cyclodextrin glucanotransferase [Geobacillus stearothermophilus]
Protein Classification
AmyAc_AmyMalt_CGTase_like and IPT_CGTD domain-containing protein( domain architecture ID 10183104)
protein containing domains AmyAc_AmyMalt_CGTase_like, Aamy_C, IPT_CGTD, and CBM20
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| AmyAc_AmyMalt_CGTase_like | cd11320 | Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ... |
39-427 | 0e+00 | ||||||
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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: 200459 [Multi-domain] Cd Length: 389 Bit Score: 606.59 E-value: 0e+00
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| CBM20 super family | cl15347 | The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ... |
609-709 | 6.97e-53 | ||||||
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. The actual alignment was detected with superfamily member cd05807: Pssm-ID: 449530 [Multi-domain] Cd Length: 101 Bit Score: 177.75 E-value: 6.97e-53
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| IPT_CGTD | cd00604 | IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ... |
526-607 | 7.90e-32 | ||||||
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown. : Pssm-ID: 238338 [Multi-domain] Cd Length: 81 Bit Score: 118.22 E-value: 7.90e-32
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| Aamy_C | smart00632 | Aamy_C domain; |
437-521 | 1.40e-16 | ||||||
Aamy_C domain; : Pssm-ID: 214749 Cd Length: 81 Bit Score: 74.97 E-value: 1.40e-16
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| Name | Accession | Description | Interval | E-value | ||||||||
| AmyAc_AmyMalt_CGTase_like | cd11320 | Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ... |
39-427 | 0e+00 | ||||||||
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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: 200459 [Multi-domain] Cd Length: 389 Bit Score: 606.59 E-value: 0e+00
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| Alpha-amylase | pfam00128 | Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ... |
80-399 | 3.31e-85 | ||||||||
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: 271.92 E-value: 3.31e-85
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| AmyA | COG0366 | Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; |
43-402 | 7.99e-77 | ||||||||
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440135 [Multi-domain] Cd Length: 413 Bit Score: 252.48 E-value: 7.99e-77
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| CBM20_CGTase | cd05807 | CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ... |
609-709 | 6.97e-53 | ||||||||
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99882 [Multi-domain] Cd Length: 101 Bit Score: 177.75 E-value: 6.97e-53
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| Aamy | smart00642 | Alpha-amylase domain; |
47-170 | 1.95e-38 | ||||||||
Alpha-amylase domain; Pssm-ID: 214758 [Multi-domain] Cd Length: 166 Bit Score: 140.16 E-value: 1.95e-38
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| PRK10785 | PRK10785 | maltodextrin glucosidase; Provisional |
44-464 | 8.66e-34 | ||||||||
maltodextrin glucosidase; Provisional Pssm-ID: 236759 [Multi-domain] Cd Length: 598 Bit Score: 137.06 E-value: 8.66e-34
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| IPT_CGTD | cd00604 | IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ... |
526-607 | 7.90e-32 | ||||||||
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown. Pssm-ID: 238338 [Multi-domain] Cd Length: 81 Bit Score: 118.22 E-value: 7.90e-32
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| CBM_20 | pfam00686 | Starch binding domain; |
611-695 | 3.23e-31 | ||||||||
Starch binding domain; Pssm-ID: 425821 [Multi-domain] Cd Length: 95 Bit Score: 117.00 E-value: 3.23e-31
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| CBM_2 | smart01065 | Starch binding domain; |
611-695 | 2.02e-25 | ||||||||
Starch binding domain; Pssm-ID: 215006 [Multi-domain] Cd Length: 88 Bit Score: 100.50 E-value: 2.02e-25
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| Aamy_C | smart00632 | Aamy_C domain; |
437-521 | 1.40e-16 | ||||||||
Aamy_C domain; Pssm-ID: 214749 Cd Length: 81 Bit Score: 74.97 E-value: 1.40e-16
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| TIG | pfam01833 | IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ... |
526-604 | 7.55e-12 | ||||||||
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members. Pssm-ID: 460355 [Multi-domain] Cd Length: 84 Bit Score: 61.69 E-value: 7.55e-12
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| pulA_typeI | TIGR02104 | pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ... |
93-438 | 3.51e-11 | ||||||||
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. Pssm-ID: 273975 [Multi-domain] Cd Length: 605 Bit Score: 66.57 E-value: 3.51e-11
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| PLN02950 | PLN02950 | 4-alpha-glucanotransferase |
