Species | Exophiala mesophila | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila | |||||||||||
CAZyme ID | PV10_01514-t45_1-p1 | |||||||||||
CAZy Family | AA3 | |||||||||||
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 | 71 | 434 | 2.2e-66 | 0.9590443686006825 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 7.89e-168 | 77 | 436 | 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 | 1.43e-67 | 71 | 607 | 1 | 435 | Glycosyl hydrolases family 32. |
350110 | GH32_FFase | 7.65e-61 | 77 | 434 | 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. |
395193 | Glyco_hydro_32N | 1.51e-54 | 71 | 439 | 1 | 302 | 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. |
224536 | SacC | 3.42e-49 | 66 | 619 | 28 | 460 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.79e-168 | 66 | 648 | 44 | 594 | |
1.53e-163 | 65 | 651 | 13 | 597 | |
1.53e-163 | 65 | 651 | 13 | 597 | |
2.43e-161 | 65 | 648 | 46 | 622 | |
3.89e-161 | 57 | 651 | 5 | 597 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5.59e-56 | 63 | 616 | 23 | 565 | 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] |
|
9.97e-53 | 63 | 614 | 23 | 594 | 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] |
|
1.26e-51 | 63 | 614 | 23 | 594 | 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] |
|
4.32e-45 | 63 | 648 | 62 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
|
4.32e-45 | 63 | 648 | 62 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.54e-33 | 49 | 618 | 107 | 624 | Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1 |
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2.24e-33 | 64 | 492 | 100 | 467 | Acid beta-fructofuranosidase OS=Solanum lycopersicum OX=4081 GN=TIV1 PE=2 SV=1 |
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1.07e-30 | 25 | 454 | 56 | 439 | Acid beta-fructofuranosidase AIV-18 OS=Capsicum annuum OX=4072 PE=2 SV=1 |
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2.84e-30 | 64 | 653 | 127 | 654 | Beta-fructofuranosidase, soluble isoenzyme I OS=Daucus carota OX=4039 GN=INV*DC4 PE=1 SV=2 |
|
1.09e-29 | 64 | 618 | 78 | 569 | Acid beta-fructofuranosidase 2, vacuolar OS=Rosa hybrid cultivar OX=128735 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999848 | 0.000176 |
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