Species | Aspergillus fischeri | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri | |||||||||||
CAZyme ID | EAW21804.1 | |||||||||||
CAZy Family | GH54|CBM42 | |||||||||||
CAZyme Description | isoamyl alcohol oxidase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 113 | 569 | 8.9e-55 | 0.9650655021834061 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 1.63e-20 | 117 | 267 | 1 | 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 | 3.37e-11 | 115 | 311 | 30 | 218 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
369658 | BBE | 7.80e-09 | 531 | 569 | 1 | 39 | 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 |
---|---|---|---|---|---|
1.80e-56 | 11 | 593 | 488 | 1064 | |
1.80e-56 | 11 | 593 | 488 | 1064 | |
8.34e-15 | 113 | 575 | 62 | 491 | |
1.48e-14 | 117 | 574 | 164 | 592 | |
4.07e-14 | 223 | 575 | 131 | 462 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.64e-165 | 21 | 593 | 28 | 596 | 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] |
|
5.14e-74 | 1 | 579 | 1 | 563 | 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] |
|
2.88e-20 | 116 | 574 | 47 | 468 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
|
3.83e-20 | 116 | 574 | 47 | 468 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
|
5.54e-16 | 117 | 317 | 54 | 238 | Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.09e-173 | 18 | 583 | 56 | 621 | FAD-linked oxidoreductase hmp9 OS=Hypomyces subiculosus OX=193393 GN=hpm9 PE=1 SV=1 |
|
2.22e-126 | 6 | 582 | 8 | 577 | FAD-linked oxidoreductase apf9 OS=Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) OX=1279085 GN=apf9 PE=1 SV=1 |
|
1.19e-92 | 3 | 582 | 7 | 560 | FAD-linked oxidoreductase patO OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patO PE=1 SV=1 |
|
2.57e-81 | 22 | 581 | 38 | 564 | FAD-linked oxidoreductase sor8 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=sor8 PE=3 SV=1 |
|
7.27e-79 | 5 | 576 | 14 | 553 | FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000227 | 0.999758 | CS pos: 17-18. Pr: 0.9781 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.