Species | Macrophomina phaseolina | |||||||||||
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Lineage | Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina | |||||||||||
CAZyme ID | EKG14269.1 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | FAD linked oxidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 200 | 527 | 5.3e-55 | 0.60727969348659 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 6.41e-26 | 76 | 234 | 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 | 3.54e-23 | 44 | 292 | 1 | 221 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
178402 | PLN02805 | 7.42e-09 | 76 | 279 | 134 | 309 | D-lactate dehydrogenase [cytochrome] |
273751 | FAD_lactone_ox | 2.10e-06 | 73 | 304 | 12 | 200 | sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. |
183043 | PRK11230 | 3.65e-06 | 76 | 150 | 56 | 128 | glycolate oxidase subunit GlcD; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
9.51e-255 | 1 | 525 | 1 | 505 | |
1.48e-137 | 5 | 525 | 7 | 516 | |
1.95e-136 | 5 | 525 | 10 | 520 | |
5.51e-136 | 5 | 525 | 10 | 520 | |
2.95e-128 | 5 | 525 | 6 | 515 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.59e-87 | 29 | 521 | 5 | 474 | 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] |
|
1.01e-66 | 29 | 521 | 6 | 479 | 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] |
|
2.80e-66 | 29 | 525 | 12 | 510 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
|
3.90e-66 | 29 | 525 | 12 | 510 | 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] |
|
3.90e-66 | 29 | 525 | 12 | 510 | 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 |
---|---|---|---|---|---|---|
5.45e-65 | 29 | 525 | 12 | 510 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
|
8.80e-65 | 26 | 523 | 6 | 478 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
|
1.17e-15 | 39 | 302 | 33 | 272 | Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1 |
|
1.28e-13 | 44 | 234 | 7 | 178 | Uncharacterized FAD-linked oxidoreductase MT2338 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2338 PE=3 SV=1 |
|
1.28e-13 | 44 | 234 | 7 | 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 |
---|---|---|
1.000041 | 0.000000 |
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