Species | UBA5446 sp900544295 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; UBA5446; UBA5446 sp900544295 | |||||||||||
CAZyme ID | MGYG000002152_00946 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Beta-fructosidase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 19313; End: 20761 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 37 | 353 | 9.9e-51 | 0.9931740614334471 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08996 | GH32_FFase | 5.15e-75 | 44 | 343 | 2 | 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. |
COG1621 | SacC | 7.07e-49 | 27 | 442 | 23 | 450 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
smart00640 | Glyco_32 | 2.92e-48 | 44 | 439 | 8 | 435 | Glycosyl hydrolases family 32. |
pfam00251 | Glyco_hydro_32N | 3.15e-47 | 37 | 353 | 1 | 307 | 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. |
cd18625 | GH32_BfrA-like | 1.17e-36 | 43 | 343 | 1 | 286 | glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414). This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that 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. 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. 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 |
---|---|---|---|---|---|
QWA13129.1 | 5.67e-123 | 26 | 477 | 22 | 488 |
AQT68938.1 | 2.14e-90 | 30 | 437 | 195 | 593 |
QDV38482.1 | 1.25e-68 | 5 | 473 | 179 | 645 |
AIE86119.1 | 5.43e-67 | 26 | 474 | 42 | 466 |
QHW33171.1 | 1.26e-64 | 33 | 472 | 6 | 454 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UYP_A | 6.33e-37 | 33 | 469 | 3 | 431 | Thethree-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8] |
1W2T_A | 1.65e-36 | 33 | 469 | 3 | 431 | beta-fructosidasefrom Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_B beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_C beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_D beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_E beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_F beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8] |
7BWB_A | 8.71e-28 | 8 | 444 | 22 | 454 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori] |
7BWC_A | 9.84e-27 | 8 | 444 | 22 | 454 | Bombyxmori GH32 beta-fructofuranosidase BmSUC1 mutant D63A in complex with sucrose [Bombyx mori] |
2AC1_A | 5.06e-25 | 27 | 378 | 3 | 358 | Crystalstructure of a cell-wall invertase from Arabidopsis thaliana [Arabidopsis thaliana] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O33833 | 1.32e-36 | 33 | 469 | 3 | 431 | Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1 |
P49174 | 1.80e-25 | 33 | 365 | 54 | 388 | Beta-fructofuranosidase, cell wall isozyme OS=Zea mays OX=4577 PE=2 SV=1 |
Q67XZ3 | 1.93e-24 | 22 | 362 | 28 | 373 | Beta-fructofuranosidase, insoluble isoenzyme CWINV3 OS=Arabidopsis thaliana OX=3702 GN=CWINV3 PE=1 SV=2 |
Q43866 | 3.35e-24 | 27 | 378 | 46 | 401 | Beta-fructofuranosidase, insoluble isoenzyme CWINV1 OS=Arabidopsis thaliana OX=3702 GN=CWINV1 PE=1 SV=1 |
Q70XE6 | 9.13e-22 | 30 | 382 | 53 | 409 | Fructan 6-exohydrolase OS=Beta vulgaris OX=161934 GN=6-FEH PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000065 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.