Species | Peribacillus simplex | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-1321; Peribacillus; Peribacillus simplex | |||||||||||
CAZyme ID | MGYG000000083_01844 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Levanbiose-producing levanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 580037; End: 581602 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 53 | 356 | 4.4e-76 | 0.9863481228668942 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1621 | SacC | 2.35e-152 | 44 | 519 | 24 | 486 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
cd18622 | GH32_Inu-like | 9.39e-135 | 60 | 348 | 3 | 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. |
smart00640 | Glyco_32 | 2.91e-106 | 53 | 481 | 1 | 437 | Glycosyl hydrolases family 32. |
pfam00251 | Glyco_hydro_32N | 3.77e-93 | 53 | 356 | 1 | 305 | 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 | 2.60e-53 | 60 | 348 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHZ49188.1 | 1.08e-297 | 43 | 521 | 43 | 521 |
AZV63824.1 | 5.73e-293 | 24 | 521 | 3 | 512 |
QGQ44167.1 | 1.89e-290 | 5 | 519 | 1 | 534 |
QYF85536.1 | 1.28e-289 | 19 | 521 | 3 | 512 |
AMM95539.1 | 3.48e-287 | 20 | 521 | 4 | 512 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4FFF_A | 3.02e-107 | 50 | 518 | 2 | 479 | CrystalStructure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_B Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_C Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_D Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens] |
4FFG_A | 3.20e-107 | 50 | 518 | 2 | 479 | CrystalStructure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_B Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_C Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_D Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens] |
4FFH_A | 1.79e-106 | 50 | 518 | 2 | 479 | CrystalStructure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_B Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_C Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_D Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFI_A Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_B Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_C Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_D Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens] |
1Y4W_A | 1.88e-60 | 45 | 505 | 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] |
4EQV_A | 4.43e-48 | 45 | 490 | 4 | 481 | Structureof Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_B Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_C Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_D Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_E Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_F Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_G Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_H Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O07003 | 5.02e-256 | 44 | 521 | 39 | 515 | Levanbiose-producing levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=levB PE=1 SV=1 |
P94469 | 1.39e-211 | 63 | 457 | 1 | 394 | Levanbiose-producing levanase (Fragment) OS=Geobacillus stearothermophilus OX=1422 GN=levB PE=1 SV=2 |
P05656 | 5.67e-78 | 45 | 520 | 31 | 512 | Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1 |
Q76HP6 | 3.65e-64 | 45 | 519 | 23 | 534 | Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1 |
E1ABX2 | 3.65e-64 | 45 | 519 | 23 | 534 | Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000029 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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