Species | Cladophialophora carrionii | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora carrionii | |||||||||||
CAZyme ID | CLCR_00087-t43_1-p1 | |||||||||||
CAZy Family | AA1 | |||||||||||
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 | 52 | 590 | 2.6e-214 | 0.9942528735632183 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
223354 | GlcD | 4.84e-30 | 110 | 577 | 31 | 454 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
396238 | FAD_binding_4 | 5.78e-28 | 115 | 251 | 5 | 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 | 9.25e-09 | 109 | 305 | 54 | 241 | glycolate oxidase subunit GlcD; Provisional |
178402 | PLN02805 | 4.83e-08 | 115 | 295 | 138 | 308 | D-lactate dehydrogenase [cytochrome] |
397178 | FAD-oxidase_C | 1.96e-06 | 453 | 576 | 125 | 246 | 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 |
---|---|---|---|---|---|
4.57e-300 | 9 | 614 | 7 | 604 | |
6.74e-295 | 12 | 614 | 10 | 604 | |
9.56e-295 | 9 | 614 | 7 | 604 | |
7.25e-294 | 12 | 607 | 12 | 601 | |
1.05e-291 | 12 | 614 | 10 | 604 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.08e-178 | 50 | 592 | 8 | 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] |
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2.89e-177 | 50 | 592 | 8 | 560 | Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum] |
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5.79e-177 | 50 | 592 | 8 | 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] |
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5.79e-177 | 50 | 592 | 8 | 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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8.20e-177 | 50 | 592 | 8 | 560 | STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.98e-176 | 50 | 592 | 8 | 560 | Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1 |
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3.34e-112 | 54 | 580 | 9 | 515 | 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3 |
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2.46e-14 | 113 | 322 | 42 | 243 | D-2-hydroxyglutarate dehydrogenase OS=Xanthomonas citri pv. viticola (strain LMG 965 / NCPPB 2475 / ICMP 3867 / CFBP 7660) OX=1232713 GN=XVT_549 PE=1 SV=1 |
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4.30e-14 | 108 | 487 | 38 | 403 | Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1 |
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5.37e-13 | 112 | 323 | 42 | 245 | D-2-hydroxyglutarate dehydrogenase OS=Pseudomonas stutzeri (strain A1501) OX=379731 GN=d2hgdh PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000056 | 0.000000 |
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