catalase/peroxidase.

catalase/peroxidase HPI. As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]

N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.

Catalase (peroxidase I) [Inorganic ion transport and metabolism].

C-terminal non-catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.

Crystalstructure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXT_B Crystal structure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b]

Crystalstructure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b],5SYU_B Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b]

Crystalstructure of the E198A variant of Burkholderia pseudomallei catalase-peroxidase KatG with INH [Burkholderia pseudomallei 1710b],5SXX_B Crystal structure of the E198A variant of Burkholderia pseudomallei catalase-peroxidase KatG with INH [Burkholderia pseudomallei 1710b]

Crystalstructure of the E198A variant of catalase-peroxidase KatG of Burkholderia pseudomallei [Burkholderia pseudomallei 1710b],5SXW_B Crystal structure of the E198A variant of catalase-peroxidase KatG of Burkholderia pseudomallei [Burkholderia pseudomallei 1710b]

Crystalstructure of Burkhoderia pseudomallei KatG variant Q233E [Burkholderia pseudomallei 1710b],5SYW_B Crystal structure of Burkhoderia pseudomallei KatG variant Q233E [Burkholderia pseudomallei 1710b]

Catalase-peroxidase OS=Synechococcus elongatus (strain PCC 7942 / FACHB-805) OX=1140 GN=katG PE=1 SV=1

Catalase-peroxidase 1 OS=Legionella pneumophila (strain Lens) OX=297245 GN=katG1 PE=3 SV=1

Catalase-peroxidase OS=Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) OX=269084 GN=katG PE=1 SV=1

Catalase-peroxidase OS=Edwardsiella tarda OX=636 GN=katG PE=3 SV=1

Catalase-peroxidase 1 OS=Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) OX=272624 GN=katG1 PE=3 SV=2