611-694 | 4.73e-05 | ||||||||
4-alpha-glucanotransferase Pssm-ID: 215512 [Multi-domain] Cd Length: 909 Bit Score: 47.02 E-value: 4.73e-05
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| Alpha-amylase_C | pfam02806 | Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ... |
440-520 | 2.72e-04 | ||||||||
Alpha amylase, C-terminal all-beta 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: 426991 [Multi-domain] Cd Length: 94 Bit Score: 40.40 E-value: 2.72e-04
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| Name | Accession | Description | Interval | E-value | ||||||||
| AmyAc_AmyMalt_CGTase_like | cd11320 | Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, ... |
39-427 | 0e+00 | ||||||||
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins; Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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: 200459 [Multi-domain] Cd Length: 389 Bit Score: 606.59 E-value: 0e+00
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| AmyAc_bac_CMD_like_2 | cd11339 | Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ... |
41-428 | 2.91e-89 | ||||||||
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: 200478 [Multi-domain] Cd Length: 344 Bit Score: 282.99 E-value: 2.91e-89
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| Alpha-amylase | pfam00128 | Alpha amylase, catalytic domain; Alpha amylase is classified as family 13 of the glycosyl ... |
80-399 | 3.31e-85 | ||||||||
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: 271.92 E-value: 3.31e-85
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| AmyA | COG0366 | Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; |
43-402 | 7.99e-77 | ||||||||
Glycosidase/amylase (phosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440135 [Multi-domain] Cd Length: 413 Bit Score: 252.48 E-value: 7.99e-77
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| AmyAc_euk_AmyA | cd11319 | Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1, ... |
42-427 | 3.36e-65 | ||||||||
Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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: 200458 [Multi-domain] Cd Length: 375 Bit Score: 220.51 E-value: 3.36e-65
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| AmyAc_bac_CMD_like_3 | cd11340 | Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ... |
42-427 | 8.00e-62 | ||||||||
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: 212.46 E-value: 8.00e-62
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| AmyAc_CMD | cd11338 | Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ... |
44-435 | 3.78e-59 | ||||||||
Alpha amylase catalytic domain found in 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). 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: 200477 [Multi-domain] Cd Length: 389 Bit Score: 204.64 E-value: 3.78e-59
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| AmyAc_bac2_AmyA | cd11316 | Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ... |
80-434 | 4.27e-54 | ||||||||
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: 191.26 E-value: 4.27e-54
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| CBM20_CGTase | cd05807 | CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known ... |
609-709 | 6.97e-53 | ||||||||
CGTase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. CGTase, also known as cyclodextrin glycosyltransferase and cyclodextrin glucanotransferase, catalyzes the formation of various cyclodextrins (alpha-1,4-glucans) from starch. CGTase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 and an IPT domain of unknown function. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99882 [Multi-domain] Cd Length: 101 Bit Score: 177.75 E-value: 6.97e-53
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| AmyAc_5 | cd11352 | Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ... |
44-424 | 4.17e-48 | ||||||||
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 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: 200489 [Multi-domain] Cd Length: 443 Bit Score: 175.97 E-value: 4.17e-48
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| AmyAc_family | cd00551 | Alpha amylase catalytic domain family; The Alpha-amylase family comprises the largest family ... |
44-387 | 2.05e-44 | ||||||||
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: 160.03 E-value: 2.05e-44
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| Aamy | smart00642 | Alpha-amylase domain; |
47-170 | 1.95e-38 | ||||||||
Alpha-amylase domain; Pssm-ID: 214758 [Multi-domain] Cd Length: 166 Bit Score: 140.16 E-value: 1.95e-38
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| AmyAc_arch_bac_AmyA | cd11313 | Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1, ... |
73-434 | 4.77e-37 | ||||||||
