Species | Claviceps purpurea | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Clavicipitaceae; Claviceps; Claviceps purpurea | |||||||||||
CAZyme ID | CCE27817.1 | |||||||||||
CAZy Family | CE5 | |||||||||||
CAZyme Description | Related to SUC2-invertase (Sucrose hydrolyzing enzyme) [Source:UniProtKB/TrEMBL;Acc:M1VUI2] | |||||||||||
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 | 39 | 348 | 3.5e-83 | 0.9761092150170648 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
350134 | GH32_Inu-like | 6.33e-126 | 44 | 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 | 1.30e-101 | 30 | 517 | 24 | 479 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
214757 | Glyco_32 | 8.72e-93 | 39 | 487 | 1 | 437 | Glycosyl hydrolases family 32. |
395193 | Glyco_hydro_32N | 1.32e-79 | 39 | 357 | 1 | 308 | 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 | 8.13e-63 | 45 | 339 | 1 | 278 | 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 |
---|---|---|---|---|---|
5.33e-255 | 1 | 544 | 1 | 551 | |
4.55e-241 | 2 | 541 | 11 | 555 | |
2.79e-234 | 23 | 543 | 44 | 563 | |
6.21e-234 | 1 | 543 | 5 | 557 | |
7.99e-232 | 26 | 543 | 41 | 556 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2.70e-94 | 35 | 499 | 10 | 479 | Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
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2.94e-94 | 35 | 499 | 13 | 482 | Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
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3.82e-93 | 20 | 496 | 24 | 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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4.30e-93 | 35 | 499 | 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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8.51e-93 | 35 | 499 | 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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4.07e-94 | 35 | 496 | 20 | 479 | Extracellular exo-inulinase OS=Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) OX=294746 GN=PGUG_02777 PE=1 SV=2 |
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8.07e-94 | 35 | 496 | 20 | 479 | Extracellular exo-inulinase inuE OS=Meyerozyma guilliermondii OX=4929 PE=1 SV=3 |
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6.89e-93 | 20 | 496 | 24 | 523 | Inulinase OS=Kluyveromyces marxianus OX=4911 GN=INU1 PE=1 SV=1 |
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1.68e-92 | 34 | 499 | 27 | 519 | Invertase OS=Wickerhamomyces anomalus OX=4927 GN=INV1 PE=3 SV=1 |
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4.79e-89 | 18 | 496 | 60 | 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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0.000262 | 0.999709 | CS pos: 15-16. Pr: 0.9805 |
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