Species | Microsporum canis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Ascomycota; Eurotiomycetes; ; Arthrodermataceae; Microsporum; Microsporum canis | |||||||||||
CAZyme ID | EEQ33692.1 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | D-arabinono-1,4-lactone oxidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 28 | 236 | 2.6e-27 | 0.4606986899563319 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
273751 | FAD_lactone_ox | 3.68e-152 | 29 | 473 | 7 | 436 | 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. |
397924 | ALO | 3.32e-113 | 197 | 480 | 2 | 259 | D-arabinono-1,4-lactone oxidase. This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway. |
223354 | GlcD | 4.03e-42 | 27 | 472 | 21 | 450 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
215258 | PLN02465 | 3.51e-36 | 29 | 476 | 89 | 565 | L-galactono-1,4-lactone dehydrogenase |
396238 | FAD_binding_4 | 1.25e-35 | 37 | 172 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
8.47e-11 | 37 | 195 | 62 | 223 | |
8.10e-10 | 43 | 196 | 70 | 226 | |
8.10e-10 | 43 | 196 | 70 | 226 | |
8.15e-10 | 82 | 195 | 121 | 234 | |
1.42e-09 | 43 | 196 | 70 | 226 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.96e-26 | 24 | 265 | 110 | 342 | Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea] |
|
2.45e-15 | 29 | 206 | 13 | 186 | Alditol Oxidase from Streptomyces coelicolor A3(2): Native Enzyme [Streptomyces coelicolor A3(2)],2VFS_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Xylitol [Streptomyces coelicolor A3(2)],2VFT_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sorbitol [Streptomyces coelicolor A3(2)],2VFU_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Mannitol [Streptomyces coelicolor A3(2)],2VFV_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sulphite [Streptomyces coelicolor A3(2)] |
|
1.44e-10 | 9 | 197 | 18 | 212 | Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens] |
|
1.44e-10 | 9 | 197 | 18 | 212 | Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens] |
|
1.37e-09 | 29 | 202 | 46 | 228 | Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPN_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPP_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPP_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPQ_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPQ_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPT_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPT_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPU_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPU_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPX_A Chain A, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens],6LPX_B Chain B, D-2-hydroxyglutarate dehydrogenase, mitochondrial [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.70e-200 | 13 | 521 | 27 | 548 | Putative D-arabinono-1,4-lactone oxidase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alo-1 PE=3 SV=1 |
|
2.77e-131 | 20 | 482 | 9 | 525 | D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1 |
|
6.76e-116 | 17 | 480 | 10 | 552 | D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1 |
|
1.75e-112 | 22 | 473 | 14 | 513 | D-arabinono-1,4-lactone oxidase OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=ALO1 PE=3 SV=1 |
|
7.94e-112 | 18 | 473 | 6 | 509 | D-arabinono-1,4-lactone oxidase OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=ALO1 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000057 | 0.000000 |
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