Alpha amylase catalytic domain found in archaeal and 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 firmicutes, bacteroidetes, and proteobacteria. 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: 200452 [Multi-domain] Cd Length: 336 Bit Score: 141.53 E-value: 4.77e-37
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| PRK10785 | PRK10785 | maltodextrin glucosidase; Provisional |
44-464 | 8.66e-34 | ||||||||
maltodextrin glucosidase; Provisional Pssm-ID: 236759 [Multi-domain] Cd Length: 598 Bit Score: 137.06 E-value: 8.66e-34
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| IPT_CGTD | cd00604 | IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These ... |
526-607 | 7.90e-32 | ||||||||
IPT domain (domain D) of cyclodextrin glycosyltransferase (CGTase) and similar enzymes. These enzymes are involved in the enzymatic hydrolysis of alpha-1,4 linkages of starch polymers and belong to the glycosyl hydrolase family 13. Most consist of three domains (A,B,C) but CGTase is more complex and has two additional domains (D,E). The function of the IPT/D domain is unknown. Pssm-ID: 238338 [Multi-domain] Cd Length: 81 Bit Score: 118.22 E-value: 7.90e-32
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| AmyAc_CMD_like | cd11337 | Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins; ... |
93-436 | 1.08e-31 | ||||||||
Alpha amylase catalytic domain found in 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 mainly 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: 200476 [Multi-domain] Cd Length: 328 Bit Score: 126.10 E-value: 1.08e-31
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| CBM_20 | pfam00686 | Starch binding domain; |
611-695 | 3.23e-31 | ||||||||
Starch binding domain; Pssm-ID: 425821 [Multi-domain] Cd Length: 95 Bit Score: 117.00 E-value: 3.23e-31
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| AmyAc_OligoGlu_like | cd11331 | Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ... |
44-394 | 1.25e-30 | ||||||||
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, 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. 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: 200470 [Multi-domain] Cd Length: 450 Bit Score: 125.52 E-value: 1.25e-30
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| AmyAc_SI_OligoGlu_DGase | cd11333 | Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called ... |
44-405 | 2.83e-30 | ||||||||
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: 124.11 E-value: 2.83e-30
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| CBM20 | cd05467 | The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is ... |
612-709 | 2.91e-30 | ||||||||
The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 119437 Cd Length: 96 Bit Score: 114.32 E-value: 2.91e-30
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| AmyAc_4 | cd11350 | Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ... |
80-432 | 1.19e-29 | ||||||||
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 (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: 200488 [Multi-domain] Cd Length: 390 Bit Score: 121.61 E-value: 1.19e-29
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| AmyAc_TreS | cd11334 | Alpha amylase catalytic domain found in Trehalose synthetase; Trehalose synthetase (TreS) ... |
44-390 | 1.77e-28 | ||||||||
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: 119.21 E-value: 1.77e-28
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| AmyAc_maltase | cd11328 | Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related ... |
80-278 | 1.18e-27 | ||||||||
Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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: 200467 [Multi-domain] Cd Length: 470 Bit Score: 116.95 E-value: 1.18e-27
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| malS | PRK09505 | alpha-amylase; Reviewed |
45-460 | 1.88e-27 | ||||||||
alpha-amylase; Reviewed Pssm-ID: 236543 [Multi-domain] Cd Length: 683 Bit Score: 118.23 E-value: 1.88e-27
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| AmyAc_euk_bac_CMD_like | cd11353 | Alpha amylase catalytic domain found in eukaryotic and bacterial cyclomaltodextrinases and ... |
86-435 | 8.16e-27 | ||||||||
Alpha amylase catalytic domain found in eukaryotic and 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 mainly 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: 200490 [Multi-domain] Cd Length: 366 Bit Score: 112.65 E-value: 8.16e-27
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| CBM20_novamyl | cd05820 | Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1, ... |
610-710 | 2.16e-26 | ||||||||
Novamyl (also known as acarviose transferase, ATase, maltogenic alpha-amylase, glucan 1,4-alpha-maltohydrolase, and AcbD), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Novamyl has a five-domain structure similar to that of cyclodextrin glucanotransferase (CGTase). Novamyl has a substrate-binding surface with an open groove which can accommodate both cyclodextrins and linear substrates. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99893 Cd Length: 103 Bit Score: 103.83 E-value: 2.16e-26
