Species | Aspergillus niger | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger | |||||||||||
CAZyme ID | M747DRAFT_327661-t43_1-p1 | |||||||||||
CAZy Family | GH51|GH51 | |||||||||||
CAZyme Description | FAD-binding domain-containing protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 48 | 483 | 7.3e-47 | 0.980349344978166 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
396238 | FAD_binding_4 | 5.08e-18 | 60 | 196 | 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 | 1.02e-16 | 60 | 268 | 32 | 244 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
215242 | PLN02441 | 2.90e-10 | 60 | 219 | 65 | 233 | cytokinin dehydrogenase |
273751 | FAD_lactone_ox | 0.004 | 46 | 206 | 2 | 160 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
7.98e-21 | 33 | 490 | 21 | 474 | |
7.98e-21 | 33 | 490 | 21 | 474 | |
2.59e-20 | 33 | 490 | 21 | 474 | |
8.22e-20 | 60 | 483 | 37 | 464 | |
2.26e-19 | 60 | 483 | 62 | 489 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.97e-21 | 60 | 483 | 43 | 470 | Chain A, Glucooligosaccharide oxidase [Sarocladium strictum] |
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7.97e-21 | 60 | 483 | 43 | 470 | The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum] |
|
5.13e-19 | 39 | 223 | 25 | 207 | The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus] |
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9.17e-19 | 39 | 223 | 25 | 207 | The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus] |
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9.17e-19 | 39 | 223 | 25 | 207 | The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.94e-85 | 25 | 493 | 32 | 507 | FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1 |
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6.40e-83 | 25 | 493 | 32 | 507 | FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1 |
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6.40e-83 | 25 | 493 | 32 | 507 | FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1 |
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4.68e-66 | 25 | 493 | 9 | 476 | FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1 |
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2.60e-62 | 48 | 493 | 66 | 517 | FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.692464 | 0.307533 |
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