Species | Aspergillus sydowii | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus sydowii | |||||||||||
CAZyme ID | ASPSYDRAFT_55449-t33_1-p1 | |||||||||||
CAZy Family | GH47 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 4 | 535 | 1.9e-145 | 0.9827586206896551 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 2.47e-32 | 62 | 201 | 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 | 4.22e-30 | 52 | 530 | 17 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
178402 | PLN02805 | 1.15e-12 | 46 | 271 | 116 | 333 | D-lactate dehydrogenase [cytochrome] |
183043 | PRK11230 | 9.79e-09 | 61 | 246 | 55 | 232 | glycolate oxidase subunit GlcD; Provisional |
397178 | FAD-oxidase_C | 0.002 | 329 | 529 | 62 | 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 |
---|---|---|---|---|---|
1.81e-208 | 2 | 537 | 3 | 535 | |
7.69e-199 | 7 | 533 | 1 | 525 | |
3.69e-196 | 2 | 532 | 3 | 534 | |
1.66e-195 | 7 | 533 | 1 | 525 | |
3.00e-195 | 2 | 532 | 3 | 534 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.05e-109 | 5 | 534 | 3 | 518 | 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] |
|
3.50e-96 | 5 | 533 | 4 | 522 | Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBG_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_A Chain A, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_B Chain B, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_C Chain C, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_D Chain D, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_E Chain E, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_F Chain F, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_G Chain G, FAD-binding oxidoreductase [Gulosibacter chungangensis],7PBI_H Chain H, FAD-binding oxidoreductase [Gulosibacter chungangensis] |
|
2.27e-95 | 7 | 535 | 12 | 551 | 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] |
|
6.33e-95 | 7 | 535 | 12 | 551 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
|
1.25e-94 | 7 | 535 | 12 | 551 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.44e-94 | 7 | 535 | 12 | 551 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
|
7.40e-88 | 60 | 532 | 56 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
|
2.51e-14 | 62 | 246 | 41 | 218 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
|
6.76e-11 | 62 | 201 | 40 | 178 | Uncharacterized FAD-linked oxidoreductase MT2338 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2338 PE=3 SV=1 |
|
6.76e-11 | 62 | 201 | 40 | 178 | Uncharacterized FAD-linked oxidoreductase Rv2280 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2280 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000051 | 0.000001 |
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