Species | Hyaloperonospora arabidopsidis | |||||||||||
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Lineage | Oomycota; NA; ; Peronosporaceae; Hyaloperonospora; Hyaloperonospora arabidopsidis | |||||||||||
CAZyme ID | HpaG806372:RNA-p1 | |||||||||||
CAZy Family | GH30 | |||||||||||
CAZyme Description | unspecified product | |||||||||||
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 | 46 | 180 | 4.7e-39 | 0.4129692832764505 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 5.16e-57 | 53 | 180 | 2 | 135 | 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 | 4.79e-38 | 53 | 190 | 2 | 128 | 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 | 3.18e-37 | 46 | 180 | 1 | 127 | Glycosyl hydrolases family 32. |
224536 | SacC | 7.38e-35 | 19 | 179 | 6 | 156 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
395193 | Glyco_hydro_32N | 4.67e-32 | 46 | 180 | 1 | 125 | 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 |
---|---|---|---|---|---|
1.34e-80 | 8 | 180 | 10 | 181 | |
4.62e-79 | 53 | 179 | 1 | 127 | |
6.68e-54 | 37 | 187 | 29 | 178 | |
3.32e-41 | 37 | 175 | 28 | 167 | |
6.04e-35 | 1 | 179 | 1 | 207 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7.21e-21 | 42 | 139 | 19 | 112 | Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis [Pachysandra terminalis],3UGF_B Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis [Pachysandra terminalis],3UGG_A Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 1-kestose [Pachysandra terminalis],3UGG_B Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 1-kestose [Pachysandra terminalis],3UGH_A Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 6-kestose [Pachysandra terminalis],3UGH_B Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 6-kestose [Pachysandra terminalis] |
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5.36e-19 | 23 | 176 | 19 | 171 | Chain A, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis] |
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7.11e-19 | 28 | 176 | 1 | 148 | Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
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7.30e-19 | 41 | 138 | 4 | 97 | Chain A, Beta-fructofuranosidase [Arabidopsis thaliana] |
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7.32e-19 | 41 | 138 | 4 | 97 | Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_C Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_E Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_G Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_I Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_K Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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7.20e-24 | 36 | 139 | 125 | 224 | Beta-fructofuranosidase, soluble isoenzyme I OS=Daucus carota OX=4039 GN=INV*DC4 PE=1 SV=2 |
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3.31e-23 | 42 | 139 | 104 | 197 | Acid beta-fructofuranosidase OS=Solanum lycopersicum OX=4081 GN=TIV1 PE=2 SV=1 |
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6.27e-23 | 42 | 140 | 125 | 219 | Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1 |
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2.12e-22 | 37 | 139 | 107 | 205 | Acid beta-fructofuranosidase AIV-18 OS=Capsicum annuum OX=4072 PE=2 SV=1 |
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1.31e-21 | 22 | 138 | 35 | 147 | Beta-fructofuranosidase, insoluble isoenzyme 2 OS=Oryza sativa subsp. indica OX=39946 GN=CIN2 PE=2 SV=2 |
Other | SP_Sec_SPI | CS Position |
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0.000220 | 0.999762 | CS pos: 24-25. Pr: 0.9777 |
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