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CAZyme Information: MGYG000000135_03864
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Murimonas intestini | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Murimonas; Murimonas intestini | |||||||||||
| CAZyme ID | MGYG000000135_03864 | |||||||||||
| CAZy Family | GH32 | |||||||||||
| CAZyme Description | Sucrose-6-phosphate hydrolase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 11994; End: 13505 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH32 | 35 | 340 | 2.9e-47 | 0.9488054607508533 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd08996 | GH32_FFase | 2.38e-69 | 37 | 337 | 3 | 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 | 4.67e-51 | 39 | 463 | 11 | 436 | Glycosyl hydrolases family 32. |
| COG1621 | SacC | 3.06e-48 | 3 | 476 | 9 | 462 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
| pfam00251 | Glyco_hydro_32N | 3.17e-33 | 39 | 342 | 11 | 302 | 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 | 6.70e-31 | 38 | 337 | 5 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AZN41469.1 | 5.23e-165 | 1 | 503 | 1 | 518 |
| ARN56627.1 | 4.34e-161 | 4 | 503 | 265 | 772 |
| CDR30229.1 | 8.71e-117 | 17 | 503 | 17 | 506 |
| AWT60516.1 | 7.37e-61 | 15 | 499 | 21 | 508 |
| AMV40650.1 | 3.75e-51 | 24 | 472 | 247 | 700 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6NUM_A | 6.89e-35 | 19 | 472 | 36 | 485 | Thestructure of GH32 from Bifidobacteium adolescentis [Bifidobacterium adolescentis],6NUN_A Structure of GH32 hydrolase from Bifidobacterium adolescentis in complex with frutose [Bifidobacterium adolescentis] |
| 3PIG_A | 2.67e-32 | 19 | 462 | 36 | 474 | 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] |
| 7VCO_A | 6.79e-27 | 22 | 476 | 25 | 462 | ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara] |
| 6NU7_A | 4.14e-15 | 21 | 472 | 31 | 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] |
| 3KF3_A | 7.75e-15 | 23 | 407 | 10 | 398 | ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P16553 | 7.49e-29 | 24 | 491 | 25 | 469 | Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1 |
| P05656 | 5.30e-24 | 19 | 499 | 31 | 508 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
| B6DZD0 | 2.47e-23 | 22 | 472 | 61 | 551 | Fructan 1-exohydrolase OS=Triticum urartu OX=4572 GN=1-FEH PE=3 SV=1 |
| Q84PN8 | 4.42e-23 | 22 | 472 | 61 | 551 | Fructan 1-exohydrolase w1 OS=Triticum aestivum OX=4565 GN=1-FEHw1 PE=1 SV=1 |
| Q84LA1 | 3.35e-22 | 22 | 472 | 60 | 550 | Fructan 1-exohydrolase w2 OS=Triticum aestivum OX=4565 GN=1-FEHw2 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000069 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |