Species | CAG-110 sp000434635 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-110; CAG-110 sp000434635 | |||||||||||
CAZyme ID | MGYG000000743_01358 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Sucrose-6-phosphate hydrolase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 52497; End: 54053 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 42 | 356 | 4.6e-40 | 0.9590443686006825 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08996 | GH32_FFase | 2.58e-61 | 41 | 346 | 3 | 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. |
smart00640 | Glyco_32 | 7.10e-53 | 43 | 477 | 11 | 436 | Glycosyl hydrolases family 32. |
COG1621 | SacC | 1.33e-46 | 18 | 510 | 20 | 482 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
pfam00251 | Glyco_hydro_32N | 2.70e-36 | 43 | 358 | 11 | 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 | 2.05e-26 | 42 | 346 | 5 | 288 | 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 |
---|---|---|---|---|---|
AZN41469.1 | 1.23e-177 | 3 | 518 | 2 | 518 |
ARN56627.1 | 8.53e-177 | 18 | 518 | 275 | 772 |
CDR30229.1 | 3.99e-119 | 18 | 518 | 14 | 506 |
APW62066.1 | 2.30e-58 | 24 | 514 | 249 | 733 |
QSG13202.1 | 1.13e-51 | 18 | 512 | 247 | 712 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7VCO_A | 4.76e-31 | 22 | 512 | 21 | 485 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
3PIG_A | 1.41e-29 | 19 | 512 | 30 | 509 | beta-fructofuranosidasefrom Bifidobacterium longum [Bifidobacterium longum],3PIG_B beta-fructofuranosidase from Bifidobacterium longum [Bifidobacterium longum],3PIJ_A beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum],3PIJ_B beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum] |
2QQU_A | 3.33e-27 | 27 | 512 | 5 | 531 | ChainA, Beta-fructofuranosidase [Arabidopsis thaliana] |
1UYP_A | 1.08e-26 | 27 | 487 | 3 | 406 | 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 | 1.47e-26 | 27 | 487 | 3 | 406 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P16553 | 1.41e-29 | 28 | 497 | 25 | 459 | Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1 |
P27217 | 2.25e-27 | 22 | 515 | 22 | 463 | Sucrose-6-phosphate hydrolase OS=Klebsiella pneumoniae OX=573 GN=scrB PE=1 SV=3 |
P40714 | 2.82e-26 | 28 | 497 | 26 | 460 | Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1 |
Q43866 | 1.40e-25 | 27 | 512 | 52 | 578 | Beta-fructofuranosidase, insoluble isoenzyme CWINV1 OS=Arabidopsis thaliana OX=3702 GN=CWINV1 PE=1 SV=1 |
O33833 | 3.66e-25 | 27 | 487 | 3 | 406 | Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000048 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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