A0A1T3CHM4 · A0A1T3CHM4_9HYPO

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

heme b (UniProtKB | Rhea| CHEBI:60344 )

Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.

Features

Showing features for site, active site, binding site.

TypeIDPosition(s)Description
Site140Transition state stabilizer
Active site144Proton acceptor
Binding site319Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncatalase activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Biological Processhydrogen peroxide catabolic process
Biological Processresponse to oxidative stress

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Catalase-peroxidase
  • EC number
  • Short names
    CP
  • Alternative names
    • Peroxidase/catalase

Gene names

    • Name
      katG
    • ORF names
      A0O28_0006310

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NJAU 4742
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma

Accessions

  • Primary accession
    A0A1T3CHM4

Proteomes

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Features

Showing features for signal, chain, cross-link.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_501182095219-793Catalase-peroxidase
Cross-link278↔304Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-143)

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

Interaction

Subunit

Homodimer; disulfide-linked.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain177-463Plant heme peroxidase family profile

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    793
  • Mass (Da)
    85,617
  • Last updated
    2017-05-10 v1
  • Checksum
    24F95ED750171E00
MPLKNILAIVGALPLATATGCPHINGNSNVHVARSGFQHPESILETRFSPDGPDFGTCPRKSTVAGGGTRSRQWWPCELNLAVLRQFSEKSNPFGSDFDYASAFSKIDVTQLKKDITAVQTTSQDWWPADFGNYGPFFIRLAWHNAGTYRAVDGRGGAGQGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGAALSWADLFVFAGNTAMENMGFPTYGFGFGRVDTWQSDEGIYWGGEQEMFPEALNNVVRYNGSTDFTTRADELESPLGAVSMGLIYVDPRGPNGTPDTKASALDIRETFGRMGMDDEETVALIAGGHAFGKTHGAVAGSNIGPEPNAAGIELQGLGWKNSFGTGNADDAYTSGLEVIWSRTPTKWANEFLFSLLNNNFTLTKSPDGAPQWEALDANASYPDPFIPGKFRRPTMLTSDLGLRDDPVYNNISKTFLNDFDYFTEKFGLAWYKLLHRDMGPISRYLGPEIPKQAPLIWQDPLPAPAYTTLAASDISSLKSQILAAPGLNISNLVTTAWGSASTFRISDKRGGANGARIALQPQVNFAANNPTRLAAVIKALKGVQTKFQSSGKKVSLADLIVLGGGAAIEKAAKAAGVTVTVPFTPGRVDATQDQTDVSTFAFLQPQADGFRNFGHGTASSLTEELLVDKAALLTLSPPELTVLIGGFRALSANFDGSSTGILTSRPGTLTNDFFVNLLGSYATWSVVNGTNEELFQSTNSAGKVQWTASRADLIFGSHPELRAISEVYGSSDGQSKFVTDFIAAWSKVMDLDRYDVKGHSGPY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LVVK01000017
EMBL· GenBank· DDBJ
OPB40552.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp