alpha-galactosidase catalyzes the hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
248-592
1.83e-140
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 pfam02065:
Pssm-ID: 476817 Cd Length: 347 Bit Score: 415.25 E-value: 1.83e-140
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many ...
22-239
2.85e-31
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
The actual alignment was detected with superfamily member pfam16875:
Pssm-ID: 465291 Cd Length: 255 Bit Score: 122.69 E-value: 2.85e-31
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
248-592
1.83e-140
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: 415.25 E-value: 1.83e-140
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
286-584
7.62e-134
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: 396.21 E-value: 7.62e-134
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many ...
22-239
2.85e-31
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
Pssm-ID: 465291 Cd Length: 255 Bit Score: 122.69 E-value: 2.85e-31
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
248-592
1.83e-140
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: 415.25 E-value: 1.83e-140
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
286-584
7.62e-134
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: 396.21 E-value: 7.62e-134
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many ...
22-239
2.85e-31
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many family 36 glycoside hydrolases. It has a beta-supersandwich fold.
Pssm-ID: 465291 Cd Length: 255 Bit Score: 122.69 E-value: 2.85e-31
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ...
288-372
6.11e-11
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 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. GH27 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: 269893 [Multi-domain] Cd Length: 271 Bit Score: 63.73 E-value: 6.11e-11
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
321-440
3.48e-09
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear envelope transmembrane protein. A member of the glycosyl hydrolase family 31 (GH31) , it has been shown to be required for myogenic differentiation of C2C12 cells. Related proteins are found in eukaryotes and prokaryotes. Enzymes of the GH31 family possess a wide range of different hydrolytic activities including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase and alpha-1,4-glucan lyase. All GH31 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.
Pssm-ID: 269878 [Multi-domain] Cd Length: 364 Bit Score: 59.15 E-value: 3.48e-09
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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