Species | Aspergillus glaucus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus glaucus | |||||||||||
CAZyme ID | ASPGLDRAFT_131303-t33_1-p1 | |||||||||||
CAZy Family | AA7 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.26:2 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 23 | 362 | 7.8e-67 | 0.962457337883959 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 5.14e-164 | 29 | 363 | 1 | 337 | glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV). This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), among others. These enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
214757 | Glyco_32 | 3.92e-63 | 23 | 531 | 1 | 436 | Glycosyl hydrolases family 32. |
350110 | GH32_FFase | 1.84e-54 | 29 | 361 | 1 | 281 | Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. |
224536 | SacC | 3.08e-51 | 10 | 565 | 20 | 482 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
395193 | Glyco_hydro_32N | 8.58e-46 | 23 | 361 | 1 | 297 | Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 2 | 572 | 28 | 598 | |
6.69e-247 | 19 | 568 | 48 | 616 | |
6.69e-247 | 19 | 568 | 48 | 616 | |
2.71e-246 | 19 | 568 | 48 | 616 | |
2.71e-246 | 19 | 568 | 48 | 616 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.05e-58 | 18 | 568 | 65 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
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9.05e-58 | 18 | 568 | 65 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
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1.16e-56 | 18 | 568 | 63 | 632 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FK7_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],5FK8_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FK8_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],5FKB_A Chain A, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FKB_B Chain B, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FKC_A Chain A, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FKC_B Chain B, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FMC_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FMC_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
|
1.20e-56 | 18 | 568 | 65 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FIX_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],5FMB_A Chain A, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FMB_B Chain B, BETA-FRUCTOFURANOSIDASE [Phaffia rhodozyma],5FMD_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5FMD_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
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1.20e-56 | 18 | 568 | 65 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5NSL_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],5O47_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5O47_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],6FJE_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6FJE_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],6FJG_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6FJG_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],6S2G_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S2G_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],6S2H_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S2H_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma],6S3Z_A Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S3Z_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.56e-30 | 17 | 363 | 122 | 449 | Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1 |
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4.86e-29 | 19 | 357 | 55 | 369 | Beta-fructofuranosidase, insoluble isoenzyme 2 OS=Oryza sativa subsp. indica OX=39946 GN=CIN2 PE=2 SV=2 |
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4.86e-29 | 19 | 357 | 55 | 369 | Beta-fructofuranosidase, insoluble isoenzyme 2 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN2 PE=1 SV=1 |
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3.64e-28 | 5 | 361 | 34 | 360 | Beta-fructofuranosidase, insoluble isoenzyme CWINV2 OS=Arabidopsis thaliana OX=3702 GN=CWINV2 PE=2 SV=1 |
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1.58e-27 | 16 | 357 | 51 | 362 | Beta-fructofuranosidase, cell wall isozyme OS=Zea mays OX=4577 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999928 | 0.000136 |
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