Species | Cladophialophora bantiana | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora bantiana | |||||||||||
CAZyme ID | KIW90058.1 | |||||||||||
CAZy Family | CE9 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
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 | 47 | 206 | 4.2e-36 | 0.5733788395904437 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350134 | GH32_Inu-like | 1.70e-70 | 54 | 249 | 3 | 239 | 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 | 2.50e-45 | 37 | 445 | 23 | 484 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
214757 | Glyco_32 | 1.87e-41 | 47 | 412 | 1 | 437 | Glycosyl hydrolases family 32. |
395193 | Glyco_hydro_32N | 2.93e-38 | 47 | 217 | 1 | 185 | 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 | 1.23e-20 | 55 | 249 | 3 | 232 | 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 |
---|---|---|---|---|---|
3.37e-136 | 13 | 467 | 14 | 541 | |
6.76e-133 | 21 | 467 | 38 | 563 | |
8.34e-133 | 6 | 467 | 6 | 543 | |
3.02e-132 | 25 | 470 | 34 | 557 | |
3.02e-132 | 25 | 470 | 34 | 557 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
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1.53e-52 | 43 | 421 | 10 | 476 | Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
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1.62e-52 | 43 | 421 | 13 | 479 | Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
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2.48e-52 | 43 | 421 | 36 | 502 | 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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2.59e-52 | 43 | 421 | 39 | 524 | The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042],6J0T_B The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042] |
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1.17e-51 | 43 | 421 | 8 | 481 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6.86e-53 | 43 | 421 | 39 | 523 | Inulinase OS=Kluyveromyces marxianus OX=4911 GN=INU1 PE=1 SV=1 |
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1.68e-52 | 43 | 421 | 28 | 501 | Invertase 1 OS=Saccharomyces cerevisiae OX=4932 GN=SUC1 PE=1 SV=1 |
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3.25e-52 | 43 | 421 | 28 | 501 | Invertase 4 OS=Saccharomyces cerevisiae OX=4932 GN=SUC4 PE=3 SV=1 |
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8.67e-51 | 43 | 421 | 28 | 501 | Invertase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SUC2 PE=1 SV=1 |
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1.99e-50 | 36 | 421 | 76 | 547 | Invertase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=inv1 PE=1 SV=1 |
Other | SP_Sec_SPI | CS Position |
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0.474943 | 0.525040 | CS pos: 18-19. Pr: 0.5127 |
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