Species | Aspergillus versicolor | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus versicolor | |||||||||||
CAZyme ID | ASPVEDRAFT_199430-t33_1-p1 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 32 | 564 | 4.3e-144 | 0.9885057471264368 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 1.62e-32 | 85 | 224 | 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 | 1.44e-23 | 63 | 555 | 7 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
178402 | PLN02805 | 5.42e-12 | 84 | 283 | 133 | 323 | D-lactate dehydrogenase [cytochrome] |
183043 | PRK11230 | 1.96e-09 | 75 | 301 | 44 | 261 | glycolate oxidase subunit GlcD; Provisional |
397178 | FAD-oxidase_C | 0.001 | 443 | 554 | 138 | 247 | FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 1 | 578 | 1 | 578 | |
3.52e-281 | 8 | 566 | 7 | 569 | |
1.27e-267 | 1 | 566 | 1 | 566 | |
8.29e-263 | 8 | 541 | 7 | 544 | |
1.15e-240 | 1 | 571 | 1 | 572 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.00e-98 | 34 | 563 | 5 | 522 | Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1] |
|
2.18e-96 | 31 | 568 | 9 | 559 | Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
|
6.05e-96 | 31 | 568 | 9 | 559 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
|
1.20e-95 | 31 | 568 | 9 | 559 | STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum] |
|
1.68e-95 | 31 | 568 | 9 | 559 | STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum],1W1J_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.71e-94 | 31 | 568 | 9 | 559 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
|
5.69e-87 | 33 | 557 | 8 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
|
4.11e-19 | 75 | 301 | 31 | 247 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
|
1.20e-15 | 54 | 315 | 12 | 260 | Uncharacterized FAD-linked oxidoreductase Rv2280 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2280 PE=1 SV=1 |
|
1.20e-15 | 54 | 315 | 12 | 260 | Uncharacterized FAD-linked oxidoreductase MT2338 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2338 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000042 | 0.000040 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.