Species | Phytophthora parasitica | |||||||||||
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Lineage | Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica | |||||||||||
CAZyme ID | PPTG_22710-t26_1-p1 | |||||||||||
CAZy Family | PL1|PL1 | |||||||||||
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 | 1 | 301 | 3.4e-51 | 0.856655290102389 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 3.01e-116 | 1 | 344 | 3 | 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 | 5.27e-60 | 1 | 344 | 3 | 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 | 2.50e-48 | 1 | 513 | 9 | 404 | Glycosyl hydrolases family 32. |
224536 | SacC | 3.12e-36 | 1 | 635 | 41 | 478 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
395193 | Glyco_hydro_32N | 8.03e-36 | 1 | 358 | 9 | 305 | 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 |
---|---|---|---|---|---|
2.12e-238 | 1 | 637 | 55 | 600 | |
3.74e-135 | 1 | 637 | 46 | 582 | |
7.09e-104 | 1 | 637 | 45 | 585 | |
7.68e-76 | 1 | 137 | 2 | 138 | |
2.69e-54 | 1 | 626 | 53 | 592 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.20e-33 | 1 | 632 | 78 | 618 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
|
9.20e-33 | 1 | 632 | 78 | 618 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
|
9.34e-32 | 1 | 632 | 76 | 616 | 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] |
|
9.43e-32 | 1 | 632 | 78 | 618 | 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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9.43e-32 | 1 | 632 | 78 | 618 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
8.81e-21 | 1 | 342 | 128 | 424 | Acid beta-fructofuranosidase OS=Vigna radiata var. radiata OX=3916 GN=INVA PE=1 SV=1 |
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3.39e-19 | 1 | 374 | 118 | 440 | Acid beta-fructofuranosidase 3, vacuolar OS=Arabidopsis thaliana OX=3702 GN=BFRUCT3 PE=2 SV=1 |
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4.70e-19 | 1 | 377 | 137 | 472 | Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1 |
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5.78e-19 | 1 | 375 | 116 | 438 | Acid beta-fructofuranosidase OS=Solanum lycopersicum OX=4081 GN=TIV1 PE=2 SV=1 |
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7.76e-19 | 1 | 342 | 120 | 416 | Acid beta-fructofuranosidase OS=Vicia faba OX=3906 GN=VCINV PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.999691 | 0.000346 |
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