Summary
Manganese containing catalase
Catalases are important antioxidant metalloenzymes that catalyse 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 [2].
Literature references
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Igarashi T, Kono Y, Tanaka K; , J Biol Chem 1996;271:29521-29524.: Molecular cloning of manganese catalase from Lactobacillus plantarum. PUBMED:8939876
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Barynin VV, Whittaker MM, Antonyuk SV, Lamzin VS, Harrison PM, Artymiuk PJ, Whittaker JW; , Structure (Camb) 2001;9:725-738.: Crystal structure of manganese catalase from Lactobacillus plantarum. PUBMED:11587647
InterPro entry IPR007760
Catalases () are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen. 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. There are three structurally independent classes of catalases: ubiquitous mono-functional haem-containing catalases (), bifunctional haem-containing catalase-peroxidases that are closely related to plant peroxidases (), and non-haem manganese-containing catalases PUBMED:14745498.
This entry represents the non-haem Mn-catalases, which are found in several bacterial species PUBMED:14871145. The structure of the Mn catalase from Lactobacillus plantarum reveals a homo-hexamer, where each subunit contains a dimanganese active site that is accessed by a single substrate channel PUBMED:11587647. The dimanganese active site performs a two-electron catalytic cycle that alternately oxidises and reduces the dimanganese atoms in a manner that is similar to its haem-counterpart found in other catalases.
Clan
This family is a member of clan Ferritin (CL0044), which contains the following 12 members:
Coat_F COQ7 DUF2202 DUF2383 DUF892 FA_desaturase_2 Ferritin MiaE Mn_catalase Phenol_Hydrox Ribonuc_red_sm RubrerythrinExternal database links
| PANDIT: | PF05067 |
| SCOP: | 1jkv |
| SYSTERS: | Mn_catalase |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | COG3546 |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 7 |
| Number in full: | 519 |
| Average length of the domain: | 227.60 aa |
| Average identity of full alignment: | 35 % |
| Average coverage of the sequence by the domain: | 95.54 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 281 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
Mn_catalaseStructures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Mn_catalase domain has been found.
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