Species | Sporothrix schenckii | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii | |||||||||||
CAZyme ID | SPSK_02428-t39_1-p1 | |||||||||||
CAZy Family | CE1 | |||||||||||
CAZyme Description | beta-fructofuranosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 1 | 312 | 4.6e-48 | 0.8361774744027304 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 7.19e-129 | 1 | 313 | 34 | 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 | 3.01e-50 | 1 | 494 | 38 | 436 | Glycosyl hydrolases family 32. |
350110 | GH32_FFase | 3.83e-49 | 1 | 311 | 32 | 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 | 1.17e-32 | 1 | 494 | 70 | 448 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
395193 | Glyco_hydro_32N | 1.21e-31 | 1 | 320 | 38 | 308 | 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 |
---|---|---|---|---|---|
1.28e-250 | 1 | 536 | 56 | 583 | |
1.58e-235 | 1 | 536 | 50 | 590 | |
1.74e-233 | 1 | 536 | 20 | 548 | |
7.22e-194 | 1 | 536 | 49 | 574 | |
9.62e-192 | 1 | 536 | 52 | 581 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.74e-51 | 16 | 536 | 79 | 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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3.70e-40 | 23 | 504 | 87 | 598 | 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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4.36e-39 | 23 | 504 | 87 | 598 | 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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1.16e-37 | 1 | 536 | 101 | 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] |
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1.18e-37 | 1 | 536 | 103 | 634 | 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 |
---|---|---|---|---|---|---|
5.70e-13 | 3 | 534 | 91 | 578 | Beta-fructofuranosidase, insoluble isoenzyme CWINV2 OS=Arabidopsis thaliana OX=3702 GN=CWINV2 PE=2 SV=1 |
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1.25e-10 | 1 | 311 | 163 | 435 | Sucrose:sucrose 1-fructosyltransferase OS=Festuca arundinacea OX=4606 GN=1-SST PE=1 SV=1 |
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4.71e-10 | 1 | 311 | 81 | 360 | Beta-fructofuranosidase, insoluble isoenzyme 6 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN6 PE=2 SV=1 |
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1.77e-09 | 3 | 321 | 139 | 401 | Probable sucrose-6-phosphate hydrolase OS=Psychromonas ingrahamii (strain 37) OX=357804 GN=Ping_0974 PE=3 SV=1 |
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4.92e-07 | 1 | 313 | 83 | 357 | Beta-fructofuranosidase, insoluble isoenzyme 7 OS=Oryza sativa subsp. indica OX=39946 GN=CIN7 PE=2 SV=2 |
Other | SP_Sec_SPI | CS Position |
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1.000067 | 0.000000 |
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