Species | Scedosporium apiospermum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum | |||||||||||
CAZyme ID | SAPIO_CDS2361-t41_1-p1 | |||||||||||
CAZy Family | CE1 | |||||||||||
CAZyme Description | Vanillyl-alcohol oxidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 1.1.3.38:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA4 | 38 | 587 | 4.1e-241 | 0.9942528735632183 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 1.37e-27 | 101 | 242 | 2 | 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 | 2.04e-23 | 101 | 576 | 33 | 455 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
178402 | PLN02805 | 5.58e-11 | 51 | 245 | 96 | 274 | D-lactate dehydrogenase [cytochrome] |
183043 | PRK11230 | 7.49e-07 | 106 | 302 | 62 | 231 | glycolate oxidase subunit GlcD; Provisional |
397178 | FAD-oxidase_C | 1.70e-05 | 469 | 575 | 143 | 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 | 23 | 590 | 5 | 561 | |
5.01e-302 | 31 | 592 | 2 | 560 | |
1.83e-297 | 19 | 590 | 13 | 579 | |
2.65e-295 | 30 | 590 | 18 | 579 | |
5.33e-295 | 19 | 590 | 13 | 579 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.09e-285 | 38 | 590 | 9 | 560 | 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] |
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3.11e-285 | 38 | 590 | 9 | 560 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
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4.41e-285 | 38 | 590 | 9 | 560 | 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] |
|
6.26e-285 | 38 | 590 | 9 | 560 | Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHU_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHV_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHV_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHZ_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1AHZ_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],1VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],2VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],2VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum] |
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1.26e-284 | 38 | 590 | 9 | 560 | Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8F_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8G_A STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8G_B STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8H_A Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum],1E8H_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.22e-284 | 38 | 590 | 9 | 560 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
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4.97e-115 | 40 | 578 | 8 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
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1.71e-13 | 102 | 302 | 43 | 217 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
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2.39e-13 | 102 | 353 | 68 | 292 | Probable D-lactate dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ldhd PE=1 SV=1 |
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3.39e-13 | 102 | 347 | 68 | 309 | Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000052 | 0.000000 |
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