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| CBM20_glucoamylase | cd05811 | Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, ... |
611-695 | 1.61e-25 | ||||||||
Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99886 [Multi-domain] Cd Length: 106 Bit Score: 101.19 E-value: 1.61e-25
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| CBM20_alpha_amylase | cd05808 | Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain ... |
611-709 | 1.73e-25 | ||||||||
Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99883 Cd Length: 95 Bit Score: 100.90 E-value: 1.73e-25
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| CBM_2 | smart01065 | Starch binding domain; |
611-695 | 2.02e-25 | ||||||||
Starch binding domain; Pssm-ID: 215006 [Multi-domain] Cd Length: 88 Bit Score: 100.50 E-value: 2.02e-25
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| AmyAc_OligoGlu_TS | cd11332 | Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ... |
44-261 | 1.91e-24 | ||||||||
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins; 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. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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: 200471 [Multi-domain] Cd Length: 481 Bit Score: 107.36 E-value: 1.91e-24
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| AmyAc_2 | cd11348 | Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ... |
80-393 | 1.12e-23 | ||||||||
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: 104.31 E-value: 1.12e-23
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| AmyAc_OligoGlu | cd11330 | Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; ... |
80-390 | 1.62e-23 | ||||||||
Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins; Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, 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. 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: 200469 [Multi-domain] Cd Length: 472 Bit Score: 104.65 E-value: 1.62e-23
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| AmyAc_SLC3A1 | cd11359 | Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, ... |
80-261 | 1.63e-22 | ||||||||
Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins; SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. 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: 200494 [Multi-domain] Cd Length: 456 Bit Score: 101.28 E-value: 1.63e-22
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| PRK09441 | PRK09441 | cytoplasmic alpha-amylase; Reviewed |
82-517 | 1.05e-21 | ||||||||
cytoplasmic alpha-amylase; Reviewed Pssm-ID: 236518 [Multi-domain] Cd Length: 479 Bit Score: 98.81 E-value: 1.05e-21
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| AmyAc_bac1_AmyA | cd11315 | Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1, ... |
96-386 | 2.25e-21 | ||||||||
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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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: 200454 [Multi-domain] Cd Length: 352 Bit Score: 96.19 E-value: 2.25e-21
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| AmyAc_bac_CMD_like | cd11354 | Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins; ... |
121-431 | 3.16e-21 | ||||||||
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: 200491 [Multi-domain] Cd Length: 357 Bit Score: 95.86 E-value: 3.16e-21
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| CBM20_beta_amylase | cd05809 | Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase ... |
611-695 | 4.57e-19 | ||||||||
Beta-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Beta-amylase has, in addition to its C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 14, which hydrolyzes the alpha-1,4-glucosidic bonds of starch, yielding beta-maltose from the nonreducing end of the substrate. Beta-amylase is found in both plants and microorganisms, however the plant members lack a C-terminal CBM20 domain and are not included in this group. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99884 Cd Length: 99 Bit Score: 82.68 E-value: 4.57e-19
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| CBM20_alpha_MTH | cd05810 | Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding ... |
611-695 | 4.65e-17 | ||||||||
Glucan 1,4-alpha-maltotetraohydrolase (alpha-MTH), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Alpha-MTH, also known as maltotetraose-forming exo-amylase or G4-amylase, is an exo-amylase found in bacteria that degrades starch from its non-reducing end. Most alpha-MTHs have, in addition to the C-terminal CBM20 domain, an N-terminal glycosyl hydrolase family 13 catalytic domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99885 Cd Length: 97 Bit Score: 77.06 E-value: 4.65e-17
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| PRK10933 | PRK10933 | trehalose-6-phosphate hydrolase; Provisional |
