Species | Kwoniella dejecticola | |||||||||||
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Lineage | Basidiomycota; Tremellomycetes; ; Cryptococcaceae; Kwoniella; Kwoniella dejecticola | |||||||||||
CAZyme ID | I303_00733-t42_1-p1 | |||||||||||
CAZy Family | AA6 | |||||||||||
CAZyme Description | beta-fructofuranosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 3.2.1.26:5 | 3.2.1.80:2 | 2.4.1.-:1 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 48 | 354 | 9.1e-91 | 0.9897610921501706 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350134 | GH32_Inu-like | 1.32e-136 | 53 | 339 | 1 | 286 | glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), 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. 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 | 2.39e-117 | 39 | 519 | 24 | 486 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
214757 | Glyco_32 | 5.23e-109 | 48 | 480 | 1 | 437 | Glycosyl hydrolases family 32. |
395193 | Glyco_hydro_32N | 6.28e-96 | 48 | 355 | 1 | 307 | 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. |
350110 | GH32_FFase | 9.76e-71 | 54 | 338 | 1 | 277 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
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2.49e-271 | 23 | 522 | 25 | 518 | |
2.49e-271 | 23 | 522 | 25 | 518 | |
7.12e-271 | 23 | 522 | 25 | 518 | |
2.04e-270 | 23 | 522 | 25 | 518 | |
1.67e-269 | 23 | 522 | 25 | 518 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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5.15e-109 | 44 | 485 | 8 | 477 | Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_B Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_C Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_D Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_E Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_F Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_G Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_H Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C] |
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3.26e-106 | 44 | 492 | 10 | 479 | Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
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3.56e-106 | 44 | 492 | 13 | 482 | Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
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5.45e-105 | 44 | 492 | 36 | 505 | 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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1.08e-104 | 44 | 492 | 36 | 505 | Chain A, Fructofuranosidase [Schwanniomyces occidentalis],3U14_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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4.77e-108 | 44 | 485 | 28 | 497 | Invertase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SUC2 PE=1 SV=1 |
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7.47e-107 | 44 | 485 | 28 | 497 | Invertase 4 OS=Saccharomyces cerevisiae OX=4932 GN=SUC4 PE=3 SV=1 |
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1.17e-105 | 44 | 485 | 28 | 497 | Invertase 1 OS=Saccharomyces cerevisiae OX=4932 GN=SUC1 PE=1 SV=1 |
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1.39e-105 | 43 | 485 | 27 | 512 | Invertase OS=Wickerhamomyces anomalus OX=4927 GN=INV1 PE=3 SV=1 |
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1.25e-104 | 44 | 485 | 39 | 519 | Inulinase OS=Kluyveromyces marxianus OX=4911 GN=INU1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.000219 | 0.999762 | CS pos: 21-22. Pr: 0.9793 |
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