family 10 glycosylhydrolase [Escherichia coli]
Protein Classification
alpha-amylase family protein( domain architecture ID 1562432)
alpha-amylase family protein may catalyze the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| AmyAc_family super family | cl38930 | Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ... |
55-390 | 1.21e-152 | ||||||
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. The actual alignment was detected with superfamily member pfam02638: Pssm-ID: 476817 [Multi-domain] Cd Length: 311 Bit Score: 435.10 E-value: 1.21e-152
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| Name | Accession | Description | Interval | E-value | |||||||
| GHL10 | pfam02638 | Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins ... |
55-390 | 1.21e-152 | |||||||
Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,. Pssm-ID: 251441 [Multi-domain] Cd Length: 311 Bit Score: 435.10 E-value: 1.21e-152
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| YddW | COG1649 | Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]; |
35-436 | 2.76e-146 | |||||||
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]; Pssm-ID: 441255 [Multi-domain] Cd Length: 451 Bit Score: 424.12 E-value: 2.76e-146
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| GH36 | cd14791 | glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ... |
142-235 | 1.99e-09 | |||||||
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. Pssm-ID: 269892 [Multi-domain] Cd Length: 299 Bit Score: 58.39 E-value: 1.99e-09
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| malS | PRK09505 | alpha-amylase; Reviewed |
89-156 | 2.66e-03 | |||||||
alpha-amylase; Reviewed Pssm-ID: 236543 [Multi-domain] Cd Length: 683 Bit Score: 40.04 E-value: 2.66e-03
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| Name | Accession | Description | Interval | E-value | |||||||
| GHL10 | pfam02638 | Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins ... |
55-390 | 1.21e-152 | |||||||
Glycosyl hydrolase-like 10; This is family of bacterial glycosyl-hydrolase-like proteins falling into the family GHL10 as described above,. Pssm-ID: 251441 [Multi-domain] Cd Length: 311 Bit Score: 435.10 E-value: 1.21e-152
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| YddW | COG1649 | Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]; |
35-436 | 2.76e-146 | |||||||
Uncharacterized lipoprotein YddW, UPF0748 family [Function unknown]; Pssm-ID: 441255 [Multi-domain] Cd Length: 451 Bit Score: 424.12 E-value: 2.76e-146
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| GH36 | cd14791 | glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ... |
142-235 | 1.99e-09 | |||||||
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively. Pssm-ID: 269892 [Multi-domain] Cd Length: 299 Bit Score: 58.39 E-value: 1.99e-09
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| GalA | COG3345 | Alpha-galactosidase [Carbohydrate transport and metabolism]; |
147-236 | 2.30e-09 | |||||||
Alpha-galactosidase [Carbohydrate transport and metabolism]; Pssm-ID: 442574 [Multi-domain] Cd Length: 219 Bit Score: 57.29 E-value: 2.30e-09
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| Melibiase | pfam02065 | Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ... |
138-252 | 2.64e-07 | |||||||
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27. Pssm-ID: 307952 Cd Length: 347 Bit Score: 52.40 E-value: 2.64e-07
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| AmyA | COG0366 | Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; |
91-164 | 8.32e-07 | |||||||
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440135 [Multi-domain] Cd Length: 413 Bit Score: 51.02 E-value: 8.32e-07
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| AmyAc_family | cd00551 | Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ... |
89-156 | 2.21e-04 | |||||||
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: 42.93 E-value: 2.21e-04
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| AmyAc_SI_OligoGlu_DGase | cd11333 | Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ... |
92-164 | 5.30e-04 | |||||||
Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins; The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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: 200472 [Multi-domain] Cd Length: 428 Bit Score: 42.06 E-value: 5.30e-04
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| AmyAc_2 | cd11348 | Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ... |
89-160 | 8.84e-04 | |||||||
Alpha amylase catalytic domain found in an uncharacterized protein 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; 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 catalytic triad (DED) is not present here. 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: 200486 [Multi-domain] Cd Length: 429 Bit Score: 41.52 E-value: 8.84e-04
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| AmyAc_TreS | cd11334 | Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ... |
92-164 | 1.17e-03 | |||||||
Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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: 200473 [Multi-domain] Cd Length: 447 Bit Score: 41.01 E-value: 1.17e-03
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| Alpha-amylase | pfam00128 | Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ... |
89-171 | 1.76e-03 | |||||||
Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain. Pssm-ID: 395077 [Multi-domain] Cd Length: 334 Bit Score: 40.42 E-value: 1.76e-03
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| GHL6 | pfam14871 | Hypothetical glycosyl hydrolase 6; GHL6 is a family of hypothetical glycoside hydrolases. |
95-235 | 1.88e-03 | |||||||
Hypothetical glycosyl hydrolase 6; GHL6 is a family of hypothetical glycoside hydrolases. Pssm-ID: 405546 [Multi-domain] Cd Length: 135 Bit Score: 38.54 E-value: 1.88e-03
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| malS | PRK09505 | alpha-amylase; Reviewed |
89-156 | 2.66e-03 | |||||||
alpha-amylase; Reviewed Pssm-ID: 236543 [Multi-domain] Cd Length: 683 Bit Score: 40.04 E-value: 2.66e-03
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| AmyAc_bac2_AmyA | cd11316 | Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ... |
89-164 | 6.96e-03 | |||||||
Alpha amylase catalytic domain found in bacterial 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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: 200455 [Multi-domain] Cd Length: 403 Bit Score: 38.72 E-value: 6.96e-03
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| Blast search parameters | ||||
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