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CAZyme Information: MGYG000003236_01671
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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 | UMGS1397 sp900761355 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1397; UMGS1397 sp900761355 | |||||||||||
| CAZyme ID | MGYG000003236_01671 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | 1,4-alpha-glucan branching enzyme GlgB | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 36495; End: 38504 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 277 | 572 | 1.7e-28 | 0.9230769230769231 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11313 | AmyAc_arch_bac_AmyA | 1.71e-31 | 258 | 590 | 2 | 305 | 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. |
| cd00551 | AmyAc_family | 1.58e-26 | 262 | 569 | 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. |
| pfam00128 | Alpha-amylase | 8.31e-16 | 287 | 572 | 8 | 325 | 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. |
| COG0296 | GlgB | 2.71e-11 | 262 | 416 | 146 | 303 | 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism]. |
| COG0366 | AmyA | 4.76e-11 | 287 | 572 | 33 | 355 | Glycosidase [Carbohydrate transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AEE96957.1 | 5.09e-193 | 3 | 641 | 13 | 650 |
| QHT61281.1 | 2.27e-192 | 8 | 650 | 17 | 658 |
| AZN42601.1 | 7.09e-187 | 12 | 635 | 24 | 658 |
| AWI27297.1 | 2.00e-26 | 285 | 643 | 63 | 420 |
| VEH99811.1 | 2.60e-26 | 285 | 664 | 62 | 449 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3DHU_A | 4.96e-18 | 289 | 572 | 36 | 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 | 2.31e-17 | 289 | 572 | 31 | 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] |
| 4M8U_A | 1.83e-12 | 260 | 431 | 7 | 213 | TheStructure of MalL mutant enzyme V200A from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168] |
| 4MAZ_A | 4.22e-12 | 260 | 431 | 7 | 213 | TheStructure of MalL mutant enzyme V200S from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168] |
| 4M56_A | 5.57e-12 | 260 | 431 | 7 | 213 | TheStructure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],4M56_B The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q45101 | 1.86e-12 | 262 | 572 | 9 | 372 | Oligo-1,6-glucosidase OS=Weizmannia coagulans OX=1398 GN=malL PE=3 SV=1 |
| P29093 | 6.78e-12 | 260 | 431 | 7 | 212 | Oligo-1,6-glucosidase OS=Bacillus sp. (strain F5) OX=268806 GN=malL PE=1 SV=2 |
| Q0AGJ0 | 1.25e-11 | 267 | 438 | 267 | 446 | 1,4-alpha-glucan branching enzyme GlgB OS=Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57) OX=335283 GN=glgB PE=3 SV=1 |
| O06994 | 3.05e-11 | 260 | 431 | 7 | 213 | Oligo-1,6-glucosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=malL PE=1 SV=1 |
| A6VP15 | 6.98e-11 | 287 | 416 | 271 | 405 | 1,4-alpha-glucan branching enzyme GlgB OS=Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z) OX=339671 GN=glgB PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000044 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |