Species | UBA4855 sp900540395 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA4855; UBA4855 sp900540395 | |||||||||||
CAZyme ID | MGYG000000974_00238 | |||||||||||
CAZy Family | CBM32 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 129593; End: 132436 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 523 | 745 | 1.2e-20 | 0.7165605095541401 |
CBM32 | 176 | 283 | 8.2e-16 | 0.8870967741935484 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0366 | AmyA | 5.37e-12 | 520 | 688 | 28 | 201 | Glycosidase [Carbohydrate transport and metabolism]. |
cd11334 | AmyAc_TreS | 5.83e-12 | 557 | 686 | 62 | 197 | 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. |
cd11316 | AmyAc_bac2_AmyA | 2.25e-10 | 578 | 706 | 78 | 204 | 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. |
pfam00754 | F5_F8_type_C | 4.82e-10 | 176 | 265 | 6 | 107 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
pfam00128 | Alpha-amylase | 4.08e-08 | 520 | 692 | 3 | 179 | 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 |
---|---|---|---|---|---|
ATB27203.1 | 2.69e-136 | 31 | 903 | 34 | 953 |
QQA30230.1 | 3.16e-123 | 28 | 913 | 37 | 866 |
QUT61733.1 | 3.32e-123 | 28 | 913 | 39 | 868 |
QNK56434.1 | 1.39e-23 | 41 | 288 | 585 | 835 |
VEU81207.1 | 4.34e-18 | 499 | 685 | 4 | 195 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5OT1_A | 1.59e-11 | 523 | 688 | 354 | 506 | ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis] |
4M8U_A | 2.60e-10 | 498 | 686 | 1 | 200 | TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168] |
5BRQ_A | 4.57e-10 | 499 | 689 | 11 | 213 | Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580],5BRQ_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA) [Bacillus licheniformis DSM 13 = ATCC 14580] |
5BRP_A | 4.57e-10 | 499 | 689 | 11 | 213 | Crystalstructure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_B Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_C Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580],5BRP_D Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG [Bacillus licheniformis DSM 13 = ATCC 14580] |
4MAZ_A | 5.96e-10 | 498 | 686 | 1 | 200 | TheStructure of MalL mutant enzyme V200S from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q54796 | 9.32e-12 | 499 | 685 | 3 | 194 | Glucan 1,6-alpha-glucosidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=dexB PE=3 SV=2 |
P39795 | 1.57e-10 | 501 | 689 | 8 | 207 | Trehalose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=treA PE=1 SV=2 |
Q9P6J3 | 8.45e-10 | 500 | 689 | 12 | 216 | Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1 |
P20845 | 3.04e-09 | 557 | 686 | 104 | 234 | Alpha-amylase OS=Priestia megaterium OX=1404 PE=1 SV=1 |
Q45101 | 3.23e-09 | 501 | 685 | 4 | 199 | Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.016392 | 0.418452 | 0.563871 | 0.000629 | 0.000343 | 0.000283 |
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