Species | ||||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; | |||||||||||
CAZyme ID | MGYG000001735_00470 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Levanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 76597; End: 78078 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 51 | 319 | 1.5e-35 | 0.9078498293515358 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08995 | GH32_EcAec43-like | 3.17e-79 | 47 | 326 | 1 | 281 | Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 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). GH32 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. |
cd08996 | GH32_FFase | 1.31e-30 | 51 | 319 | 9 | 280 | 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. |
pfam00251 | Glyco_hydro_32N | 3.04e-23 | 51 | 294 | 15 | 269 | 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. |
smart00640 | Glyco_32 | 4.29e-23 | 51 | 254 | 15 | 223 | Glycosyl hydrolases family 32. |
cd18609 | GH32-like | 4.66e-22 | 84 | 266 | 48 | 245 | Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that 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). 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 |
---|---|---|---|---|---|
QHT70636.1 | 7.95e-176 | 1 | 491 | 2 | 489 |
QUT19040.1 | 5.69e-163 | 18 | 491 | 20 | 491 |
ATP58653.1 | 8.34e-163 | 1 | 492 | 1 | 490 |
QEM10766.1 | 1.34e-158 | 1 | 492 | 1 | 489 |
AYL95637.1 | 5.99e-157 | 3 | 493 | 2 | 490 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7BWB_A | 8.33e-12 | 53 | 258 | 69 | 252 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
7BWC_A | 8.33e-12 | 53 | 258 | 69 | 252 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
6R3R_A | 1.53e-11 | 103 | 418 | 96 | 421 | Firstcrystal structure of endo-levanase BT1760 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron] |
3KF3_A | 2.69e-11 | 80 | 215 | 56 | 188 | ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
3KF5_A | 2.71e-11 | 80 | 215 | 59 | 191 | ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O33833 | 4.83e-09 | 76 | 335 | 42 | 299 | Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1 |
P16553 | 1.65e-08 | 53 | 334 | 44 | 333 | Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1 |
P92916 | 2.62e-08 | 51 | 235 | 89 | 272 | Bifunctional 6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferase OS=Allium cepa OX=4679 PE=1 SV=1 |
P07819 | 3.85e-08 | 74 | 224 | 66 | 206 | Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2 |
A1STJ9 | 3.97e-07 | 53 | 334 | 116 | 404 | Probable sucrose-6-phosphate hydrolase OS=Psychromonas ingrahamii (strain 37) OX=357804 GN=Ping_0974 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000401 | 0.998814 | 0.000214 | 0.000187 | 0.000181 | 0.000168 |
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