80-258 | 5.00e-17 | ||||||||
trehalose-6-phosphate hydrolase; Provisional Pssm-ID: 182849 [Multi-domain] Cd Length: 551 Bit Score: 84.80 E-value: 5.00e-17
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| PRK14510 | PRK14510 | bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase; |
73-435 | 6.01e-17 | ||||||||
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase; Pssm-ID: 237739 [Multi-domain] Cd Length: 1221 Bit Score: 85.71 E-value: 6.01e-17
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| AmyAc_bac_fung_AmyA | cd11318 | Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1, ... |
93-388 | 9.86e-17 | ||||||||
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: 82.95 E-value: 9.86e-17
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| Aamy_C | smart00632 | Aamy_C domain; |
437-521 | 1.40e-16 | ||||||||
Aamy_C domain; Pssm-ID: 214749 Cd Length: 81 Bit Score: 74.97 E-value: 1.40e-16
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| AmyAc_arch_bac_plant_AmyA | cd11314 | Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also ... |
79-387 | 2.07e-15 | ||||||||
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: 77.65 E-value: 2.07e-15
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| AmyAc_GTHase | cd11325 | Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called ... |
79-442 | 8.07e-15 | ||||||||
Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase); Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase Pssm-ID: 200464 [Multi-domain] Cd Length: 436 Bit Score: 77.20 E-value: 8.07e-15
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| AmyAc_3 | cd11349 | Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ... |
44-390 | 4.32e-12 | ||||||||
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 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: 200487 [Multi-domain] Cd Length: 456 Bit Score: 68.85 E-value: 4.32e-12
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| CBM20_DPE2_repeat2 | cd05816 | Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ... |
612-695 | 7.11e-12 | ||||||||
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 2. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal CBM20 domains. Included in this group are PDE2-like proteins from Dictyostelium, Entamoeba, and Bacteroides. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99890 Cd Length: 99 Bit Score: 62.34 E-value: 7.11e-12
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| TIG | pfam01833 | IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These ... |
526-604 | 7.55e-12 | ||||||||
IPT/TIG domain; This family consists of a domain that has an immunoglobulin like fold. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. CAUTION: This family does not currently recognize a significant number of members. Pssm-ID: 460355 [Multi-domain] Cd Length: 84 Bit Score: 61.69 E-value: 7.55e-12
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| AmyAc_bac_euk_AmyA | cd11317 | Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1, ... |
139-398 | 1.55e-11 | ||||||||
Alpha amylase catalytic domain found in bacterial and eukaryotic 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 proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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: 200456 [Multi-domain] Cd Length: 329 Bit Score: 66.05 E-value: 1.55e-11
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| pulA_typeI | TIGR02104 | pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which ... |
93-438 | 3.51e-11 | ||||||||
pullulanase, type I; Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases. Pssm-ID: 273975 [Multi-domain] Cd Length: 605 Bit Score: 66.57 E-value: 3.51e-11
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| AmyAc_Amylosucrase | cd11324 | Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase ... |
79-267 | 8.38e-11 | ||||||||
Alpha amylase catalytic domain found in Amylosucrase; Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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: 200463 Cd Length: 536 Bit Score: 64.90 E-value: 8.38e-11
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| AmyAc_AGS | cd11323 | Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine ... |
46-163 | 2.18e-10 | ||||||||
Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase); Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. 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: 200462 [Multi-domain] Cd Length: 569 Bit Score: 63.85 E-value: 2.18e-10
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| GlgB | COG0296 | 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]; |
79-261 | 3.24e-10 | ||||||||
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]; Pssm-ID: 440065 [Multi-domain] Cd Length: 625 Bit Score: 63.23 E-value: 3.24e-10
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| AmyAc_maltase-like | cd11329 | Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the ... |
