Species | Fusarium mangiferae | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium mangiferae | |||||||||||
CAZyme ID | CVK85901.1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A1L7SHA7] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 119 | 324 | 1.3e-47 | 0.43013100436681223 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
223354 | GlcD | 8.10e-28 | 95 | 559 | 19 | 458 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
396238 | FAD_binding_4 | 2.05e-23 | 119 | 257 | 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. |
369658 | BBE | 3.96e-13 | 500 | 538 | 1 | 39 | Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. |
215242 | PLN02441 | 3.16e-06 | 122 | 288 | 72 | 240 | cytokinin dehydrogenase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.05e-72 | 18 | 558 | 495 | 1065 | |
8.05e-72 | 18 | 558 | 495 | 1065 | |
1.05e-17 | 119 | 545 | 74 | 497 | |
4.49e-15 | 126 | 289 | 31 | 189 | |
6.74e-15 | 122 | 288 | 55 | 216 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.23e-135 | 1 | 558 | 6 | 573 | Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464] |
|
1.44e-72 | 21 | 558 | 28 | 597 | Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464] |
|
4.37e-18 | 116 | 537 | 45 | 462 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
|
4.37e-18 | 116 | 537 | 45 | 462 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
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5.66e-18 | 127 | 543 | 49 | 469 | Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.50e-207 | 6 | 559 | 13 | 563 | FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2 |
|
2.94e-157 | 1 | 558 | 1 | 567 | FAD-linked oxidoreductase patO OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patO PE=1 SV=1 |
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5.69e-157 | 9 | 558 | 10 | 566 | FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1 |
|
4.70e-151 | 17 | 558 | 33 | 572 | FAD-linked oxidoreductase sor8 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=sor8 PE=3 SV=1 |
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1.15e-134 | 1 | 558 | 6 | 573 | VAO-type flavoprotein oxidase VAO615 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=MYCTH_2305637 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.000318 | 0.999643 | CS pos: 18-19. Pr: 0.9720 |
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