Species | Alistipes sp000434235 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp000434235 | |||||||||||
CAZyme ID | MGYG000004006_01272 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Levanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 225763; End: 227607 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 132 | 427 | 2.3e-88 | 0.9795221843003413 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18622 | GH32_Inu-like | 1.56e-148 | 138 | 421 | 2 | 289 | 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. |
smart00640 | Glyco_32 | 1.64e-119 | 132 | 514 | 1 | 397 | Glycosyl hydrolases family 32. |
COG1621 | SacC | 8.30e-108 | 127 | 608 | 28 | 484 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
pfam00251 | Glyco_hydro_32N | 7.50e-103 | 132 | 429 | 1 | 305 | 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. |
cd08996 | GH32_FFase | 3.48e-81 | 138 | 421 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQA29111.1 | 1.75e-198 | 26 | 608 | 35 | 601 |
QUT60630.1 | 1.75e-198 | 26 | 608 | 35 | 601 |
QUT35475.1 | 1.75e-198 | 26 | 608 | 35 | 601 |
QUT66770.1 | 2.48e-198 | 26 | 608 | 35 | 601 |
QPH59594.1 | 2.48e-198 | 26 | 608 | 35 | 601 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3RWK_X | 1.72e-75 | 127 | 597 | 28 | 502 | Firstcrystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum] |
1Y4W_A | 1.05e-72 | 124 | 583 | 4 | 488 | Crystalstructure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori] |
3KF3_A | 7.34e-67 | 128 | 581 | 10 | 476 | ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
3KF5_A | 7.88e-67 | 128 | 581 | 13 | 479 | ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
3U75_A | 9.75e-66 | 128 | 581 | 36 | 502 | ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P05656 | 1.01e-128 | 109 | 608 | 14 | 509 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
O94220 | 9.41e-75 | 127 | 597 | 28 | 502 | Extracellular endo-inulinase inu2 OS=Aspergillus ficuum OX=5058 GN=inu2 PE=1 SV=1 |
K0E681 | 1.08e-74 | 127 | 607 | 18 | 502 | Putative glycosyl hydrolase ecdF OS=Aspergillus rugulosus OX=41736 GN=ecdF PE=3 SV=1 |
O31411 | 2.59e-74 | 79 | 608 | 347 | 875 | Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2 |
O74641 | 3.60e-74 | 127 | 597 | 28 | 502 | Extracellular endo-inulinase inuA OS=Aspergillus niger OX=5061 GN=inuA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000438 | 0.998753 | 0.000207 | 0.000210 | 0.000193 | 0.000165 |
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