Species | Fusarium oxysporum | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum | |||||||||||
CAZyme ID | FOZG_18067-t36_1-p1 | |||||||||||
CAZy Family | GT50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 19 | 364 | 3.1e-64 | 0.9590443686006825 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350133 | GH32_XdINV-like | 1.17e-146 | 24 | 366 | 1 | 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 | 6.13e-73 | 19 | 543 | 1 | 436 | Glycosyl hydrolases family 32. |
350110 | GH32_FFase | 5.92e-66 | 25 | 364 | 2 | 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. |
395193 | Glyco_hydro_32N | 1.01e-46 | 19 | 364 | 1 | 297 | 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 | 3.27e-46 | 15 | 543 | 29 | 448 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
0.0 | 48 | 594 | 11 | 557 | |
1.12e-291 | 15 | 590 | 14 | 588 | |
3.23e-268 | 15 | 587 | 8 | 592 | |
5.40e-220 | 10 | 585 | 2 | 574 | |
1.56e-204 | 11 | 593 | 6 | 590 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.98e-51 | 5 | 585 | 22 | 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] |
|
1.84e-45 | 15 | 585 | 66 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
|
1.84e-45 | 15 | 585 | 66 | 634 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
|
2.16e-44 | 15 | 585 | 64 | 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] |
|
2.20e-44 | 15 | 585 | 66 | 634 | 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 |
---|---|---|---|---|---|---|
3.47e-28 | 15 | 590 | 125 | 660 | Beta-fructofuranosidase 1 OS=Zea mays OX=4577 GN=IVR1 PE=3 SV=1 |
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1.12e-27 | 15 | 364 | 47 | 362 | Beta-fructofuranosidase, cell wall isozyme OS=Pisum sativum OX=3888 GN=BFRUCT1 PE=2 SV=1 |
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2.06e-27 | 8 | 582 | 65 | 594 | 6(G)-fructosyltransferase OS=Asparagus officinalis OX=4686 GN=FT1 PE=1 SV=1 |
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5.52e-25 | 15 | 362 | 104 | 413 | Acid beta-fructofuranosidase OS=Solanum lycopersicum OX=4081 GN=TIV1 PE=2 SV=1 |
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1.42e-24 | 15 | 552 | 121 | 614 | Acid beta-fructofuranosidase 4, vacuolar OS=Arabidopsis thaliana OX=3702 GN=BFRUCT4 PE=1 SV=2 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.998833 | 0.001210 |
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