catalase (plasmid) [Halostagnicola larsenii XH-48]
Protein Classification
manganese catalase family protein( domain architecture ID 11466390)
manganese catalase family protein similar to manganese catalase, which catalyzes the conversion of hydrogen peroxide to water and molecular oxygen, and to Bacillus paralicheniformis spore coat peptide assembly protein CotJC
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| CotJC | COG3546 | Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ... |
1-261 | 6.61e-106 | |||||
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism]; : Pssm-ID: 442767 Cd Length: 253 Bit Score: 307.92 E-value: 6.61e-106
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| Name | Accession | Description | Interval | E-value | |||||
| CotJC | COG3546 | Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ... |
1-261 | 6.61e-106 | |||||
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism]; Pssm-ID: 442767 Cd Length: 253 Bit Score: 307.92 E-value: 6.61e-106
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| Mn_catalase | pfam05067 | Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ... |
1-268 | 4.63e-87 | |||||
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Two families of catalases are known, one having a heme cofactor, and this family that is a structurally distinct family containing non-heme manganese. Pssm-ID: 252986 [Multi-domain] Cd Length: 283 Bit Score: 261.04 E-value: 4.63e-87
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| Mn_catalase | cd01051 | Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ... |
1-194 | 1.45e-73 | |||||
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member of a broad superfamily of ferritin-like diiron enzymes. While many diiron enzymes catalyze dioxygen-dependent reactions, manganese catalase performs peroxide-dependent oxidation-reduction. Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Manganese catalase, a nonheme type II catalase, contains a binuclear manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting between dimanganese(II) [(2,2)] and dimanganese(III) [(3,3)] oxidation states during turnover. Mn catalases are found in a broad range of microorganisms in microaerophilic environments, including the mesophilic lactic acid bacteria (e.g., Lactobacillus plantarum) and bacterial and archaeal thermophiles (e.g., Thermus thermophilus and Pyrobaculum caldifontis). L. plantarum and T. thermophilus holoenzymes are homohexameric structures; each subunit contains a dimanganese active site. The manganese ions are linked by a mu 1,3-bridging glutamate carboxylate and two mu-bridging solvent oxygens that electronically couple the metal centers. Several members of this CD lack the C-terminal strands that pack against the neighboring catalytic domains as seen in L. plantarum. One such sequence, Bacillus subtilis CotJC, is known to be a component of the inner spore coat that interacts with spore coat protein, CotJA. It has been suggested that CotJC could modulate the degree of Mn SodA-dependent cross-linking of an outer coat component, or the two enzymes could serve to protect specific cellular structures during the developmental process. Pssm-ID: 153110 Cd Length: 156 Bit Score: 222.07 E-value: 1.45e-73
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| Name | Accession | Description | Interval | E-value | |||||
| CotJC | COG3546 | Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ... |
1-261 | 6.61e-106 | |||||
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism]; Pssm-ID: 442767 Cd Length: 253 Bit Score: 307.92 E-value: 6.61e-106
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| Mn_catalase | pfam05067 | Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ... |
1-268 | 4.63e-87 | |||||
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Two families of catalases are known, one having a heme cofactor, and this family that is a structurally distinct family containing non-heme manganese. Pssm-ID: 252986 [Multi-domain] Cd Length: 283 Bit Score: 261.04 E-value: 4.63e-87
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| Mn_catalase | cd01051 | Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ... |
1-194 | 1.45e-73 | |||||
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member of a broad superfamily of ferritin-like diiron enzymes. While many diiron enzymes catalyze dioxygen-dependent reactions, manganese catalase performs peroxide-dependent oxidation-reduction. Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Manganese catalase, a nonheme type II catalase, contains a binuclear manganese cluster that catalyzes the redox dismutation of hydrogen peroxide, interconverting between dimanganese(II) [(2,2)] and dimanganese(III) [(3,3)] oxidation states during turnover. Mn catalases are found in a broad range of microorganisms in microaerophilic environments, including the mesophilic lactic acid bacteria (e.g., Lactobacillus plantarum) and bacterial and archaeal thermophiles (e.g., Thermus thermophilus and Pyrobaculum caldifontis). L. plantarum and T. thermophilus holoenzymes are homohexameric structures; each subunit contains a dimanganese active site. The manganese ions are linked by a mu 1,3-bridging glutamate carboxylate and two mu-bridging solvent oxygens that electronically couple the metal centers. Several members of this CD lack the C-terminal strands that pack against the neighboring catalytic domains as seen in L. plantarum. One such sequence, Bacillus subtilis CotJC, is known to be a component of the inner spore coat that interacts with spore coat protein, CotJA. It has been suggested that CotJC could modulate the degree of Mn SodA-dependent cross-linking of an outer coat component, or the two enzymes could serve to protect specific cellular structures during the developmental process. Pssm-ID: 153110 Cd Length: 156 Bit Score: 222.07 E-value: 1.45e-73
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| Mn_catalase_like | cd07908 | Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ... |
11-183 | 3.04e-09 | |||||
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized bacterial protein family has a ferritin-like domain similar to that of the manganese catalase protein of Lactobacillus plantarum and the bll3758 protein of Bradyrhizobium japonicum. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF). Pssm-ID: 153117 Cd Length: 154 Bit Score: 54.59 E-value: 3.04e-09
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| Ferritin_like | cd00657 | Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, ... |
23-191 | 1.15e-03 | |||||
Ferritin-like superfamily of diiron-containing four-helix-bundle proteins; Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF). Pssm-ID: 153097 Cd Length: 130 Bit Score: 38.25 E-value: 1.15e-03
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