Species | Paenibacillus polymyxa | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus polymyxa | |||||||||||
CAZyme ID | MGYG000003687_04974 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 26014; End: 27579 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH32 | 171 | 493 | 3.7e-70 | 0.9863481228668942 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd08996 | GH32_FFase | 5.06e-100 | 177 | 481 | 1 | 276 | 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 | 7.46e-93 | 171 | 503 | 1 | 318 | Glycosyl hydrolases family 32. |
pfam00251 | Glyco_hydro_32N | 5.40e-70 | 171 | 496 | 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. |
COG1621 | SacC | 8.40e-57 | 164 | 503 | 26 | 343 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]. |
cd18622 | GH32_Inu-like | 4.54e-53 | 176 | 486 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCC85374.1 | 0.0 | 1 | 514 | 504 | 1017 |
ADO56681.1 | 0.0 | 1 | 514 | 491 | 1004 |
AAL82574.1 | 0.0 | 1 | 514 | 491 | 1004 |
QDY82655.1 | 0.0 | 1 | 514 | 491 | 1004 |
AOK92850.1 | 0.0 | 1 | 514 | 491 | 1004 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2QQU_A | 4.92e-49 | 166 | 515 | 4 | 350 | ChainA, Beta-fructofuranosidase [Arabidopsis thaliana] |
2XQR_A | 5.09e-49 | 166 | 515 | 4 | 350 | Crystalstructure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_C Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_E Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_G Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_I Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana],2XQR_K Crystal structure of plant cell wall invertase in complex with a specific protein inhibitor [Arabidopsis thaliana] |
2AC1_A | 5.45e-49 | 166 | 515 | 8 | 354 | Crystalstructure of a cell-wall invertase from Arabidopsis thaliana [Arabidopsis thaliana] |
2OXB_A | 1.35e-48 | 166 | 515 | 4 | 350 | ChainA, Beta-fructofuranosidase [Arabidopsis thaliana] |
2QQW_A | 1.35e-48 | 166 | 515 | 4 | 350 | ChainA, Beta-fructofuranosidase [Arabidopsis thaliana] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q1PEF8 | 1.87e-49 | 166 | 507 | 47 | 382 | Beta-fructofuranosidase, insoluble isoenzyme CWINV2 OS=Arabidopsis thaliana OX=3702 GN=CWINV2 PE=2 SV=1 |
Q43866 | 5.91e-48 | 166 | 515 | 51 | 397 | Beta-fructofuranosidase, insoluble isoenzyme CWINV1 OS=Arabidopsis thaliana OX=3702 GN=CWINV1 PE=1 SV=1 |
B6DZD2 | 1.74e-46 | 143 | 503 | 37 | 389 | Fructan 1-exohydrolase OS=Aegilops tauschii OX=37682 GN=1-FEH PE=3 SV=1 |
Q8W413 | 8.02e-46 | 166 | 505 | 49 | 381 | Beta-fructofuranosidase, insoluble isoenzyme CWINV4 OS=Arabidopsis thaliana OX=3702 GN=CWINV4 PE=2 SV=1 |
Q8W4S6 | 1.15e-45 | 166 | 507 | 16 | 352 | Beta-fructofuranosidase, insoluble isoenzyme CWINV6 OS=Arabidopsis thaliana OX=3702 GN=CWINV6 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000042 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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