putative GTFB [Lactobacillus delbrueckii]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| Glyco_hydro_70 super family | cl27864 | Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ... |
2-579 | 3.51e-148 | |||||||||
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain. The actual alignment was detected with superfamily member pfam02324: Pssm-ID: 426720 [Multi-domain] Cd Length: 831 Bit Score: 449.51 E-value: 3.51e-148
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| Name | Accession | Description | Interval | E-value | |||||||||
| Glyco_hydro_70 | pfam02324 | Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ... |
2-579 | 3.51e-148 | |||||||||
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain. Pssm-ID: 426720 [Multi-domain] Cd Length: 831 Bit Score: 449.51 E-value: 3.51e-148
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| AmyAc_arch_bac_plant_AmyA | cd11314 | Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ... |
369-453 | 3.18e-16 | |||||||||
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Pssm-ID: 200453 [Multi-domain] Cd Length: 302 Bit Score: 79.57 E-value: 3.18e-16
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| PRK09441 | PRK09441 | cytoplasmic alpha-amylase; Reviewed |
369-466 | 1.53e-14 | |||||||||
cytoplasmic alpha-amylase; Reviewed Pssm-ID: 236518 [Multi-domain] Cd Length: 479 Bit Score: 76.47 E-value: 1.53e-14
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| Aamy | smart00642 | Alpha-amylase domain; |
372-451 | 3.39e-07 | |||||||||
Alpha-amylase domain; Pssm-ID: 214758 [Multi-domain] Cd Length: 166 Bit Score: 50.41 E-value: 3.39e-07
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| AmyA | COG0366 | Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; |
381-449 | 6.89e-04 | |||||||||
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440135 [Multi-domain] Cd Length: 413 Bit Score: 42.54 E-value: 6.89e-04
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| Name | Accession | Description | Interval | E-value | |||||||||
| Glyco_hydro_70 | pfam02324 | Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 ... |
2-579 | 3.51e-148 | |||||||||
Glycosyl hydrolase family 70; Members of this family belong to glycosyl hydrolase family 70 Glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) catalyze the transfer of D-glucopyramnosyl units from sucrose onto acceptor molecules, EC:2.4.1.5. This family roughly corresponds to the N-terminal catalytic domain of the enzyme. Members of this family also contain the Putative cell wall binding domain pfam01473, which corresponds with the C-terminal glucan-binding domain. Pssm-ID: 426720 [Multi-domain] Cd Length: 831 Bit Score: 449.51 E-value: 3.51e-148
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| AmyAc_arch_bac_plant_AmyA | cd11314 | Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ... |
369-453 | 3.18e-16 | |||||||||
Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Pssm-ID: 200453 [Multi-domain] Cd Length: 302 Bit Score: 79.57 E-value: 3.18e-16
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| AmyAc_bac_fung_AmyA | cd11318 | Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ... |
369-472 | 4.99e-15 | |||||||||
Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase); AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Pssm-ID: 200457 [Multi-domain] Cd Length: 391 Bit Score: 77.17 E-value: 4.99e-15
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| PRK09441 | PRK09441 | cytoplasmic alpha-amylase; Reviewed |
369-466 | 1.53e-14 | |||||||||
cytoplasmic alpha-amylase; Reviewed Pssm-ID: 236518 [Multi-domain] Cd Length: 479 Bit Score: 76.47 E-value: 1.53e-14
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| PRK09441 | PRK09441 | cytoplasmic alpha-amylase; Reviewed |
145-315 | 1.12e-09 | |||||||||
cytoplasmic alpha-amylase; Reviewed Pssm-ID: 236518 [Multi-domain] Cd Length: 479 Bit Score: 61.06 E-value: 1.12e-09
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| Aamy | smart00642 | Alpha-amylase domain; |
372-451 | 3.39e-07 | |||||||||
Alpha-amylase domain; Pssm-ID: 214758 [Multi-domain] Cd Length: 166 Bit Score: 50.41 E-value: 3.39e-07
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| PLN02784 | PLN02784 | alpha-amylase |
369-460 | 3.47e-07 | |||||||||
alpha-amylase Pssm-ID: 215419 [Multi-domain] Cd Length: 894 Bit Score: 53.48 E-value: 3.47e-07
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| AmyAc_family | cd00551 | Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ... |
379-449 | 5.01e-06 | |||||||||
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Pssm-ID: 200451 [Multi-domain] Cd Length: 260 Bit Score: 48.32 E-value: 5.01e-06
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| PLN00196 | PLN00196 | alpha-amylase; Provisional |
383-478 | 1.16e-04 | |||||||||
alpha-amylase; Provisional Pssm-ID: 165762 [Multi-domain] Cd Length: 428 Bit Score: 44.91 E-value: 1.16e-04
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| AmyA | COG0366 | Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; |
381-449 | 6.89e-04 | |||||||||
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440135 [Multi-domain] Cd Length: 413 Bit Score: 42.54 E-value: 6.89e-04
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| AmyAc_bac_CMD_like_3 | cd11340 | Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ... |
380-449 | 2.38e-03 | |||||||||
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase. Pssm-ID: 200479 [Multi-domain] Cd Length: 407 Bit Score: 40.66 E-value: 2.38e-03
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| Blast search parameters | ||||
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