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CAZyme Information: EPE09117.1

You are here: Home > Sequence: EPE09117.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Ophiostoma piceae
Lineage Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
CAZyme ID EPE09117.1
CAZy Family GT2
CAZyme Description Catalase-peroxidase [Source:UniProtKB/TrEMBL;Acc:S3C8F2]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
806 87471.10 6.5147
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346 8884 1262450 0 8884
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EPE09117.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA2 130 232 2.1e-18 0.396078431372549

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
237891 PRK15061 0.0 59 798 4 726
catalase/peroxidase.
173824 catalase_peroxidase_1 0.0 69 484 1 406
N-terminal catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.
272957 cat_per_HPI 0.0 58 797 1 713
catalase/peroxidase HPI. As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]
223453 KatG 0.0 59 798 16 730
Catalase (peroxidase I) [Inorganic ion transport and metabolism].
173828 catalase_peroxidase_2 2.15e-172 492 794 1 297
C-terminal non-catalytic domain of catalase-peroxidases. This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 11 799 6 788
0.0 12 799 6 790
4.50e-312 57 797 3 750
7.78e-292 60 805 66 813
4.01e-253 74 797 5 714

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 24 801 2 764
Crystal Structure of Eukaryotic Oxoiron MagKatG2 at pH 8.5 [Pyricularia oryzae 70-15],5CJH_B Crystal Structure of Eukaryotic Oxoiron MagKatG2 at pH 8.5 [Pyricularia oryzae 70-15],5JHX_A Crystal Structure of Fungal MagKatG2 at pH 3.0 [Pyricularia oryzae 70-15],5JHX_B Crystal Structure of Fungal MagKatG2 at pH 3.0 [Pyricularia oryzae 70-15],5JHY_A Crystal Structure of Fungal MagKatG2 at pH 5.5 [Pyricularia oryzae 70-15],5JHY_B Crystal Structure of Fungal MagKatG2 at pH 5.5 [Pyricularia oryzae 70-15],5JHZ_A Crystal Structure of Fungal MagKatG2 at pH 7.0 [Pyricularia oryzae 70-15],5JHZ_B Crystal Structure of Fungal MagKatG2 at pH 7.0 [Pyricularia oryzae 70-15]
0.0 24 801 2 764
Crystal Structure of Fungal MagKatG2 [Pyricularia oryzae 70-15],3UT2_B Crystal Structure of Fungal MagKatG2 [Pyricularia oryzae 70-15]
1.44e-295 60 797 6 727
Crystal structure of catalase-peroxidase KATG of burkholderia pseudomallei treated with INH [Burkholderia pseudomallei 1710b],5L05_B Crystal structure of catalase-peroxidase KATG of burkholderia pseudomallei treated with INH [Burkholderia pseudomallei 1710b],5SW6_A Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6 [Burkholderia pseudomallei 1710b],5SW6_B Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH5.6 [Burkholderia pseudomallei 1710b],5SX0_B Crystal structure of an oxoferryl species of catalase-peroxidase KatG at pH7.5 [Burkholderia pseudomallei 1710b],5SX3_A Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5 [Burkholderia pseudomallei 1710b],5SX3_B Crystal structure of the catalase-peroxidase KatG of B. pseudomaallei at pH 4.5 [Burkholderia pseudomallei 1710b],5SXQ_A Crystal structure of B. pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXQ_B Crystal structure of B. pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXS_A Crystal structure of catalase-peroxidase KatG with isonicotinic acid hydrazide and AMP bound [Burkholderia pseudomallei 1710b],5SXS_B Crystal structure of catalase-peroxidase KatG with isonicotinic acid hydrazide and AMP bound [Burkholderia pseudomallei 1710b],5SYL_A B. pseudomallei KatG with KCN bound [Burkholderia pseudomallei 1710b],5SYL_B B. pseudomallei KatG with KCN bound [Burkholderia pseudomallei 1710b],6MPY_A B. pseudomallei KatG crystallized in the presence of benzoyl hydrazide [Burkholderia pseudomallei],6MPY_B B. pseudomallei KatG crystallized in the presence of benzoyl hydrazide [Burkholderia pseudomallei],6MQ0_A B. pseudomallei KatG crystallized in the presence of furoyl hydrazide [Burkholderia pseudomallei],6MQ0_B B. pseudomallei KatG crystallized in the presence of furoyl hydrazide [Burkholderia pseudomallei],6MQ1_A Chain A, Catalase-peroxidase [Burkholderia pseudomallei],6MQ1_B Chain B, Catalase-peroxidase [Burkholderia pseudomallei]
4.12e-295 60 797 6 727
Crystal structure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b],5SXT_B Crystal structure of the S324T variant of Burkholderia pseudomallei KatG with isonicotinic acid hydrazide bound [Burkholderia pseudomallei 1710b]
4.12e-295 60 797 6 727
Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei with acetate bound [Burkholderia pseudomallei 1710b],5V53_B Crystal structure of the D141A/Q233E/N240D variant of catalase-peroxidase from B. pseudomallei with acetate bound [Burkholderia pseudomallei 1710b]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 10 801 9 786
Catalase-peroxidase 2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=KATG2 PE=1 SV=1
7.41e-316 60 799 5 754
Catalase-peroxidase OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=katG PE=3 SV=1
9.78e-316 60 801 5 754
Catalase-peroxidase OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=katG PE=3 SV=1
3.26e-313 60 805 5 733
Catalase-peroxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=katG PE=3 SV=1
1.02e-309 57 797 7 756
Catalase-peroxidase OS=Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) OX=376686 GN=katG PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000319 0.999651 CS pos: 23-24. Pr: 0.9740

TMHMM  Annotations      help

There is no transmembrane helices in EPE09117.1.