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297  structures 2080  species 0  interactions 2747  sequences 23  architectures

Family: Catalase_C (PF18011)

Summary: C-terminal domain found in long catalases

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C-terminal domain found in long catalases Provide feedback

This domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain.

Literature references

  1. Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I;, J Biol Chem. 1999;274:27717-27725.: Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli. PUBMED:10488114 EPMC:10488114

  2. Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC;, Proteins. 2001;44:270-281.: Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli. PUBMED:11455600 EPMC:11455600

  3. Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I;, Structure. 1995;3:491-502.: Crystal structure of catalase HPII from Escherichia coli. PUBMED:7663946 EPMC:7663946

  4. Chelikani P, Carpena X, Fita I, Loewen PC;, J Biol Chem. 2003;278:31290-31296.: An electrical potential in the access channel of catalases enhances catalysis. PUBMED:12777389 EPMC:12777389

  5. Jha V, Louis S, Chelikani P, Carpena X, Donald LJ, Fita I, Loewen PC;, Biochemistry. 2011;50:2101-2110.: Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli. PUBMED:21332158 EPMC:21332158

  6. Jha V, Donald LJ, Loewen PC;, Arch Biochem Biophys. 2012;525:207-214.: Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage. PUBMED:22172685 EPMC:22172685

  7. Yonekura K, Watanabe M, Kageyama Y, Hirata K, Yamamoto M, Maki-Yonekura S;, PLoS One. 2013;8:e78216.: Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex. PUBMED:24223139 EPMC:24223139

  8. Jha V, Chelikani P, Carpena X, Fita I, Loewen PC;, Arch Biochem Biophys. 2012;526:54-59.: Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli. PUBMED:22820098 EPMC:22820098

  9. Diaz A, Valdes VJ, Rudino-Pinera E, Horjales E, Hansberg W;, J Mol Biol. 2009;386:218-232.: Structure-function relationships in fungal large-subunit catalases. PUBMED:19109972 EPMC:19109972

  10. Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E;, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013;69:753-758.: Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3. PUBMED:23832201 EPMC:23832201

  11. Diaz A, Horjales E, Rudino-Pinera E, Arreola R, Hansberg W;, J Mol Biol. 2004;342:971-985.: Unusual Cys-Tyr covalent bond in a large catalase. PUBMED:15342250 EPMC:15342250

Internal database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR041399

The most conspicuous difference between small and large catalases is the presence in large catalases of an extra C-terminal domain. This domain is found at the C terminus of a variety of large catalase enzymes. Structurally it is related to class I glutamine amidotransferase domains [ PUBMED:11119647 ]. The precise molecular function of this domain is uncertain.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Glutaminase_I (CL0014), which has the following description:

Most members of this clan are glutaminase enzymes. This superfamily is shown to be related in [1]. The clan also contains the DJ-1/PfpI family that includes the peptidase PfpI that has a catalytic Cys-His-Glu triad that differs from the class I GAT Cys-His-Glu triad.

The clan contains the following 18 members:

ABC_transp_aux BPL_N Catalase_C DJ-1_PfpI DUF4159 GATase GATase1_like GATase_3 GATase_5 Glyco_hydro_42M HTS LBP_M Peptidase_C26 Peptidase_S51 Peptidase_S66 SNO ThiJ_like ThuA


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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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This page displays the phylogenetic tree for this family's seed alignment. 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 alignment.

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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 View help on the curation process

Seed source: ECOD:EUF00986
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 28
Number in full: 2747
Average length of the domain: 151.70 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 21.38 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.6 24.6
Trusted cut-off 24.6 24.6
Noise cut-off 24.5 24.5
Model length: 151
Family (HMM) version: 3
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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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 Catalase_C domain has been found. There are 297 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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