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Conserved domains on  [gi|489337863|ref|WP_003245071|]
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MULTISPECIES: manganese catalase family protein [Bacillus]

Protein Classification

manganese catalase family protein( domain architecture ID 10523835)

manganese catalase family protein, similar to manganese catalase that performs a peroxide-dependent oxidation-reduction, catalyzing the conversion of hydrogen peroxide to water and molecular oxygen.; belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins

CATH:  1.20.1260.10
EC:  1.11.1.6
Gene Ontology:  GO:0046872|GO:0004096
PubMed:  14745498|14871145|8749363|9444766|3304136
SCOP:  3001658

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-278 5.83e-169

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: 468.66  E-value: 5.83e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863    1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRADAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKYKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   81 LDNAPADVQEDAYKsNPAIAAVMSGMNPQHAIVSGLGAMASDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:pfam05067  81 LKGATFDQQEDAAE-EPVIGSVLGGMNPQHAIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYMRL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELEERErDIVVPTTFPRELEKQEVSYDLFNFSRGDESSQGRWAHGEAF 240
Cdd:pfam05067 160 YEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVE-TIVVPVPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEAP 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 489337863  241 DGRGEFRYIPAPIAFASAPHLKPAPMWLHNT-------VPPMSKC 278
Cdd:pfam05067 239 DGGGAFEYVKEPGAGAPIPDLRPAPMISHNTfleiakrLPPMKGF 283
 
Name Accession Description Interval E-value
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-278 5.83e-169

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: 468.66  E-value: 5.83e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863    1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRADAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKYKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   81 LDNAPADVQEDAYKsNPAIAAVMSGMNPQHAIVSGLGAMASDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:pfam05067  81 LKGATFDQQEDAAE-EPVIGSVLGGMNPQHAIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYMRL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELEERErDIVVPTTFPRELEKQEVSYDLFNFSRGDESSQGRWAHGEAF 240
Cdd:pfam05067 160 YEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVE-TIVVPVPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEAP 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 489337863  241 DGRGEFRYIPAPIAFASAPHLKPAPMWLHNT-------VPPMSKC 278
Cdd:pfam05067 239 DGGGAFEYVKEPGAGAPIPDLRPAPMISHNTfleiakrLPPMKGF 283
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-265 1.80e-131

Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism];


Pssm-ID: 442767  Cd Length: 253  Bit Score: 372.64  E-value: 1.80e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRaDAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:COG3546    1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMR-DPKYKDLLMDIGTEELGHVEMVATTIALL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  81 LDNAPADVQEDayksNPAIAAVMSGMNPQHAIVSGLGAMASDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:COG3546   80 LEGAPPELAPE----DPPLAAIKGGGNPQHFIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYERL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863 161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELEErerdivvptTFPRE--LEKQEVSYDLFNFSRGDESSQGRWAHGE 238
Cdd:COG3546  156 YEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQG---------KFPEKkkYEDQEFSYKYFNFSTGDYSDRGPWNGGP 226

                        250       260
                 ....*....|....*....|....*..
gi 489337863 239 AFDgrGEFRYIPAPIAFasAPHLKPAP 265
Cdd:COG3546  227 PPG--GEFEYVDGPEGG--PPDLPEDP 249
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-195 1.19e-82

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: 245.18  E-value: 1.19e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRADAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:cd01051    1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNFREDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  81 LDnapadvqedayksnpaiaavmsgmnpqhaivsglgamasDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:cd01051   81 LK---------------------------------------DSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYERL 121

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489337863 161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELE 195
Cdd:cd01051  122 YEMTDDPGVKDTLSFLLVREIVHQNAFGKALESLG 156
 
Name Accession Description Interval E-value
Mn_catalase pfam05067
Manganese containing catalase; Catalases are important antioxidant metalloenzymes that ...
 1-278 5.83e-169

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: 468.66  E-value: 5.83e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863    1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRADAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:pfam05067   1 MFVHDKLLQYPVKPDHPDPVLAKKLQEQLGGQFGELSAAMRYLFQGFNTRDKGKYKDLLMDIGTEELGHVEMIATMIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   81 LDNAPADVQEDAYKsNPAIAAVMSGMNPQHAIVSGLGAMASDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:pfam05067  81 LKGATFDQQEDAAE-EPVIGSVLGGMNPQHAIVSGLGAMPMDSMGVPWTADYIVASGNLIADLRANIAAEAQARLQYMRL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELEERErDIVVPTTFPRELEKQEVSYDLFNFSRGDESSQGRWAHGEAF 240
Cdd:pfam05067 160 YEMTDDPGVRDMLSFLLARETVHQNQFYKALEILEEVE-TIVVPVPFPRKLEKQEVARKLFNFSRGDESTIGRWAKGEAP 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 489337863  241 DGRGEFRYIPAPIAFASAPHLKPAPMWLHNT-------VPPMSKC 278
Cdd:pfam05067 239 DGGGAFEYVKEPGAGAPIPDLRPAPMISHNTfleiakrLPPMKGF 283
CotJC COG3546
Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and ...
 1-265 1.80e-131

Mn-containing catalase (includes spore coat protein CotJC) [Inorganic ion transport and metabolism];


Pssm-ID: 442767  Cd Length: 253  Bit Score: 372.64  E-value: 1.80e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRaDAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:COG3546    1 MFYHEKKLQYPVRVDKPDPRFAKLLQEQLGGPFGELSAAMQYLFQSFNMR-DPKYKDLLMDIGTEELGHVEMVATTIALL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  81 LDNAPADVQEDayksNPAIAAVMSGMNPQHAIVSGLGAMASDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:COG3546   80 LEGAPPELAPE----DPPLAAIKGGGNPQHFIVHGGGALPVDSNGVPWTAAYVQASGNLVADLLSNIAAEQRARLVYERL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863 161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELEErerdivvptTFPRE--LEKQEVSYDLFNFSRGDESSQGRWAHGE 238
Cdd:COG3546  156 YEMTDDPGVKDMLGFLLAREIVHQQRFGKALEELQG---------KFPEKkkYEDQEFSYKYFNFSTGDYSDRGPWNGGP 226

                        250       260
                 ....*....|....*....|....*..
gi 489337863 239 AFDgrGEFRYIPAPIAFasAPHLKPAP 265
Cdd:COG3546  227 PPG--GEFEYVDGPEGG--PPDLPEDP 249
Mn_catalase cd01051
Manganese catalase, ferritin-like diiron-binding domain; Manganese (Mn) catalase is a member ...
 1-195 1.19e-82

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: 245.18  E-value: 1.19e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863   1 MFYHIKELQYQAKPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFNCRADAKYKDLLYDVGTEEIGHVEMLATMISRL 80
Cdd:cd01051    1 MFYHVKKLQYPVRVDKPDPRFAKLLQEQLGGAFGELSAAMQYLFQSFNFREDPKYRDLLLDIGTEELSHLEMVATLIAML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  81 LDnapadvqedayksnpaiaavmsgmnpqhaivsglgamasDSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRL 160
Cdd:cd01051   81 LK---------------------------------------DSQGVPWTAAYIQSSGNLVADLRSNIAAESRARLTYERL 121

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489337863 161 YAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKELE 195
Cdd:cd01051  122 YEMTDDPGVKDTLSFLLVREIVHQNAFGKALESLG 156
Mn_catalase_like cd07908
Manganese catalase-like protein, ferritin-like diiron-binding domain; This uncharacterized ...
 13-183 5.61e-06

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: 45.35  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  13 KPAHPDPVYAKKLQEVLGGQFGEISVMMQYLFQGFncRADAKYK---DLLYDVGTEEIGHVEMLATMISRLldnapadvq 89
Cdd:cd07908    6 KVAGPNPRYAELLLDDYAGTNSELTAISQYIYQHL--ISEEKYPeiaETFLGIAIVEMHHLEILGQLIVLL--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  90 edayksnpaiaavmsGMNPQHAIVSGlgamasdSEGYPWNAKYIISSGNLLADFRANLNAEAQGRLQVTRLYAMTDDPGV 169
Cdd:cd07908   75 ---------------GGDPRYRSSSS-------DKFTYWTGKYVNYGESIKEMLKLDIASEKAAIAKYKRQAETIKDPYI 132

                        170
                 ....*....|....
gi 489337863 170 RDMLSFLIARDTYH 183
Cdd:cd07908  133 RALLNRIILDEKLH 146
YhjR COG1633
Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];
52-194 7.74e-03

Rubrerythrin, includes spore coat protein YhjR [Inorganic ion transport and metabolism];


Pssm-ID: 441240  Cd Length: 141  Bit Score: 35.85  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489337863  52 DAKYKDLLYDVGTEEIGHVEMLATMISRLLDNapaDVQEDAYKSNPAIAAVMSGMNPqhaivsglgaMASDSEGypwnak 131
Cdd:COG1633   29 DPELKKLFEELAEEEKKHAELLEKLYEKLGGK---PVAPPEEESQPGLAELMDKLDG----------SVSDAEA------ 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489337863 132 yiissgnlladFRANLNAEAQGRLQVTRLYAMTDDPGVRDMLSFLIARDTYHQNMWYAAIKEL 194
Cdd:COG1633   90 -----------LELAIATEKDAIEFYRELAAKVGDPEIKKLFEELAADEKEHAALLEGLYDRL 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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