136-260 | 8.75e-10 | ||||||||
Alpha amylase catalytic domain family found in maltase; Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. The catalytic triad (DED) which is highly conserved in the other maltase group is not present in this subfamily. 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: 200468 [Multi-domain] Cd Length: 477 Bit Score: 61.63 E-value: 8.75e-10
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| AmyAc_Glg_BE | cd11322 | Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1, ... |
93-261 | 1.29e-09 | ||||||||
Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme); The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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: 200461 [Multi-domain] Cd Length: 402 Bit Score: 60.62 E-value: 1.29e-09
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| PRK14706 | PRK14706 | glycogen branching enzyme; Provisional |
93-261 | 1.36e-09 | ||||||||
glycogen branching enzyme; Provisional Pssm-ID: 237795 [Multi-domain] Cd Length: 639 Bit Score: 61.54 E-value: 1.36e-09
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| PLN02784 | PLN02784 | alpha-amylase |
94-295 | 1.97e-09 | ||||||||
alpha-amylase Pssm-ID: 215419 [Multi-domain] Cd Length: 894 Bit Score: 61.18 E-value: 1.97e-09
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| trehalose_TreY | TIGR02401 | malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan ... |
93-183 | 2.07e-09 | ||||||||
malto-oligosyltrehalose synthase; This enzyme, formally named (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase, is the TreY enzyme of the TreYZ pathway of trehalose biosynthesis, an alternative to the OtsAB pathway. Trehalose may be incorporated into more complex compounds but is best known as compatible solute. It is one of the most effective osmoprotectants, and unlike the various betaines does not require nitrogen for its synthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides] Pssm-ID: 274113 [Multi-domain] Cd Length: 825 Bit Score: 60.88 E-value: 2.07e-09
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| CBM20_DSP | cd05817 | Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) ... |
621-694 | 2.12e-09 | ||||||||
Dual-specificity phosphatase (DSP), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This CBM20 domain is located at the N-terminus of a protein tyrosine phosphatase of unknown function found in slime molds and ciliated protozoans. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99891 Cd Length: 100 Bit Score: 55.17 E-value: 2.12e-09
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| PRK14511 | PRK14511 | malto-oligosyltrehalose synthase; |
92-183 | 2.15e-09 | ||||||||
malto-oligosyltrehalose synthase; Pssm-ID: 237740 [Multi-domain] Cd Length: 879 Bit Score: 60.76 E-value: 2.15e-09
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| AmyAc_MTSase | cd11336 | Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); ... |
93-183 | 2.90e-09 | ||||||||
Alpha amylase catalytic domain found in maltooligosyl trehalose synthase (MTSase); Maltooligosyl trehalose synthase (MTSase) domain. MTSase and maltooligosyl trehalose trehalohydrolase (MTHase) work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. 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: 200475 [Multi-domain] Cd Length: 660 Bit Score: 60.20 E-value: 2.90e-09
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| IPT | cd00102 | Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as ... |
526-607 | 4.40e-09 | ||||||||
Immunoglobulin-like fold, Plexins, Transcription factors (IPT). IPTs are also known as Transcription factor ImmunoGlobin (TIG) domains. They are present in intracellular transcription factors, cell surface receptors (such as plexins and scatter factor receptors), as well as, cyclodextrin glycosyltransferase and similar enzymes. Although they are involved in DNA binding in transcription factors, their function in other proteins is unknown. In these transcription factors, IPTs form homo- or heterodimers with the exception of the nuclear factor of activated Tcells (NFAT) transcription factors which are mainly monomers. Pssm-ID: 238050 [Multi-domain] Cd Length: 89 Bit Score: 54.00 E-value: 4.40e-09
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| AmyAc_SLC3A2 | cd11345 | Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 ... |
131-267 | 3.91e-08 | ||||||||
Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins; 4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. 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: 200483 [Multi-domain] Cd Length: 326 Bit Score: 55.52 E-value: 3.91e-08
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| AmyAc_Glg_debranch | cd11326 | Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes ... |
93-256 | 2.28e-07 | ||||||||
