Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ...
300-647
3.88e-178
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: 513.86 E-value: 3.88e-178
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many ...
40-296
8.91e-47
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: 166.99 E-value: 8.91e-47
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
300-647
3.88e-178
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: 513.86 E-value: 3.88e-178
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
342-641
6.60e-124
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: 372.71 E-value: 6.60e-124
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many ...
40-296
8.91e-47
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: 166.99 E-value: 8.91e-47
Melibiase; Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan ...
300-647
3.88e-178
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: 513.86 E-value: 3.88e-178
glycosyl hydrolase family 36 (GH36); GH36 enzymes occur in prokaryotes, eukaryotes, and ...
342-641
6.60e-124
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: 372.71 E-value: 6.60e-124
Glycosyl hydrolase family 36 N-terminal domain; This domain is found at the N-terminus of many ...
40-296
8.91e-47
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: 166.99 E-value: 8.91e-47
glycosyl hydrolase family 27 (GH27); GH27 enzymes occur in eukaryotes, prokaryotes, and ...
348-427
6.61e-14
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: 72.59 E-value: 6.61e-14
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) ...
355-496
1.82e-10
alpha-xylosidase YicI-like; YicI alpha-xylosidase is a glycosyl hydrolase family 31 (GH31) enzyme that catalyzes the release of an alpha-xylosyl residue from the non-reducing end of alpha-xyloside substrates such as alpha-xylosyl fluoride and isoprimeverose. YicI forms a homohexamer (a trimer of dimers). 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. The YicI family corresponds to subgroup 4 in the Ernst et al classification of GH31 enzymes.
Pssm-ID: 269879 [Multi-domain] Cd Length: 308 Bit Score: 62.97 E-value: 1.82e-10
glucosidase NET37; NET37 (also known as KIAA1161) is a human lamina-associated nuclear ...
343-496
3.64e-10
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: 62.24 E-value: 3.64e-10
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of ...
343-447
1.73e-04
Glycoside hydrolases, clan D; This group of glycosyl hydrolase families is comprised of glycosyl hydrolase family 31 (GH31), family 36 (GH36), and family 27 (GH27). These structurally and mechanistically related protein families 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. They have a wide range of functions including alpha-glucosidase, alpha-xylosidase, 6-alpha-glucosyltransferase, 3-alpha-isomaltosyltransferase, alpha-N-acetylgalactosaminidase, stachyose synthase, raffinose synthase, and alpha-1,4-glucan lyase.
Pssm-ID: 269891 [Multi-domain] Cd Length: 253 Bit Score: 44.15 E-value: 1.73e-04
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in ...
378-495
6.23e-03
xylosidase XylS-like; XylS is a glycosyl hydrolase family 31 (GH31) alpha-xylosidase found in prokaryotes, eukaryotes, and archaea, that catalyzes the release of alpha-xylose from the non-reducing terminal side of the alpha-xyloside substrate. XylS has been characterized in Sulfolobus solfataricus where it hydrolyzes isoprimeverose, the p-nitrophenyl-beta derivative of isoprimeverose, and xyloglucan oligosaccharides, and has transxylosidic activity. 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. The XylS family corresponds to subgroup 3 in the Ernst et al classification of GH31 enzymes.
Pssm-ID: 269877 [Multi-domain] Cd Length: 322 Bit Score: 39.46 E-value: 6.23e-03
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.
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