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Conserved domains on  [gi|169636911|gb|ACA58500|]
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catalase, partial [Exiguobacterium sp. CNU020]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KatE super family cl29004
Catalase [Inorganic ion transport and metabolism];
1-84 3.16e-59

Catalase [Inorganic ion transport and metabolism];


The actual alignment was detected with superfamily member COG0753:

Pssm-ID: 440516 [Multi-domain]  Cd Length: 489  Bit Score: 187.56  E-value: 3.16e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:COG0753   53 IPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGN 132


                 ....
gi 169636911  81 NTPV 84
Cdd:COG0753  133 NTPV 136
 
Name Accession Description Interval E-value
KatE COG0753
Catalase [Inorganic ion transport and metabolism];
1-84 3.16e-59

Catalase [Inorganic ion transport and metabolism];


Pssm-ID: 440516 [Multi-domain]  Cd Length: 489  Bit Score: 187.56  E-value: 3.16e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:COG0753   53 IPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGN 132


                 ....
gi 169636911  81 NTPV 84
Cdd:COG0753  133 NTPV 136
katE PRK11249
hydroperoxidase II; Provisional
 1-84 1.09e-57

hydroperoxidase II; Provisional


Pssm-ID: 236886 [Multi-domain]  Cd Length: 752  Bit Score: 187.94  E-value: 1.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:PRK11249 119 IPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGN 198


                 ....
gi 169636911  81 NTPV 84
Cdd:PRK11249 199 NTPV 202
Catalase pfam00199
Catalase;
1-84 5.60e-57

Catalase;


Pssm-ID: 459708  Cd Length: 383  Bit Score: 179.11  E-value: 5.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911    1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:pfam00199  42 IPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTPVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGN 121


                  ....
gi 169636911   81 NTPV 84
Cdd:pfam00199 122 NTPV 125
Catalase smart01060
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ...
 1-84 1.90e-55

Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.


Pssm-ID: 215003  Cd Length: 373  Bit Score: 174.96  E-value: 1.90e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911     1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:smart01060  39 IPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFVRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGN 118


                   ....
gi 169636911    81 NTPV 84
Cdd:smart01060 119 NTPV 122
catalase_clade_2 cd08155
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ...
 1-84 3.78e-55

Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163711  Cd Length: 443  Bit Score: 176.02  E-value: 3.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:cd08155    5 IPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLVGN 84


                 ....
gi 169636911  81 NTPV 84
Cdd:cd08155   85 NIPV 88
 
Name Accession Description Interval E-value
KatE COG0753
Catalase [Inorganic ion transport and metabolism];
1-84 3.16e-59

Catalase [Inorganic ion transport and metabolism];


Pssm-ID: 440516 [Multi-domain]  Cd Length: 489  Bit Score: 187.56  E-value: 3.16e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:COG0753   53 IPERVVHARGSGAHGTFEVTEDISKYTKAKFFQEPGKKTPVFVRFSTVAGERGSADTERDVRGFAVKFYTEEGNWDLVGN 132


                 ....
gi 169636911  81 NTPV 84
Cdd:COG0753  133 NTPV 136
katE PRK11249
hydroperoxidase II; Provisional
 1-84 1.09e-57

hydroperoxidase II; Provisional


Pssm-ID: 236886 [Multi-domain]  Cd Length: 752  Bit Score: 187.94  E-value: 1.09e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:PRK11249 119 IPERIVHARGSAAHGYFQPYKSLSDITKAAFLQDPGKITPVFVRFSTVQGPRGSADTVRDIRGFATKFYTEEGNFDLVGN 198


                 ....
gi 169636911  81 NTPV 84
Cdd:PRK11249 199 NTPV 202
Catalase pfam00199
Catalase;
1-84 5.60e-57

Catalase;


Pssm-ID: 459708  Cd Length: 383  Bit Score: 179.11  E-value: 5.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911    1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:pfam00199  42 IPERVVHAKGAGAHGYFEVTHDISDYTKAKFLSEVGKKTPVFVRFSTVAGERGSADTARDPRGFAVKFYTEEGNWDLVGN 121


                  ....
gi 169636911   81 NTPV 84
Cdd:pfam00199 122 NTPV 125
Catalase smart01060
Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water ...
 1-84 1.90e-55

Catalases are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects; Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via transition metals, this radical being able to damage a wide variety of molecules within a cell, leading to oxidative stress and cell death. Catalases act to neutralise hydrogen peroxide toxicity, and are produced by all aerobic organisms ranging from bacteria to man. Most catalases are mono-functional, haem-containing enzymes, although there are also bifunctional haem-containing peroxidase/catalases that are closely related to plant peroxidases, and non-haem, manganese-containing catalases that are found in bacteria.


