MULTISPECIES: sucrose-6-phosphate hydrolase [Staphylococcus]
Protein Classification
sucrose-6-phosphate hydrolase( domain architecture ID 1003399)
sucrose-6-phosphate hydrolase catalyzes the hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| scrB_fam super family | cl36871 | sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of ... |
22-464 | 0e+00 | |||||||
sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of polysaccharides] The actual alignment was detected with superfamily member TIGR01322: Pssm-ID: 273554 [Multi-domain] Cd Length: 445 Bit Score: 625.95 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||
| scrB_fam | TIGR01322 | sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of ... |
22-464 | 0e+00 | |||||||
sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of polysaccharides] Pssm-ID: 273554 [Multi-domain] Cd Length: 445 Bit Score: 625.95 E-value: 0e+00
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| SacC | COG1621 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]; |
29-490 | 0e+00 | |||||||
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]; Pssm-ID: 441228 [Multi-domain] Cd Length: 459 Bit Score: 587.27 E-value: 0e+00
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| GH32_ScrB-like | cd18623 | glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase ... |
44-331 | 3.25e-175 | |||||||
glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme 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. 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. 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. Pssm-ID: 350135 Cd Length: 289 Bit Score: 493.57 E-value: 3.25e-175
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| Glyco_32 | smart00640 | Glycosyl hydrolases family 32; |
38-454 | 5.63e-147 | |||||||
Glycosyl hydrolases family 32; Pssm-ID: 214757 [Multi-domain] Cd Length: 437 Bit Score: 427.51 E-value: 5.63e-147
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| Glyco_hydro_32N | pfam00251 | Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal ... |
38-338 | 6.12e-140 | |||||||
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. Pssm-ID: 425557 Cd Length: 308 Bit Score: 404.71 E-value: 6.12e-140
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| beta-fruc_BfrA | NF041092 | beta-fructosidase; |
33-464 | 5.60e-62 | |||||||
beta-fructosidase; Pssm-ID: 469018 [Multi-domain] Cd Length: 433 Bit Score: 208.60 E-value: 5.60e-62
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| Name | Accession | Description | Interval | E-value | |||||||
| scrB_fam | TIGR01322 | sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of ... |
22-464 | 0e+00 | |||||||
sucrose-6-phosphate hydrolase; [Energy metabolism, Biosynthesis and degradation of polysaccharides] Pssm-ID: 273554 [Multi-domain] Cd Length: 445 Bit Score: 625.95 E-value: 0e+00
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| SacC | COG1621 | Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]; |
29-490 | 0e+00 | |||||||
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism]; Pssm-ID: 441228 [Multi-domain] Cd Length: 459 Bit Score: 587.27 E-value: 0e+00
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| GH32_ScrB-like | cd18623 | glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase ... |
44-331 | 3.25e-175 | |||||||
glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase); Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme 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. 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. 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. Pssm-ID: 350135 Cd Length: 289 Bit Score: 493.57 E-value: 3.25e-175
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| Glyco_32 | smart00640 | Glycosyl hydrolases family 32; |
38-454 | 5.63e-147 | |||||||
Glycosyl hydrolases family 32; Pssm-ID: 214757 [Multi-domain] Cd Length: 437 Bit Score: 427.51 E-value: 5.63e-147
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| Glyco_hydro_32N | pfam00251 | Glycosyl hydrolases family 32 N-terminal domain; This domain corresponds to the N-terminal ... |
38-338 | 6.12e-140 | |||||||
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. Pssm-ID: 425557 Cd Length: 308 Bit Score: 404.71 E-value: 6.12e-140
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| GH32_FFase | cd08996 | Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves ... |
44-327 | 6.07e-102 | |||||||
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. Pssm-ID: 350110 Cd Length: 281 Bit Score: 306.87 E-value: 6.07e-102
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| beta-fruc_BfrA | NF041092 | beta-fructosidase; |
33-464 | 5.60e-62 | |||||||
beta-fructosidase; Pssm-ID: 469018 [Multi-domain] Cd Length: 433 Bit Score: 208.60 E-value: 5.60e-62
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| GH32_BfrA-like | cd18625 | glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414); ... |
44-329 | 1.97e-54 | |||||||
glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414); This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that 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. 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. 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. Pssm-ID: 350137 Cd Length: 286 Bit Score: 184.03 E-value: 1.97e-54
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| GH32_Inu-like | cd18622 | glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2); This ... |
43-327 | 1.53e-47 | |||||||
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. Pssm-ID: 350134 Cd Length: 289 Bit Score: 166.25 E-value: 1.53e-47
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| GH32_Fruct1-like | cd18624 | glycoside hydrolase family 32 protein such as Arabidopsis thaliana cell-wall invertase 1 ... |
44-327 | 3.74e-39 | |||||||
