Species | CAG-873 sp002493945 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp002493945 | |||||||||||
CAZyme ID | MGYG000003985_01187 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Alpha-amylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1; End: 717 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11315 | AmyAc_bac1_AmyA | 2.84e-56 | 11 | 166 | 195 | 352 | 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. |
pfam18612 | Bac_A_amyl_C | 0.002 | 165 | 224 | 1 | 61 | Bacterial Alpha amylase C-terminal domain. This is a bacterial alpha amaylase C-terminal domain found mostly in bacilli. |
smart00632 | Aamy_C | 0.004 | 167 | 213 | 3 | 49 | Aamy_C domain. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QCD43159.1 | 1.18e-106 | 1 | 236 | 239 | 476 |
QCD40786.1 | 9.51e-101 | 1 | 236 | 228 | 465 |
QCP73835.1 | 9.51e-101 | 1 | 236 | 228 | 465 |
QCD35398.1 | 1.75e-100 | 1 | 236 | 241 | 476 |
AGK84826.1 | 2.05e-99 | 1 | 235 | 239 | 474 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1UA7_A | 2.37e-46 | 22 | 236 | 203 | 420 | ChainA, Alpha-amylase [Bacillus subtilis] |
3DC0_A | 3.32e-46 | 22 | 236 | 203 | 420 | Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104] |
1BAG_A | 4.94e-46 | 22 | 236 | 206 | 423 | ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P00691 | 2.66e-44 | 22 | 236 | 247 | 464 | Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2 |
P30269 | 1.70e-35 | 17 | 227 | 368 | 597 | Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1 |
P23671 | 5.49e-29 | 18 | 236 | 256 | 461 | Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000074 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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