Species | Zymoseptoria tritici | |||||||||||
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Lineage | Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici | |||||||||||
CAZyme ID | ZTRI_8.269.mRNA-p1 | |||||||||||
CAZy Family | GT90 | |||||||||||
CAZyme Description | similar to peroxidase/catalase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
272957 | cat_per_HPI | 0.0 | 47 | 776 | 11 | 716 | 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 | 34 | 774 | 14 | 730 | Catalase (peroxidase I) [Inorganic ion transport and metabolism]. |
237891 | PRK15061 | 0.0 | 33 | 774 | 1 | 726 | catalase/peroxidase. |
173824 | catalase_peroxidase_1 | 0.0 | 47 | 478 | 1 | 409 | 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. |
173828 | catalase_peroxidase_2 | 7.25e-178 | 482 | 770 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 38 | 773 | 7 | 750 | |
0.0 | 33 | 773 | 62 | 805 | |
2.56e-298 | 38 | 773 | 58 | 786 | |
3.89e-298 | 38 | 774 | 58 | 789 | |
8.72e-287 | 52 | 774 | 5 | 715 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 38 | 773 | 7 | 727 | Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b],5SYU_B Crystal structure of Burkholderia pseudomallei KatG E242Q variant [Burkholderia pseudomallei 1710b] |
|
0.0 | 38 | 773 | 7 | 727 | Crystal structure of the S324G variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b],5SYY_B Crystal structure of the S324G variant of catalase-peroxidase from B. pseudomallei [Burkholderia pseudomallei 1710b] |
|
0.0 | 38 | 773 | 7 | 727 | Crystal structure of Burkhoderia pseudomallei KatG variant Q233E [Burkholderia pseudomallei 1710b],5SYW_B Crystal structure of Burkhoderia pseudomallei KatG variant Q233E [Burkholderia pseudomallei 1710b] |
|
0.0 | 38 | 773 | 7 | 727 | Crystal structure of Burkholderia pseudomallei KatG N240D variant [Burkholderia pseudomallei 1710b],5SYV_B Crystal structure of Burkholderia pseudomallei KatG N240D variant [Burkholderia pseudomallei 1710b] |
|
0.0 | 38 | 773 | 7 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
0.0 | 38 | 774 | 7 | 754 | Catalase-peroxidase OS=Pseudomonas fluorescens (strain Pf0-1) OX=205922 GN=katG PE=3 SV=1 |
|
0.0 | 38 | 773 | 7 | 755 | Catalase-peroxidase OS=Pseudomonas syringae pv. syringae (strain B728a) OX=205918 GN=katG PE=3 SV=1 |
|
0.0 | 41 | 782 | 15 | 748 | Catalase-peroxidase OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=katG PE=3 SV=2 |
|
0.0 | 38 | 773 | 7 | 755 | Catalase-peroxidase OS=Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OX=264730 GN=katG PE=3 SV=1 |
|
0.0 | 33 | 783 | 1 | 759 | Catalase-peroxidase OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=katG PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000067 | 0.000000 |
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