Species | RF16 sp900766775 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae; RF16; RF16 sp900766775 | |||||||||||
CAZyme ID | MGYG000003419_01144 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 3368; End: 5854 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 277 | 577 | 4.6e-55 | 0.9965870307167235 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08996 | GH32_FFase | 1.35e-76 | 283 | 567 | 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. |
smart00640 | Glyco_32 | 2.47e-66 | 277 | 703 | 1 | 436 | Glycosyl hydrolases family 32. |
COG1621 | SacC | 6.27e-57 | 267 | 731 | 23 | 476 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
pfam00251 | Glyco_hydro_32N | 4.43e-46 | 277 | 577 | 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. |
cd18622 | GH32_Inu-like | 4.65e-33 | 282 | 567 | 1 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUB90817.1 | 3.12e-191 | 15 | 762 | 289 | 1011 |
AXV49252.1 | 7.44e-191 | 15 | 762 | 308 | 1030 |
QUB92629.1 | 6.35e-187 | 56 | 762 | 30 | 720 |
AEA21196.1 | 7.12e-186 | 56 | 762 | 30 | 720 |
QUB89002.1 | 7.12e-186 | 56 | 762 | 30 | 720 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7VCO_A | 2.81e-34 | 274 | 732 | 27 | 477 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
6NU7_A | 1.73e-24 | 276 | 712 | 36 | 462 | Structureof sucrose-6-phosphate hydrolase from Lactobacillus gasseri [Lactobacillus gasseri 224-1],6NU8_A Structure of sucrose-6-phosphate hydrolase from Lactobacillus gasseri in complex with fructose [Lactobacillus gasseri 224-1] |
3UGF_A | 7.94e-22 | 273 | 727 | 19 | 520 | Crystalstructure of a 6-SST/6-SFT from Pachysandra terminalis [Pachysandra terminalis],3UGF_B Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis [Pachysandra terminalis],3UGG_A Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 1-kestose [Pachysandra terminalis],3UGG_B Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 1-kestose [Pachysandra terminalis],3UGH_A Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 6-kestose [Pachysandra terminalis],3UGH_B Crystal structure of a 6-SST/6-SFT from Pachysandra terminalis in complex with 6-kestose [Pachysandra terminalis] |
7BWB_A | 9.49e-20 | 273 | 586 | 49 | 358 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
7BWC_A | 2.23e-19 | 273 | 586 | 49 | 358 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P16553 | 5.17e-34 | 274 | 730 | 25 | 465 | Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1 |
P40714 | 7.06e-34 | 274 | 741 | 26 | 477 | Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1 |
P05656 | 5.08e-31 | 266 | 748 | 28 | 517 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
P0DJA7 | 1.10e-27 | 274 | 713 | 30 | 473 | Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1 |
F8DVG5 | 4.69e-27 | 274 | 713 | 30 | 473 | Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1) OX=555217 GN=sacA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000316 | 0.999028 | 0.000178 | 0.000156 | 0.000142 | 0.000140 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.