Alpha amylase catalytic domain found in glycogen debranching enzymes; Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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: 200465 [Multi-domain] Cd Length: 433 Bit Score: 53.63 E-value: 2.28e-07
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| CBM20_water_dikinase | cd05818 | Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 ... |
623-694 | 3.13e-07 | ||||||||
Phosphoglucan water dikinase (also known as alpha-glucan water dikinase), N-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in the chloroplast-encoded phosphoglucan water dikinase, one of two enzymes involved in the phosphorylation of plant starches. In addition to the CBM20 domain, phosphoglucan water dikinase contains a C-terminal pyruvate binding domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99892 Cd Length: 92 Bit Score: 48.65 E-value: 3.13e-07
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| PRK14507 | PRK14507 | malto-oligosyltrehalose synthase; |
93-184 | 5.45e-07 | ||||||||
malto-oligosyltrehalose synthase; Pssm-ID: 237737 [Multi-domain] Cd Length: 1693 Bit Score: 53.18 E-value: 5.45e-07
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| CBM20_Prei4 | cd05814 | Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation ... |
613-689 | 3.01e-06 | ||||||||
Prei4, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Preimplantation protein 4 (Prei4) is a protein of unknown function that is expressed during mouse preimplantation embryogenesis. In addition to the N-terminal CBM20 domain, Prei4 contains a C-terminal glycerophosphoryl diester phosphodiesterase (GDPD) domain. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99888 Cd Length: 120 Bit Score: 46.93 E-value: 3.01e-06
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| PRK12313 | PRK12313 | 1,4-alpha-glucan branching protein GlgB; |
93-261 | 5.60e-06 | ||||||||
1,4-alpha-glucan branching protein GlgB; Pssm-ID: 237052 [Multi-domain] Cd Length: 633 Bit Score: 49.51 E-value: 5.60e-06
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| PLN02447 | PLN02447 | 1,4-alpha-glucan-branching enzyme |
113-284 | 1.88e-05 | ||||||||
1,4-alpha-glucan-branching enzyme Pssm-ID: 215246 [Multi-domain] Cd Length: 758 Bit Score: 48.13 E-value: 1.88e-05
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| PRK05402 | PRK05402 | 1,4-alpha-glucan branching protein GlgB; |
93-167 | 1.93e-05 | ||||||||
1,4-alpha-glucan branching protein GlgB; Pssm-ID: 235445 [Multi-domain] Cd Length: 726 Bit Score: 47.86 E-value: 1.93e-05
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| CBM20_DPE2_repeat1 | cd05815 | Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) ... |
621-690 | 2.68e-05 | ||||||||
Disproportionating enzyme 2 (DPE2), N-terminal CBM20 (carbohydrate-binding module, family 20) domain, repeat 1. DPE2 is a transglucosidase that is essential for the cytosolic metabolism of maltose in plant leaves at night. Maltose is an intermediate on the pathway from starch to sucrose and DPE2 is thought to metabolize the maltose that is exported from the chloroplast. DPE2 has two N-terminal CBM20 starch binding domains as well as a C-terminal amylomaltase (4-alpha-glucanotransferase) catalytic domain. DPE1, the plastid version of this enzyme, has a transglucosidase domain that is similar to that of DPE2 but lacks the N-terminal carbohydrate-binding domains. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99889 Cd Length: 101 Bit Score: 43.59 E-value: 2.68e-05
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| AmyAc_1 | cd11347 | Alpha amylase catalytic domain found in an uncharacterized protein family; The Alpha-amylase ... |
134-182 | 4.46e-05 | ||||||||
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 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: 200485 [Multi-domain] Cd Length: 391 Bit Score: 46.46 E-value: 4.46e-05
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| PLN02950 | PLN02950 | 4-alpha-glucanotransferase |
611-694 | 4.73e-05 | ||||||||
4-alpha-glucanotransferase Pssm-ID: 215512 [Multi-domain] Cd Length: 909 Bit Score: 47.02 E-value: 4.73e-05
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| AmyAc_bac_euk_BE | cd11321 | Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching ... |
139-261 | 5.12e-05 | ||||||||
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes; Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic 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: 200460 [Multi-domain] Cd Length: 406 Bit Score: 46.07 E-value: 5.12e-05
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| PLN00196 | PLN00196 | alpha-amylase; Provisional |
76-387 | 1.79e-04 | ||||||||
alpha-amylase; Provisional Pssm-ID: 165762 [Multi-domain] Cd Length: 428 Bit Score: 44.52 E-value: 1.79e-04
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| Alpha-amylase_C | pfam02806 | Alpha amylase, C-terminal all-beta domain; Alpha amylase is classified as family 13 of the ... |
440-520 | 2.72e-04 | ||||||||
