Species | Paenibacillus polymyxa | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa | |||||||||||
CAZyme ID | MGYG000003687_04977 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | 5-dehydro-2-deoxygluconokinase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 31493; End: 33976 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 332 | 645 | 1e-102 | 0.9897610921501706 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd18622 | GH32_Inu-like | 3.64e-162 | 337 | 634 | 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. |
COG1621 | SacC | 2.01e-147 | 309 | 797 | 9 | 479 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
smart00640 | Glyco_32 | 1.43e-143 | 332 | 767 | 1 | 437 | Glycosyl hydrolases family 32. |
pfam00251 | Glyco_hydro_32N | 7.06e-118 | 332 | 647 | 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. |
cd01167 | bac_FRK | 3.66e-105 | 4 | 302 | 2 | 294 | Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AHM66125.1 | 0.0 | 1 | 827 | 1 | 827 |
AIY07082.1 | 0.0 | 1 | 827 | 1 | 827 |
AUS26717.1 | 0.0 | 1 | 827 | 1 | 827 |
ADO56683.1 | 0.0 | 1 | 816 | 1 | 816 |
CCC85376.1 | 0.0 | 1 | 816 | 1 | 816 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1Y4W_A | 3.04e-100 | 324 | 791 | 4 | 501 | 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 | 7.62e-84 | 327 | 797 | 28 | 507 | 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 | 6.92e-75 | 328 | 776 | 10 | 476 | ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis] |
3KF5_A | 7.47e-75 | 328 | 776 | 13 | 479 | ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis] |
3U75_A | 9.47e-74 | 328 | 776 | 36 | 502 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P05656 | 7.87e-161 | 324 | 806 | 31 | 512 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
O31411 | 2.62e-113 | 325 | 806 | 395 | 878 | Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2 |
Q96TU3 | 2.87e-99 | 324 | 791 | 23 | 520 | Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1 |
E1ABX2 | 1.10e-98 | 324 | 777 | 23 | 506 | Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1 |
Q76HP6 | 1.10e-98 | 324 | 777 | 23 | 506 | Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000088 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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