Pssm-ID: 215003  Cd Length: 373  Bit Score: 174.96  E-value: 1.90e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911     1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:smart01060  39 IPERVVHAKGSGAHGYFEVTEDISDYTKAAFFQKVGKKTPVFVRFSTVAGERGSADTVRDPRGFAVKFYTEEGNWDLVGN 118


                   ....
gi 169636911    81 NTPV 84
Cdd:smart01060 119 NTPV 122
catalase_clade_2 cd08155
Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ...
 1-84 3.78e-55

Clade 2 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 2 catalases are mostly found in bacteria and fungi; they have a large subunit size of 75 to 84 kDa, and bind a heme d group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163711  Cd Length: 443  Bit Score: 176.02  E-value: 3.78e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:cd08155    5 IPERVVHARGSGAHGYFQVYESLSQYTKAKFLQDPGKKTPVFVRFSTVAGSRGSADTVRDVRGFAVKFYTEEGNYDLVGN 84


                 ....
gi 169636911  81 NTPV 84
Cdd:cd08155   85 NIPV 88
catalase_clade_1 cd08154
Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ...
 1-84 9.01e-45

Clade 1 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 1 catalases are found in bacteria, algae, and plants; they have a relatively small subunit size of 55 to 69 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. They appear to form tetramers. In eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163710 [Multi-domain]  Cd Length: 469  Bit Score: 149.37  E-value: 9.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:cd08154   44 IPERVVHARGAGAHGYFEAYGDISDYTRASFLQEPGKKTPVFVRFSTVIHGKGSPETLRDPRGFAVKFYTEEGNWDLVGN 123


                 ....
gi 169636911  81 NTPV 84
Cdd:cd08154  124 NLPV 127
catalase cd00328
Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and ...
 1-84 8.21e-44

Catalase heme-binding enzyme; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Most catalases exist as tetramers of 65KD subunits containing a protoheme IX group buried deep inside the structure. In eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163705 [Multi-domain]  Cd Length: 433  Bit Score: 146.07  E-value: 8.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:cd00328    2 IPERVVHARGAGAFGYFTAYGDWSDISAAAFFSAIGKKTPVFVRFSTVVGGAGSADTVRDPHGFATKFYTEEGNFDLVGN 81


                 ....
gi 169636911  81 NTPV 84
Cdd:cd00328   82 NTPI 85
catalase_clade_3 cd08156
Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both ...
 1-84 1.38e-43

Clade 3 of the heme-binding enzyme catalase; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. Clade 3 catalases are the most abundant subfamily and are found in all three kingdoms of life; they have a relatively small subunit size of 43 to 75 kDa, and bind a protoheme IX (heme b) group buried deep inside the structure. Clade 3 catalases also bind NADPH as a second redox-active cofactor. They form tetramers, and in eukaryotic cells, catalases are located in peroxisomes.


Pssm-ID: 163712 [Multi-domain]  Cd Length: 429  Bit Score: 145.37  E-value: 1.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:cd08156    2 IPERVVHAKGAGAFGTFEVTHDITKYTKAKIFSEVGKKTPVFVRFSTVAGERGSADTERDPRGFALKFYTEEGNWDLVGN 81


                 ....
gi 169636911  81 NTPV 84
Cdd:cd08156   82 NTPV 85
catalase_fungal cd08157
Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in ...
 1-84 2.62e-42

Fungal catalases similar to yeast catalases A and T; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes, which is involved in the protection of cells from the toxic effects of peroxides. It catalyzes the conversion of hydrogen peroxide to water and molecular oxygen. Catalases also utilize hydrogen peroxide to oxidize various substrates such as alcohol or phenols. This family of fungal catalases has a relatively small subunit size, and binds a protoheme IX (heme b) group buried deep inside the structure. Fungal catalases also bind NADPH as a second redox-active cofactor. They form tetramers; in eukaryotic cells, catalases are typically located in peroxisomes. Saccharomyces cerevisiae catalase T is found in the cytoplasm, though.


Pssm-ID: 163713 [Multi-domain]  Cd Length: 451  Bit Score: 142.49  E-value: 2.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:cd08157   18 IPERVVHAKGAGAYGEFEVTDDISDITSADMLQGVGKKTPCLVRFSTVGGEKGSADTVRDPRGFAVKFYTEEGNWDWVFN 97


                 ....
gi 169636911  81 NTPV 84
Cdd:cd08157   98 NTPV 101
PLN02609 PLN02609
catalase
 1-84 1.02e-39

catalase


Pssm-ID: 215328 [Multi-domain]  Cd Length: 492  Bit Score: 136.41  E-value: 1.02e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   1 IPESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGNYDLVGN 80
Cdd:PLN02609  59 IPERVVHARGASAKGFFEVTHDISNLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDMVGN 138


                 ....
gi 169636911  81 NTPV 84
Cdd:PLN02609 139 NFPV 142
catalase_like cd08150
Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found ...
 2-84 1.32e-20

Catalase-like heme-binding proteins and protein domains; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity.


Pssm-ID: 163706  Cd Length: 283  Bit Score: 82.22  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169636911   2 PESVVHARGVGAHGEFQVYEPLAEITKAGFLNDPsKTTPVFVRFSTVQgsrGSGDTVRDVRGFSTKLYT--DEGNYDLVG 79
Cdd:cd08150    1 GLRGQHFQGTCAFGTFEVLADLKERLRVGLFAEG-KVYPAYIRFSNGA---GIDDTKPDIRGFAIKFTGvaDAGTLDFVL 76


                 ....*
gi 169636911  80 NNTPV 84
Cdd:cd08150   77 NNTPV 81
srpA_like cd08153
Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ...
 7-84 6.71e-09

Catalase-like heme-binding proteins similar to the uncharacterized srpA; Catalase is a ubiquitous enzyme found in both prokaryotes and eukaryotes involved in the protection of cells from the toxic effects of peroxides. It catalyses the conversion of hydrogen peroxide to water and molecular oxygen. Several other related protein families share the catalase fold and bind to heme, but do not necessarily have catalase activity. This family contains uncharacterized proteins similar to the Synechococcus elongatus PCC 7942 periplasmic protein srpA, of mostly bacterial origin. The plasmid-encoded srpA is regulated by sulfate, but does not seem to function in its uptake or metabolism.


Pssm-ID: 163709  Cd Length: 295  Bit Score: 50.31  E-value: 6.71e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169636911   7 HARGVGAHGEFQVYEPLAEITKAGFLNdpSKTTPVFVRFSTVQGSRGSGDTVRDVRGFSTKLYTDEGN-YDLVGNNTPV 84
Cdd:cd08153   18 HAKGICVSGTFTPSGAAASLSRAPLFS--GGSVPVTGRFSLGGGNPKAPDDAANPRGMALKFRLPDGEqWRMVMNSFPV 94
AOS cd08151
Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene ...
 7-80 9.52e-06

Allene oxide synthase; Allene oxide synthase converts a fatty acid hydroperoxide to an allene oxide, which is an unstable epoxide. In corals, the enzyme is part of a eiconaosid synthesis pathway that is initiated by a lipoxygenase, which generates the fatty acid hydroperoxides in the first step. The structure of allene oxide synthase closely resembles that of catalase, but allene oxide synthase does not have catalase activity.


Pssm-ID: 163707  Cd Length: 328  Bit Score: 41.64  E-value: 9.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169636911   7 HARGVGAHGEFQVYEPLaEITKAGFLNdPSKTTPVFVRFSTVQGSRgsGDTVRDVRGFSTKLYT----DEGNYDLVGN 80
Cdd:cd08151   31 HTIGVGAKGVLTVLAES-DFPEHAFFT-AGKRFPVILRHANIVGGD--DDASLDGRGAALRFLNagddDAGPLDLVMN 104
 
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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