLAWYKLLHRDMGPISRYLGPEIPKQAPLIWQDPLPAPAYTTLAASDISSLKSQILAAPGLNISNLVTTAWGSASTFRISDKRGGANGARIALQPQVNFAANNPTRLAAVIKALKGVQTKFQSSGKKVSLADLIVLGGGAAIEKAAKAAGVTVTVPFTPGRVDATQDQTDVSTFAFLQPQADGFRNFGHGTASSLTEELLVDKAALLTLSPPELTVLIGGFRALSANFDGSSTGILTSRPGTLTNDFFVNLLGSYATWSVVNGTNEELFQSTNSAGKVQWTASRADLIFGSHPELRAISEVYGSSDGQSKFVTDFIAAWSKVMDLDRYDVKGHSGPY | ||||||
Cross-link | 278↔304 | Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-143) | ||||
Sequence: YVDPRGPNGTPDTKASALDIRETFGRM |
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 | 177-463 | Plant heme peroxidase family profile | ||||
Sequence: LDKARRLLWPIKQKYGAALSWADLFVFAGNTAMENMGFPTYGFGFGRVDTWQSDEGIYWGGEQEMFPEALNNVVRYNGSTDFTTRADELESPLGAVSMGLIYVDPRGPNGTPDTKASALDIRETFGRMGMDDEETVALIAGGHAFGKTHGAVAGSNIGPEPNAAGIELQGLGWKNSFGTGNADDAYTSGLEVIWSRTPTKWANEFLFSLLNNNFTLTKSPDGAPQWEALDANASYPDPFIPGKFRRPTMLTSDLGLRDDPVYNNISKTFLNDFDYFTEKFGLAWYKL |
Sequence similarities
Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length793
- Mass (Da)85,617
- Last updated2017-05-10 v1
- Checksum24F95ED750171E00