Species | Globisporangium ultimum | |||||||||||
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Lineage | Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum | |||||||||||
CAZyme ID | PUG3_T011597-RA-p1 | |||||||||||
CAZy Family | GT19 | |||||||||||
CAZyme Description | Glycoside hydrolase | |||||||||||
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 | 1 | 302 | 1.1e-53 | 0.8805460750853242 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 2.23e-115 | 1 | 302 | 20 | 335 | 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. |
350110 | GH32_FFase | 1.42e-62 | 1 | 302 | 18 | 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. |
214757 | Glyco_32 | 8.28e-48 | 1 | 439 | 24 | 404 | Glycosyl hydrolases family 32. |
395193 | Glyco_hydro_32N | 2.83e-40 | 1 | 300 | 24 | 295 | 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 | 2.27e-32 | 1 | 522 | 56 | 479 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
3.81e-211 | 1 | 542 | 72 | 619 | |
1.52e-176 | 1 | 539 | 63 | 598 | |
1.81e-145 | 1 | 533 | 62 | 595 | |
1.81e-70 | 1 | 536 | 70 | 618 | |
2.17e-70 | 1 | 526 | 106 | 634 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.70e-53 | 3 | 533 | 94 | 636 | 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] |
|
2.77e-53 | 3 | 533 | 96 | 638 | 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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2.77e-53 | 3 | 533 | 96 | 638 | 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] |
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2.77e-53 | 3 | 533 | 96 | 638 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
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2.77e-53 | 3 | 533 | 96 | 638 | 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 |
---|---|---|---|---|---|---|
2.38e-22 | 1 | 530 | 76 | 571 | Beta-fructofuranosidase, insoluble isoenzyme 1 OS=Oryza sativa subsp. indica OX=39946 GN=CIN1 PE=2 SV=2 |
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1.02e-21 | 1 | 403 | 30 | 382 | Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1 |
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1.78e-21 | 1 | 530 | 76 | 571 | Beta-fructofuranosidase, insoluble isoenzyme 1 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN1 PE=2 SV=1 |
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2.74e-20 | 1 | 527 | 131 | 622 | Acid beta-fructofuranosidase OS=Solanum lycopersicum OX=4081 GN=TIV1 PE=2 SV=1 |
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4.96e-20 | 2 | 526 | 134 | 627 | Acid beta-fructofuranosidase 3, vacuolar OS=Arabidopsis thaliana OX=3702 GN=BFRUCT3 PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000057 | 0.000000 |
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