Alpha amylase, C-terminal all-beta 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: 426991 [Multi-domain] Cd Length: 94 Bit Score: 40.40 E-value: 2.72e-04
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| IPT_PCSR | cd00603 | IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup ... |
532-607 | 4.68e-04 | ||||||||
IPT domain of Plexins and Cell Surface Receptors (PCSR) and related proteins . This subgroup contains IPT domains of plexins, receptors, like the plasminogen-related growth factor receptors, the hepatocyte growth factor-scatter factors, and the macrophage-stimulating receptors and of fibrocystin. Plexins are involved in the regulation of cell proliferation and of cellular adhesion and repulsion receptors. In general, there are three copies of the IPT_PCSR domain present preceeded by SEMA (semaphorin) and PSI (plexin, semaphorin, integrin) domains. Pssm-ID: 238337 [Multi-domain] Cd Length: 90 Bit Score: 39.75 E-value: 4.68e-04
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| PLN02950 | PLN02950 | 4-alpha-glucanotransferase |
603-694 | 6.06e-04 | ||||||||
4-alpha-glucanotransferase Pssm-ID: 215512 [Multi-domain] Cd Length: 909 Bit Score: 43.17 E-value: 6.06e-04
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| AmyAc_GlgE_like | cd11344 | Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan: ... |
136-167 | 6.53e-04 | ||||||||
Alpha amylase catalytic domain found in GlgE-like proteins; GlgE is a (1,4)-a-D-glucan:phosphate a-D-maltosyltransferase, involved in a-glucan biosynthesis in bacteria. It is also an anti-tuberculosis drug target. GlgE isoform I from Streptomyces coelicolor has the same catalytic and very similar kinetic properties to GlgE from Mycobacterium tuberculosis. GlgE from Streptomyces coelicolor forms a homodimer with each subunit comprising five domains (A, B, C, N, and S) and 2 inserts. Domain A is a catalytic alpha-amylase-type domain that along with domain N, which has a beta-sandwich fold and forms the core of the dimer interface, binds cyclodextrins. Domain A, B, and the 2 inserts define a well conserved donor pocket that binds maltose. Cyclodextrins competitively inhibit the binding of maltooligosaccharides to the S. coelicolor enzyme, indicating that the hydrophobic patch overlaps with the acceptor binding site. This is not the case in M. tuberculosis GlgE because cyclodextrins do not inhibit this enzyme, despite acceptor length specificity being conserved. Domain C is hypothesized to help stabilize domain A and could be involved in substrate binding. Domain S is a helix bundle that is inserted within the N domain and it plays a role in the dimer interface and interacts directly with domain B. 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: 200482 [Multi-domain] Cd Length: 355 Bit Score: 42.59 E-value: 6.53e-04
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| AmyAc_plant_IsoA | cd11346 | Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching ... |
80-176 | 7.24e-04 | ||||||||
Alpha amylase catalytic domain family found in plant isoamylases; Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like 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: 200484 [Multi-domain] Cd Length: 347 Bit Score: 42.46 E-value: 7.24e-04
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| CBM20_laforin | cd05806 | Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) ... |
613-693 | 1.05e-03 | ||||||||
Laforin protein tyrosine phosphatase, N-terminal CBM20 (carbohydrate-binding module, family 20) domain. Laforin, encoded by the EPM2A gene, is a dual-specificity phosphatase that dephosphorylates complex carbohydrates. Mutations in the gene encoding laforin result in Lafora disease, a fatal autosomal recessive neurodegenerative disorder characterized by the presence of intracellular deposits of insoluble, abnormally branched, glycogen-like polymers, known as Lafora bodies, in neurons, muscle, liver, and other tissues. The molecular basis for the formation of these Lafora bodies is unknown. Laforin is one of the only phosphatases that contains a carbohydrate-binding module. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch. Pssm-ID: 99881 Cd Length: 112 Bit Score: 39.42 E-value: 1.05e-03
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| PLN02960 | PLN02960 | alpha-amylase |
127-170 | 1.44e-03 | ||||||||
alpha-amylase Pssm-ID: 215519 [Multi-domain] Cd Length: 897 Bit Score: 42.13 E-value: 1.44e-03
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| Malt_amylase_C | pfam16657 | Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an ... |
442-464 | 5.94e-03 | ||||||||
Maltogenic Amylase, C-terminal domain; This is the C-terminal domain of Maltogenic amylase, an enzyme that hydrolyses starch material. Maltogenic amylases are central to carbohydrate metabolism. Pssm-ID: 435493 [Multi-domain] Cd Length: 75 Bit Score: 35.99 E-value: 5.94e-03
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