glycoside hydrolase family 32 protein such as Arabidopsis thaliana cell-wall invertase 1 (AtBFruct1;Fruct1;AtcwINV1;At3g13790); This subfamily of glycosyl hydrolase family GH32 includes fructan beta-(2,1)-fructosidase and fructan 1-exohydrolase IIa (1-FEH IIa, EC 3.2.1.153), cell-wall invertase 1 (EC 3.2.1.26), sucrose:fructan 6-fructosyltransferase (6-Sst/6-Dft, EC 2.4.1.10), and levan fructosyltransferases (EC 2.4.1.-) among others. This enzyme 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. 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. 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. Pssm-ID: 350136 [Multi-domain] Cd Length: 296 Bit Score: 143.68 E-value: 3.74e-39
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| GH32_XdINV-like | cd18621 | glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous ... |
44-327 | 4.40e-37 | |||||||
glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV); This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), 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. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. 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. Pssm-ID: 350133 Cd Length: 337 Bit Score: 139.30 E-value: 4.40e-37
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| Glyco_hydro_32C | pfam08244 | Glycosyl hydrolases family 32 C terminal; This domain corresponds to the C terminal domain of ... |
342-480 | 2.46e-24 | |||||||
Glycosyl hydrolases family 32 C terminal; This domain corresponds to the C terminal domain of glycosyl hydrolase family 32. It forms a beta sandwich module. Pssm-ID: 462408 [Multi-domain] Cd Length: 162 Bit Score: 98.96 E-value: 2.46e-24
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| GH_J | cd08979 | Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase ... |
47-328 | 1.05e-23 | |||||||
Glycosyl hydrolase families 32 and 68, which form the clan GH-J; This glycosyl hydrolase family clan J (according to carbohydrate-active enzymes database (CAZY)) includes family 32 (GH32) and 68 (GH68). GH32 enzymes include invertase (EC 3.2.1.26) and other 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.-). The GH68 family consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10, also known as beta-D-fructofuranosyl transferase), beta-fructofuranosidase (EC 3.2.1.26) and inulosucrase (EC 2.4.1.9). GH32 and GH68 family enzymes are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) and 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. 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. Pssm-ID: 350093 [Multi-domain] Cd Length: 292 Bit Score: 100.72 E-value: 1.05e-23
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| GH32_EcAec43-like | cd08995 | Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 ... |
53-334 | 1.48e-21 | |||||||
Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2); This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 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). GH32 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. Pssm-ID: 350109 [Multi-domain] Cd Length: 281 Bit Score: 94.56 E-value: 1.48e-21
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| GH43_62_32_68_117_130 | cd08772 | Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ... |
47-303 | 2.64e-11 | |||||||
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that 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. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans. Pssm-ID: 350091 [Multi-domain] Cd Length: 257 Bit Score: 63.77 E-value: 2.64e-11
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| GH43_HoAraf43-like | cd08991 | Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ... |
53-135 | 2.74e-05 | |||||||
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. Pssm-ID: 350105 [Multi-domain] Cd Length: 283 Bit Score: 46.01 E-value: 2.74e-05
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| GH43_62_32_68_117_130-like | cd08994 | Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ... |
53-207 | 3.46e-05 | |||||||
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that 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. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans. Pssm-ID: 350108 [Multi-domain] Cd Length: 294 Bit Score: 45.72 E-value: 3.46e-05
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| GH32-like | cd18609 | Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase ... |
81-239 | 5.27e-05 | |||||||
Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase family GH32 proteins that 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). 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. Pssm-ID: 350121 Cd Length: 303 Bit Score: 45.32 E-value: 5.27e-05
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| GH43_AXH_like | cd08990 | Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, ... |
48-251 | 8.67e-05 | |||||||
Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase; This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. Pssm-ID: 350104 [Multi-domain] Cd Length: 269 Bit Score: 44.13 E-value: 8.67e-05
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| XynB2 | COG3507 | Beta-xylosidase [Carbohydrate transport and metabolism]; |
57-134 | 1.39e-04 | |||||||
Beta-xylosidase [Carbohydrate transport and metabolism]; Pssm-ID: 442730 [Multi-domain] Cd Length: 351 Bit Score: 44.17 E-value: 1.39e-04
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| GH43_Xsa43E-like | cd18618 | Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase ... |
77-132 | 1.66e-03 | |||||||
Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E; This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. Pssm-ID: 350130 [Multi-domain] Cd Length: 275 Bit Score: 40.28 E-value: 1.66e-03
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| GH43_bXyl-like | cd09004 | Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ... |
48-122 | 7.61e-03 | |||||||
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases; This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain 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. Pssm-ID: 350118 [Multi-domain] Cd Length: 266 Bit Score: 38.36 E-value: 7.61e-03
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