Species | Akkermansia sp004167605 | |||||||||||
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Lineage | Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; Akkermansiaceae; Akkermansia; Akkermansia sp004167605 | |||||||||||
CAZyme ID | MGYG000000870_02473 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16567; End: 18330 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 29 | 408 | 2.1e-119 | 0.9946666666666667 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11349 | AmyAc_3 | 4.59e-172 | 3 | 464 | 1 | 451 | 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 | 3.58e-50 | 4 | 471 | 6 | 336 | 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 | 1.21e-34 | 3 | 474 | 1 | 390 | 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 | 2.58e-21 | 4 | 398 | 1 | 253 | 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. |
COG0366 | AmyA | 6.59e-20 | 4 | 522 | 2 | 488 | Glycosidase [Carbohydrate transport and metabolism]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QWO86199.1 | 0.0 | 1 | 587 | 1 | 589 |
QWO96080.1 | 0.0 | 1 | 587 | 1 | 589 |
QWO91137.1 | 0.0 | 1 | 587 | 1 | 589 |
QWO93507.1 | 0.0 | 1 | 587 | 1 | 589 |
QWP70844.1 | 0.0 | 1 | 587 | 1 | 589 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3DHU_A | 2.16e-18 | 4 | 402 | 14 | 313 | 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] |
4GKL_A | 9.76e-13 | 39 | 402 | 28 | 291 | Crystalstructure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana],4GKL_B Crystal structure of a noncanonic maltogenic alpha-amylase AmyB from Thermotoga neapolitana [Thermotoga neapolitana] |
3WY4_A | 2.11e-10 | 4 | 264 | 12 | 202 | 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] |
3WY1_A | 2.11e-10 | 4 | 264 | 12 | 202 | 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] |
3WY3_A | 8.51e-10 | 4 | 264 | 12 | 202 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O16098 | 2.68e-11 | 4 | 264 | 87 | 280 | Maltase 1 OS=Drosophila virilis OX=7244 GN=Mal-B1 PE=3 SV=2 |
P14898 | 6.37e-09 | 4 | 473 | 135 | 496 | Alpha-amylase 2 OS=Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) OX=309799 GN=amyB PE=1 SV=2 |
O16099 | 8.74e-09 | 4 | 264 | 48 | 241 | Maltase 2 OS=Drosophila virilis OX=7244 GN=Mal-B2 PE=3 SV=2 |
P07190 | 2.60e-08 | 6 | 264 | 29 | 221 | Maltase A1 OS=Drosophila melanogaster OX=7227 GN=Mal-A1 PE=2 SV=2 |
Q2RTZ1 | 1.51e-07 | 200 | 411 | 356 | 551 | Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgE PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000044 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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