Species | Aspergillus clavatus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus | |||||||||||
CAZyme ID | ACLA_020400-t26_1-p1 | |||||||||||
CAZy Family | CE16 | |||||||||||
CAZyme Description | sugar 1,4-lactone oxidase, putative | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
AA7 | 29 | 204 | 1.5e-27 | 0.38427947598253276 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
273751 | FAD_lactone_ox | 2.90e-141 | 30 | 472 | 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 | 4.78e-105 | 197 | 479 | 1 | 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 | 1.21e-40 | 14 | 471 | 14 | 450 | FAD/FMN-containing dehydrogenase [Energy production and conversion]. |
215258 | PLN02465 | 6.34e-39 | 30 | 261 | 89 | 315 | L-galactono-1,4-lactone dehydrogenase |
396238 | FAD_binding_4 | 7.00e-37 | 38 | 173 | 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 |
---|---|---|---|---|---|
2.93e-11 | 83 | 257 | 121 | 318 | |
4.67e-11 | 38 | 217 | 164 | 354 | |
1.34e-10 | 38 | 221 | 59 | 254 | |
2.05e-10 | 38 | 221 | 62 | 256 | |
1.01e-09 | 16 | 200 | 51 | 242 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.80e-29 | 25 | 483 | 110 | 607 | Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea] |
|
5.76e-20 | 23 | 207 | 6 | 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)] |
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7.50e-15 | 30 | 478 | 24 | 464 | Chain A, Decaprenyl-phosphoryl-beta-d-ribofuranose-2- Oxidoreductase [Mycolicibacterium smegmatis],4F4Q_A Crystal structure of M. smegmatis DprE1 in complex with FAD and covalently bound BTZ043 [Mycolicibacterium smegmatis MC2 155] |
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9.53e-14 | 83 | 478 | 13 | 399 | Chain A, oxidoreductase DprE1 [Mycolicibacterium smegmatis],4G3U_A Chain A, oxidoreductase DprE1 [Mycolicibacterium smegmatis],4G3U_B Chain B, oxidoreductase DprE1 [Mycolicibacterium smegmatis] |
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8.92e-12 | 38 | 221 | 37 | 232 | 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 |
---|---|---|---|---|---|---|
2.99e-203 | 4 | 520 | 13 | 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 |
|
1.18e-124 | 25 | 479 | 13 | 523 | D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1 |
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2.36e-110 | 22 | 484 | 14 | 556 | D-arabinono-1,4-lactone oxidase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALO1 PE=3 SV=2 |
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7.28e-109 | 26 | 484 | 17 | 557 | D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1 |
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9.80e-107 | 19 | 472 | 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 |
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1.000079 | 0.000000 |
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