Species | Aspergillus oryzae | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae | |||||||||||
CAZyme ID | AO090003000878-T-p1 | |||||||||||
CAZy Family | PL7 | |||||||||||
CAZyme Description | Has domain(s) with predicted UDP-N-acetylmuramate dehydrogenase activity, catalytic activity, flavin adenine dinucleotide binding activity and role in oxidation-reduction process | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 1.1.3.38:1 |
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Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
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396238 | FAD_binding_4 | 6.68e-10 | 11 | 93 | 1 | 78 | 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 | 2.28e-06 | 10 | 98 | 31 | 114 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
397178 | FAD-oxidase_C | 0.002 | 285 | 369 | 147 | 247 | FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold. |
183043 | PRK11230 | 0.004 | 287 | 370 | 372 | 471 | glycolate oxidase subunit GlcD; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.78e-116 | 6 | 381 | 63 | 552 | |
3.78e-116 | 6 | 381 | 63 | 552 | |
3.78e-116 | 6 | 381 | 63 | 552 | |
4.26e-115 | 6 | 381 | 63 | 552 | |
8.50e-115 | 6 | 381 | 63 | 552 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.40e-81 | 3 | 377 | 63 | 553 | STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant [Penicillium simplicissimum],1W1M_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant [Penicillium simplicissimum] |
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1.32e-80 | 3 | 377 | 63 | 553 | 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] |
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1.32e-80 | 3 | 377 | 63 | 553 | Structure of the Y503F mutant of vanillyl alcohol oxidase [Penicillium simplicissimum],5MXU_B Structure of the Y503F mutant of vanillyl alcohol oxidase [Penicillium simplicissimum] |
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2.61e-80 | 3 | 377 | 63 | 553 | 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] |
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2.61e-80 | 3 | 377 | 63 | 553 | STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE [Penicillium simplicissimum],1QLT_B STRUCTURE OF THE H422A MUTANT OF THE FLAVOENZYME VANILLYL-ALCOHOL OXIDASE [Penicillium simplicissimum],1QLU_A Structure Of The H422a Mutant Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],1QLU_B Structure Of The H422a Mutant Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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1.89e-79 | 3 | 377 | 63 | 553 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
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7.79e-34 | 11 | 372 | 58 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
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5.48e-06 | 11 | 110 | 144 | 241 | D-lactate dehydrogenase [cytochrome], mitochondrial OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=DLD1 PE=3 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000025 | 0.000000 |
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