Species | Aspergillus niger | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger | |||||||||||
CAZyme ID | M747DRAFT_318077-t43_1-p1 | |||||||||||
CAZy Family | GH35 | |||||||||||
CAZyme Description | Arabinanase/levansucrase/invertase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 14 | 365 | 4.8e-65 | 0.9590443686006825 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 5.02e-156 | 20 | 367 | 2 | 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 | 2.15e-71 | 14 | 540 | 1 | 436 | Glycosyl hydrolases family 32. |
350110 | GH32_FFase | 1.45e-65 | 19 | 365 | 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 | 1.73e-52 | 10 | 540 | 29 | 448 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
395193 | Glyco_hydro_32N | 9.20e-51 | 14 | 365 | 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 | 1 | 601 | 1 | 601 | |
0.0 | 1 | 601 | 1 | 601 | |
6.88e-230 | 11 | 581 | 8 | 574 | |
1.73e-218 | 11 | 581 | 9 | 590 | |
3.98e-216 | 11 | 582 | 15 | 584 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.88e-53 | 11 | 581 | 28 | 596 | Aspergillus kawachii beta-fructofuranosidase complexed with glycerol [Aspergillus luchuensis IFO 4308],5XH9_A Aspergillus kawachii beta-fructofuranosidase [Aspergillus luchuensis IFO 4308],5XHA_A Aspergillus kawachii beta-fructofuranosidase complexed with fructose [Aspergillus luchuensis IFO 4308] |
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2.71e-48 | 11 | 581 | 28 | 627 | Crystal structure of fructosyltransferase (wild-type) from A. japonicus [Aspergillus japonicus],3LFI_A Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus],3LFI_B Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus] |
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3.36e-47 | 11 | 581 | 28 | 627 | Crystal Structure of A. japonicus CB05 [Aspergillus japonicus],3LDR_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with 1-Kestose [Aspergillus japonicus],3LEM_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with Nystose [Aspergillus japonicus],3LIG_A Crystal structure of fructosyltransferase (D191A) from A. japonicus [Aspergillus japonicus],3LIH_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with raffinose [Aspergillus japonicus] |
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3.33e-44 | 11 | 594 | 67 | 656 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
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3.33e-44 | 11 | 594 | 67 | 656 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.63e-29 | 14 | 578 | 129 | 653 | Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1 |
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1.10e-27 | 13 | 578 | 58 | 583 | Beta-fructofuranosidase, insoluble isoenzyme 1 OS=Daucus carota OX=4039 GN=INV1 PE=1 SV=1 |
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2.44e-27 | 19 | 406 | 114 | 450 | Acid beta-fructofuranosidase OS=Solanum lycopersicum OX=4081 GN=TIV1 PE=2 SV=1 |
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6.78e-27 | 8 | 578 | 54 | 577 | Fructan 6-exohydrolase OS=Beta vulgaris OX=161934 GN=6-FEH PE=1 SV=1 |
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8.19e-27 | 14 | 550 | 51 | 547 | Beta-fructofuranosidase, insoluble isoenzyme 3 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN3 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999992 | 0.000070 |
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