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CAZyme Information: MGYG000003687_01379
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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 | Paenibacillus polymyxa | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa | |||||||||||
| CAZyme ID | MGYG000003687_01379 | |||||||||||
| CAZy Family | GH32 | |||||||||||
| CAZyme Description | Levanase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 186855; End: 188312 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH32 | 14 | 330 | 3.5e-105 | 0.9965870307167235 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd18622 | GH32_Inu-like | 2.44e-164 | 20 | 317 | 2 | 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. |
| COG1621 | SacC | 1.04e-158 | 4 | 485 | 23 | 485 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
| smart00640 | Glyco_32 | 1.58e-151 | 14 | 448 | 1 | 437 | Glycosyl hydrolases family 32. |
| pfam00251 | Glyco_hydro_32N | 3.55e-133 | 14 | 330 | 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. |
| cd08996 | GH32_FFase | 4.58e-96 | 20 | 317 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AHN08014.1 | 0.0 | 1 | 485 | 1 | 485 |
| QPK56956.1 | 0.0 | 1 | 485 | 1 | 485 |
| QPK51873.1 | 0.0 | 1 | 485 | 1 | 485 |
| QDA25999.1 | 0.0 | 1 | 485 | 1 | 485 |
| AHM64698.1 | 0.0 | 1 | 485 | 1 | 485 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1Y4W_A | 3.88e-105 | 7 | 462 | 5 | 491 | Crystalstructure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori] |
| 3RWK_X | 1.97e-83 | 4 | 467 | 23 | 496 | Firstcrystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum] |
| 3KF3_A | 2.50e-73 | 1 | 331 | 1 | 330 | ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
| 3KF5_A | 2.69e-73 | 1 | 331 | 4 | 333 | ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
| 3U75_A | 3.54e-72 | 1 | 331 | 27 | 356 | ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P05656 | 1.11e-167 | 7 | 485 | 32 | 510 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
| O31411 | 3.71e-110 | 7 | 485 | 395 | 876 | Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2 |
| A2R0E0 | 9.27e-105 | 7 | 476 | 24 | 527 | Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1 |
| E1ABX2 | 3.67e-104 | 7 | 476 | 24 | 527 | Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1 |
| Q76HP6 | 3.67e-104 | 7 | 476 | 24 | 527 | Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE 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 |
|---|---|---|---|---|---|
| 1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |