CAZyme Information: KLU89463.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU89463.1
• CAZy Family: GT8
• CAZyme Description: Peroxidase (Fragment) [Source:UniProtKB/TrEMBL;Acc:A0A0H2TZX6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
521		56724.96	6.4368

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

• Gene Location: location=GL876973:243986-245773(+)

Full Sequence      

MRAPTFATALLLAVAPLAHAASCPFSQQSSNVIPETLEKRAEGGAPATFGTCARKSNMAG
GGTRSSDWWPCSLRLDVLRQFFPEISPLGGQFDYAEAFSKLDYAALKKDLTALMTQSQDW
WPADFGHYGGLFIRLAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNGNLDKARLLLWP
IKQKYGNAISWADLYLLAGNVALESMGFKTIGFGAGRPDTFQSDEGIYWGAETTFVPKGN
DVRYNGSTDVRERASHLETPLGASHMGLIYVNPEGPDGNSKPEDSALDIRVAFARMGMND
TETAALIAGGHAFGKTHGAVPGDKIGPEPEANDMGMGLGWINSVGKGNAENTRTSGLEVV
WTKTPTKWSNDFIESLYKNQWQLVTGPGGGKHWEAVNGTLDYPDAFDKKKFHKARMLTSD
LALIKDPAYAKITKRWLDHPQELADEFAKAWYKLLHRDMGPRARYLGPEVPKQDFIWQDP
LPAAEGPVIDDGEVAQLKQQILSTPGLTVANLVSAAWASAS

Enzyme Prediction     

No EC number prediction in KLU89463.1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173824	catalase_peroxidase_1	0.0	60	475	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.
272957	cat_per_HPI	0.0	59	521	10	460	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]
237891	PRK15061	0.0	59	521	12	467	catalase/peroxidase.
223453	KatG	0.0	47	521	13	477	Catalase (peroxidase I) [Inorganic ion transport and metabolism].
173823	plant_peroxidase_like	1.50e-46	123	456	12	255	Heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ91589.1|AA0	1.03e-222	16	521	14	532
UKZ83034.1|AA0	1.45e-219	16	521	14	531
UKZ91289.1|AA0	1.01e-209	57	521	13	493
UPK95725.1|AA0	5.37e-188	57	521	75	548
UPM44564.1|AA0	6.67e-164	65	521	5	456

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5CJH_A	3.82e-276	23	521	4	503	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]
3UT2_A	2.53e-274	23	521	4	503	Crystal Structure of Fungal MagKatG2 [Pyricularia oryzae 70-15],3UT2_B Crystal Structure of Fungal MagKatG2 [Pyricularia oryzae 70-15]
5WHQ_A	4.69e-205	54	521	22	504	Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A [Neurospora crassa OR74A],5WHQ_B Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.9 A [Neurospora crassa OR74A]
5WHS_A	3.04e-203	54	521	22	504	Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.6 A [Neurospora crassa OR74A],5WHS_B Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.6 A [Neurospora crassa OR74A]
5L05_A	1.06e-196	59	521	13	469	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A4QUT2|KATG2_MAGO7	4.20e-275	23	521	26	525	Catalase-peroxidase 2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=KATG2 PE=1 SV=1
sp|Q0CD12|KATG_ASPTN	3.09e-218	57	521	9	470	Catalase-peroxidase OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=katG PE=3 SV=1
sp|A1C8R3|KATG_ASPCL	1.98e-214	49	521	8	493	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
sp|Q8NJN2|KATG_TALMA	5.38e-214	55	521	14	480	Catalase-peroxidase OS=Talaromyces marneffei OX=37727 GN=katG PE=2 SV=1
sp|B2WH84|KATG_PYRTR	5.62e-214	50	521	4	493	Catalase-peroxidase OS=Pyrenophora tritici-repentis (strain Pt-1C-BFP) OX=426418 GN=katG PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000437	0.999554	CS pos: 20-21. Pr: 0.9726

TMHMM  Annotations     

There is no transmembrane helices in KLU89463.1.