AC   MF_03108;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01961; -; 1; level=0
XX
Names: Catal-peroxid_euk
XX
ID   KATG
DE   RecName: Full=Catalase-peroxidase;
DE            Short=CP;
DE            EC=1.11.1.21;
DE   AltName: Full=Peroxidase/catalase;
GN   Name=katG;
XX
case <Feature:Signal==1>
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play
CC       an antioxidative role in fungal defense against the host-produced
CC       H(2)O(2) (oxidative burst) at the early stage of plant infection.
else
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.;
case <Feature:Signal==1>
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
else
CC   -!- SUBUNIT: Homodimer or homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily.
XX
DR   PROSITE; PS00435; PEROXIDASE_1; 1; trigger=no
DR   PROSITE; PS00436; PEROXIDASE_2; 1; trigger=no
DR   PROSITE; PS50873; PEROXIDASE_4; 1; trigger=no
DR   Pfam; PF00141; peroxidase; 2; trigger=no
DR   PRINTS; PR00460; BPEROXIDASE; 1; trigger=no
DR   PRINTS; PR00458; PEROXIDASE; 1; trigger=no
DR   NCBIfam; TIGR00198; cat_per_HPI; 1; trigger=no
DR   General; Signal; -; 0-1; trigger=yes
XX
KW   Heme
KW   Hydrogen peroxide
KW   Iron
KW   Metal-binding
KW   Oxidoreductase
KW   Peroxidase
case <Feature:Signal==1>
KW   Disulfide bond
KW   Secreted
else
KW   Cytoplasm
end case
XX
GO   GO:0004096; F:catalase activity
GO   GO:0004601; F:peroxidase activity
XX
FT   From: KATG2_PYRO7 (A4QUT2)
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         314
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   Condition: H
FT   SITE            137
FT                   /note="Transition state stabilizer"
FT   Condition: R
FT   CROSSLNK        140..273
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with
FT                   #{Met-299})"
FT   Condition: W-x*-Y
FT   CROSSLNK        273..299
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with
FT                   #{Trp-140})"
FT   Condition: Y-x*-M
case <Feature:Signal==1>
FT   DISULFID        55
FT                   /note="Interchain (with #{Cys-74})"
FT   Condition: C
FT   DISULFID        74
FT                   /note="Interchain (with #{Cys-55})"
FT   Condition: C
end case
XX
Size: 730-786;
Related: None;
Template: A4QUT2; A4R5S9; Q8X182; Q96VT4;
Scope:
 Eukaryota; Fungi
Fusion:
 Nter: None
 Cter: None
Duplicate: in PYRO7
Plasmid: None
Comments: None
XX
# Revision 1.13 2023/12/07
//