Species | RC9 sp000432655 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp000432655 | |||||||||||
CAZyme ID | MGYG000001767_01307 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Alpha-amylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 24728; End: 26017 Strand: - |
Family | Start | End | Evalue | family coverage |
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GH13 | 132 | 296 | 7.6e-55 | 0.43733333333333335 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11349 | AmyAc_3 | 3.38e-116 | 3 | 333 | 1 | 433 | 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. |
cd11313 | AmyAc_arch_bac_AmyA | 2.81e-47 | 27 | 308 | 29 | 305 | 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. |
cd11347 | AmyAc_1 | 1.31e-35 | 4 | 358 | 2 | 391 | 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. |
cd00551 | AmyAc_family | 4.83e-33 | 4 | 278 | 1 | 243 | 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. |
pfam00128 | Alpha-amylase | 7.75e-24 | 28 | 292 | 12 | 327 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BCS86666.1 | 1.19e-82 | 2 | 406 | 4 | 507 |
QRO26211.1 | 2.91e-80 | 2 | 406 | 6 | 516 |
AWX07627.1 | 5.60e-80 | 1 | 406 | 1 | 518 |
ATV33586.1 | 5.60e-80 | 1 | 406 | 1 | 518 |
ATV40006.1 | 5.60e-80 | 1 | 406 | 1 | 518 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3DHU_A | 4.71e-23 | 29 | 258 | 39 | 284 | Crystalstructure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_B Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_C Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum],3DHU_D Crystal structure of an alpha-amylase from Lactobacillus plantarum [Lactiplantibacillus plantarum] |
3WY1_A | 1.24e-13 | 28 | 297 | 41 | 379 | Crystalstructure of alpha-glucosidase [Halomonas sp. H11],3WY1_B Crystal structure of alpha-glucosidase [Halomonas sp. H11],3WY2_A Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11],3WY2_B Crystal structure of alpha-glucosidase in complex with glucose [Halomonas sp. H11] |
3WY4_A | 2.91e-13 | 28 | 297 | 41 | 379 | Crystalstructure of alpha-glucosidase mutant E271Q in complex with maltose [Halomonas sp. H11],3WY4_B Crystal structure of alpha-glucosidase mutant E271Q in complex with maltose [Halomonas sp. H11] |
3WY3_A | 5.15e-13 | 28 | 297 | 41 | 379 | Crystalstructure of alpha-glucosidase mutant D202N in complex with glucose and glycerol [Halomonas sp. H11],3WY3_B Crystal structure of alpha-glucosidase mutant D202N in complex with glucose and glycerol [Halomonas sp. H11] |
1WZA_A | 8.25e-13 | 29 | 400 | 44 | 448 | Crystalstructure of alpha-amylase from H.orenii [Halothermothrix orenii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P14899 | 1.12e-13 | 28 | 347 | 65 | 418 | Alpha-amylase 3 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyC PE=3 SV=2 |
P31746 | 1.02e-10 | 28 | 290 | 90 | 385 | Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1-1) OX=29334 GN=cgt PE=1 SV=1 |
P29094 | 1.55e-10 | 28 | 169 | 39 | 209 | Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1 |
P20845 | 1.94e-10 | 60 | 347 | 101 | 442 | Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1 |
Q07837 | 1.26e-09 | 28 | 184 | 151 | 340 | Neutral and basic amino acid transport protein rBAT OS=Homo sapiens OX=9606 GN=SLC3A1 PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000062 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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