Species | Aspergillus terreus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus | |||||||||||
CAZyme ID | ATEG_06388-t26_1-p1 | |||||||||||
CAZy Family | GH36 | |||||||||||
CAZyme Description | predicted protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 122 | 568 | 7.7e-50 | 0.9475982532751092 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 3.83e-17 | 121 | 265 | 5 | 139 | FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. |
223354 | GlcD | 8.83e-13 | 108 | 566 | 24 | 450 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
369658 | BBE | 2.97e-10 | 529 | 566 | 1 | 38 | Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.97e-60 | 10 | 578 | 491 | 1055 | |
1.97e-60 | 10 | 578 | 491 | 1055 | |
1.57e-14 | 121 | 382 | 63 | 303 | |
1.84e-13 | 127 | 320 | 80 | 259 | |
2.40e-13 | 124 | 574 | 70 | 492 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.16e-91 | 19 | 584 | 27 | 573 | Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464] |
|
4.19e-64 | 1 | 585 | 1 | 598 | Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464] |
|
3.27e-17 | 123 | 566 | 65 | 519 | Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y08_B Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y3R_A Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_B Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_C Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_D Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3S_A Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y3S_B Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y4G_A Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9],2Y4G_B Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9] |
|
2.85e-16 | 125 | 566 | 39 | 491 | Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6] |
|
1.41e-15 | 121 | 382 | 41 | 281 | Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.17e-204 | 6 | 584 | 11 | 587 | Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07056 PE=1 SV=2 |
|
1.67e-133 | 20 | 585 | 25 | 578 | FAD-linked oxidoreductase malF OS=Malbranchea aurantiaca OX=78605 GN=malF PE=1 SV=1 |
|
6.50e-132 | 11 | 583 | 17 | 587 | FAD-linked oxidoreductase notD OS=Aspergillus sp. (strain MF297-2) OX=877550 GN=notD PE=1 SV=1 |
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2.22e-127 | 13 | 584 | 24 | 580 | FAD-linked oxidoreductase notD' OS=Aspergillus versicolor OX=46472 GN=notD' PE=1 SV=1 |
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1.49e-119 | 8 | 583 | 17 | 581 | FAD-linked oxidoreductase easE OS=Epichloe festucae var. lolii OX=73839 GN=easE PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000400 | 0.999595 | CS pos: 15-16. Pr: 0.9627 |
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