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CAZyme Information: FPRO_09580-t41_1-p1
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Fusarium proliferatum | |||||||||||
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| Lineage | Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum | |||||||||||
| CAZyme ID | FPRO_09580-t41_1-p1 | |||||||||||
| CAZy Family | GH2 | |||||||||||
| CAZyme Description | uncharacterized protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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Enzyme Prediction help
| EC | 3.2.1.26:10 | 2.4.1.100:6 | 2.4.1.-:2 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH32 | 48 | 396 | 4.2e-42 | 0.962457337883959 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 350133 | GH32_XdINV-like | 6.67e-127 | 54 | 395 | 1 | 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 | 1.75e-45 | 54 | 395 | 1 | 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 | 5.30e-44 | 48 | 571 | 1 | 436 | Glycosyl hydrolases family 32. |
| 400517 | Glyco_hydro_32C | 8.83e-26 | 457 | 608 | 22 | 162 | Glycosyl hydrolases family 32 C terminal. This domain corresponds to the C terminal domain of glycosyl hydrolase family 32. It forms a beta sandwich module. |
| 395193 | Glyco_hydro_32N | 1.99e-24 | 48 | 395 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 0.0 | 1 | 619 | 1 | 619 | |
| 0.0 | 1 | 619 | 1 | 619 | |
| 0.0 | 1 | 619 | 64 | 682 | |
| 0.0 | 1 | 619 | 82 | 700 | |
| 0.0 | 1 | 619 | 1 | 619 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3.92e-294 | 22 | 618 | 5 | 604 | 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] |
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| 1.20e-249 | 22 | 617 | 4 | 634 | Crystal structure of fructosyltransferase (wild-type) from A. japonicus [Aspergillus japonicus],3LFI_A Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus],3LFI_B Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus] |
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| 1.96e-248 | 22 | 617 | 4 | 634 | Crystal Structure of A. japonicus CB05 [Aspergillus japonicus],3LDR_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with 1-Kestose [Aspergillus japonicus],3LEM_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with Nystose [Aspergillus japonicus],3LIG_A Crystal structure of fructosyltransferase (D191A) from A. japonicus [Aspergillus japonicus],3LIH_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with raffinose [Aspergillus japonicus] |
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| 4.06e-77 | 22 | 617 | 44 | 641 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
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| 4.06e-77 | 22 | 617 | 44 | 641 | Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma] |
Swiss-Prot Hits help
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 0.000449 | 0.999531 | CS pos: 15-16. Pr: 0.9799 |