Species | Chryseobacterium gambrini | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Flavobacteriales; Weeksellaceae; Chryseobacterium; Chryseobacterium gambrini | |||||||||||
CAZyme ID | MGYG000001095_03273 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Alpha-amylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 2445; End: 3881 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 92 | 372 | 3.3e-137 | 0.9965397923875432 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK09441 | PRK09441 | 2.06e-168 | 66 | 475 | 1 | 479 | cytoplasmic alpha-amylase; Reviewed |
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.26e-113 | 70 | 399 | 1 | 302 | 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. |
cd11318 | AmyAc_bac_fung_AmyA | 5.89e-67 | 70 | 372 | 3 | 366 | 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. |
PLN00196 | PLN00196 | 9.46e-39 | 68 | 412 | 24 | 393 | alpha-amylase; Provisional |
PLN02784 | PLN02784 | 1.37e-30 | 65 | 369 | 499 | 814 | alpha-amylase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QWA40389.1 | 0.0 | 1 | 478 | 1 | 478 |
ALR31194.1 | 0.0 | 1 | 478 | 1 | 476 |
AYZ13580.1 | 0.0 | 1 | 478 | 1 | 479 |
QUY54407.1 | 0.0 | 1 | 478 | 1 | 479 |
AZB34008.1 | 0.0 | 1 | 477 | 1 | 478 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1MWO_A | 1.06e-161 | 60 | 475 | 1 | 430 | CrystalStructure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase [Pyrococcus woesei],1MXD_A Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei [Pyrococcus woesei],1MXG_A Crystal Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose [Pyrococcus woesei] |
3QGV_A | 4.92e-160 | 68 | 475 | 9 | 430 | Crystalstructure of a thermostable amylase variant [Pyrococcus woesei] |
1W9X_A | 2.26e-40 | 71 | 474 | 5 | 478 | ChainA, Alpha Amylase [Sutcliffiella halmapala] |
2GJP_A | 2.40e-40 | 71 | 474 | 9 | 482 | ChainA, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala] |
3BC9_A | 4.97e-39 | 71 | 474 | 125 | 595 | Alpha-amylaseB in complex with acarbose [Halothermothrix orenii H 168],3BCD_A Alpha-amylase B in complex with maltotetraose and alpha-cyclodextrin [Halothermothrix orenii H 168],3BCF_A Alpha-amylase B from Halothermothrix orenii [Halothermothrix orenii H 168] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P06279 | 3.70e-37 | 63 | 474 | 34 | 514 | Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3 |
P17859 | 1.03e-36 | 69 | 409 | 24 | 385 | Alpha-amylase OS=Vigna mungo OX=3915 GN=AMY1.1 PE=2 SV=1 |
P19571 | 5.97e-36 | 71 | 474 | 42 | 515 | Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1 |
P26613 | 2.13e-35 | 71 | 476 | 6 | 491 | Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3 |
P00692 | 3.39e-34 | 71 | 371 | 36 | 396 | Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000000 | 1.000048 | 0.000000 | 0.000000 | 0.000000 |
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