Species | Exophiala aquamarina | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina | |||||||||||
CAZyme ID | KEF53978.1 | |||||||||||
CAZy Family | CE4 | |||||||||||
CAZyme Description | FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A072P3W6] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 25 | 511 | 1.8e-114 | 0.9099616858237548 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
223354 | GlcD | 4.39e-28 | 43 | 272 | 1 | 222 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
396238 | FAD_binding_4 | 2.05e-27 | 74 | 213 | 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. |
183043 | PRK11230 | 2.60e-10 | 36 | 258 | 17 | 232 | glycolate oxidase subunit GlcD; Provisional |
178402 | PLN02805 | 2.29e-08 | 40 | 272 | 98 | 323 | D-lactate dehydrogenase [cytochrome] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
9.29e-148 | 1 | 508 | 2 | 505 | |
1.64e-144 | 4 | 508 | 10 | 520 | |
3.83e-144 | 4 | 508 | 10 | 519 | |
2.03e-141 | 4 | 510 | 7 | 518 | |
9.48e-141 | 4 | 508 | 10 | 520 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.37e-80 | 28 | 504 | 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] |
|
1.34e-73 | 27 | 516 | 7 | 487 | p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVE_B p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVF_A p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida] |
|
1.37e-73 | 27 | 516 | 8 | 488 | Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DII_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_A Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida] |
|
1.57e-68 | 21 | 510 | 5 | 512 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
|
2.20e-68 | 25 | 510 | 9 | 512 | 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 |
---|---|---|---|---|---|---|
7.05e-73 | 27 | 516 | 8 | 488 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
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8.39e-67 | 25 | 510 | 9 | 512 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
|
1.79e-19 | 74 | 271 | 41 | 231 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
|
4.07e-18 | 45 | 290 | 9 | 249 | Uncharacterized FAD-linked oxidoreductase MT2338 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2338 PE=3 SV=1 |
|
4.07e-18 | 45 | 290 | 9 | 249 | 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 |
---|---|---|
1.000078 | 0.000000 |
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