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CAZyme Information: MGYG000001548_02455
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Paenibacillus_A tuaregi | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A tuaregi | |||||||||||
| CAZyme ID | MGYG000001548_02455 | |||||||||||
| CAZy Family | GH14 | |||||||||||
| CAZyme Description | 1,4-alpha-glucan branching enzyme GlgB | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2596902; End: 2600294 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH14 | 44 | 429 | 3.2e-129 | 0.9805825242718447 |
| GH13 | 714 | 1016 | 1.8e-97 | 0.9967320261437909 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam01373 | Glyco_hydro_14 | 0.0 | 44 | 439 | 1 | 402 | Glycosyl hydrolase family 14. This family are beta amylases. |
| cd11339 | AmyAc_bac_CMD_like_2 | 1.19e-128 | 678 | 1042 | 2 | 344 | Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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. |
| cd11319 | AmyAc_euk_AmyA | 7.07e-125 | 672 | 1044 | 2 | 374 | Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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. |
| cd11320 | AmyAc_AmyMalt_CGTase_like | 3.23e-97 | 675 | 1041 | 1 | 389 | Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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. |
| pfam00128 | Alpha-amylase | 3.07e-79 | 715 | 1014 | 1 | 334 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ASR45322.1 | 0.0 | 1 | 1128 | 1 | 1141 |
| ALP36976.1 | 0.0 | 1 | 1128 | 1 | 1141 |
| AET57982.1 | 0.0 | 1 | 1128 | 1 | 1141 |
| ALA44490.1 | 0.0 | 1 | 1128 | 1 | 1197 |
| APQ62243.1 | 0.0 | 1 | 1128 | 1 | 1197 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VOC_A | 6.80e-235 | 37 | 449 | 2 | 416 | Crystalstructure of the catalytic domain of beta-amylase from paenibacillus polymyxa [Paenibacillus polymyxa] |
| 1B90_A | 7.18e-143 | 40 | 421 | 10 | 397 | BacillusCereus Beta-Amylase Apo Form [Bacillus cereus],1B9Z_A Bacillus Cereus Beta-Amylase Complexed With Maltose [Bacillus cereus],1J0Y_A Beta-amylase from Bacillus cereus var. mycoides in complex with glucose [Bacillus cereus],1J0Y_B Beta-amylase from Bacillus cereus var. mycoides in complex with glucose [Bacillus cereus],1J0Y_C Beta-amylase from Bacillus cereus var. mycoides in complex with glucose [Bacillus cereus],1J0Y_D Beta-amylase from Bacillus cereus var. mycoides in complex with glucose [Bacillus cereus],1J0Z_A Beta-amylase from Bacillus cereus var. mycoides in complex with maltose [Bacillus cereus],1J0Z_B Beta-amylase from Bacillus cereus var. mycoides in complex with maltose [Bacillus cereus],1J0Z_C Beta-amylase from Bacillus cereus var. mycoides in complex with maltose [Bacillus cereus],1J0Z_D Beta-amylase from Bacillus cereus var. mycoides in complex with maltose [Bacillus cereus],1J10_A beta-amylase from Bacillus cereus var. mycoides in complex with GGX [Bacillus cereus],1J10_B beta-amylase from Bacillus cereus var. mycoides in complex with GGX [Bacillus cereus],1J10_C beta-amylase from Bacillus cereus var. mycoides in complex with GGX [Bacillus cereus],1J10_D beta-amylase from Bacillus cereus var. mycoides in complex with GGX [Bacillus cereus],1J11_A beta-amylase from Bacillus cereus var. mycoides in complex with alpha-EPG [Bacillus cereus],1J11_B beta-amylase from Bacillus cereus var. mycoides in complex with alpha-EPG [Bacillus cereus],1J11_C beta-amylase from Bacillus cereus var. mycoides in complex with alpha-EPG [Bacillus cereus],1J11_D beta-amylase from Bacillus cereus var. mycoides in complex with alpha-EPG [Bacillus cereus],1J12_A Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG [Bacillus cereus],1J12_B Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG [Bacillus cereus],1J12_C Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG [Bacillus cereus],1J12_D Beta-Amylase from Bacillus cereus var. mycoides in Complex with alpha-EBG [Bacillus cereus],1J18_A Crystal Structure of a Beta-Amylase from Bacillus cereus var. mycoides Cocrystallized with Maltose [Bacillus cereus],1VEM_A Crystal Structure Analysis of Bacillus Cereus Beta-Amylase at the optimum pH (6.5) [Bacillus cereus],5BCA_A Beta-Amylase From Bacillus Cereus Var. Mycoides [Bacillus cereus],5BCA_B Beta-Amylase From Bacillus Cereus Var. Mycoides [Bacillus cereus],5BCA_C Beta-Amylase From Bacillus Cereus Var. Mycoides [Bacillus cereus],5BCA_D Beta-Amylase From Bacillus Cereus Var. Mycoides [Bacillus cereus] |
| 1VEO_A | 2.78e-142 | 40 | 421 | 10 | 397 | ChainA, Beta-amylase [Bacillus cereus] |
| 1ITC_A | 5.48e-142 | 40 | 421 | 10 | 397 | ChainA, Beta-Amylase [Bacillus cereus] |
| 1VEN_A | 1.51e-141 | 40 | 421 | 10 | 397 | ChainA, Beta-amylase [Bacillus cereus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P21543 | 0.0 | 1 | 1128 | 1 | 1196 | Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1 |
| P06547 | 1.92e-300 | 5 | 556 | 6 | 559 | Beta-amylase OS=Niallia circulans OX=1397 PE=3 SV=1 |
| P96513 | 3.52e-249 | 1 | 466 | 1 | 468 | Beta-amylase (Fragment) OS=Cytobacillus firmus OX=1399 PE=3 SV=1 |
| P19584 | 1.68e-171 | 32 | 531 | 29 | 535 | Thermophilic beta-amylase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 PE=1 SV=1 |
| P36924 | 1.36e-142 | 5 | 421 | 2 | 427 | Beta-amylase OS=Bacillus cereus OX=1396 GN=spoII PE=1 SV=2 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000346 | 0.998971 | 0.000162 | 0.000199 | 0.000148 | 0.000141 |
