AC   MF_01961;
DC   Protein; auto
c?   <OC:Bacteria> or <OC:Archaea>
TR   HAMAP; MF_01961; -; 1; level=0
XX
Names: Catal_peroxid
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
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity.
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 dimer.;
CC   -!- SUBUNIT: Homodimer or homotetramer.
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.
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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
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KW   Heme
KW   Hydrogen peroxide
KW   Iron
KW   Metal-binding
KW   Oxidoreductase
KW   Peroxidase
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GO   GO:0004096; F:catalase activity
GO   GO:0004601; F:peroxidase activity
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FT   From: KATG_ECOLI (P13029)
FT   ACT_SITE        106
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         267
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   Condition: H
FT   SITE            102
FT                   /note="Transition state stabilizer"
FT   Condition: R
FT   CROSSLNK        105..226
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with
FT                   #{Met-252})"
FT   Condition: W-x*-Y
FT   CROSSLNK        226..252
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with
FT                   #{Trp-105})"
FT   Condition: Y-x*-M
XX
Size: 699-781;
Related: None;
Template: P13029; O59651; Q939D2; P9WIE5; Q31MN3;
Scope:
 Bacteria
 Archaea; Euryarchaeota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ALKMQ, BURA4, BURO1, BURO0, BURCH, BURCJ, BURCM, BURVG, CELJU,
 ECO57, HALMA, IDILO, LEGPA, LEGPC, LEGPH, LEGPL, LEGPN, MYCFO, MYCS2, MYCVP,
 CUPPJ, SHEAM, SHEFN, SHEON, SHESA, SHESM, SHESR, VIBPA
Plasmid: in DINSH, ECO57, ECOLX, HALS3, HALSA, CUPMC, RHIE6, RHIEC, RHIET,
 RHIJ3, RHIME, SINFN, CERS5, RUEPO, SINMW
Comments: None
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# Revision 1.32 2023/11/28
//