You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000003208_04346
You are here: Home > Sequence: MGYG000003208_04346
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 | Pseudomonas_E extremaustralis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis | |||||||||||
| CAZyme ID | MGYG000003208_04346 | |||||||||||
| CAZy Family | GH13 | |||||||||||
| CAZyme Description | Glucan 1,4-alpha-maltotetraohydrolase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 80258; End: 81847 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH13 | 60 | 346 | 4.4e-44 | 0.9930795847750865 |
| CBM20 | 437 | 522 | 1.7e-19 | 0.9222222222222223 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd11314 | AmyAc_arch_bac_plant_AmyA | 9.28e-89 | 34 | 377 | 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. |
| PLN02361 | PLN02361 | 8.61e-42 | 31 | 377 | 10 | 353 | alpha-amylase |
| PLN00196 | PLN00196 | 9.39e-35 | 28 | 427 | 20 | 426 | alpha-amylase; Provisional |
| PLN02784 | PLN02784 | 1.15e-32 | 20 | 429 | 490 | 894 | alpha-amylase |
| PRK09441 | PRK09441 | 1.16e-23 | 34 | 368 | 5 | 393 | cytoplasmic alpha-amylase; Reviewed |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| SDF70084.1 | 0.0 | 1 | 529 | 1 | 529 |
| QDH63340.1 | 0.0 | 8 | 529 | 8 | 529 |
| QVN02521.1 | 0.0 | 1 | 529 | 1 | 528 |
| QVN08034.1 | 0.0 | 1 | 529 | 1 | 531 |
| QKJ71969.1 | 0.0 | 1 | 529 | 1 | 531 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6JQB_A | 6.98e-214 | 22 | 529 | 6 | 530 | Thestructure of maltooligosaccharide-forming amylase from Pseudomonas saccharophila STB07 with pseudo-maltoheptaose [Pelomonas saccharophila] |
| 6J3X_A | 5.68e-213 | 22 | 529 | 6 | 530 | TheStructure of Maltooligosaccharide-forming Amylase from Pseudomonas saccharophila STB07 with Maltotriose [Pelomonas saccharophila] |
| 6IYG_A | 2.83e-212 | 22 | 516 | 6 | 517 | TheStructure of Maltooligosaccharide-forming Amylase from Pseudomonas saccharophila STB07 with Maltotetraose [Pelomonas saccharophila] |
| 1GCY_A | 2.93e-212 | 22 | 528 | 6 | 526 | HighResolution Crystal Structure Of Maltotetraose-Forming Exo-Amylase [Pseudomonas stutzeri] |
| 6IWK_A | 1.75e-191 | 22 | 428 | 6 | 418 | TheStructure of Maltooligosaccharide-forming Amylase from Pseudomonas saccharophila STB07 [Pelomonas saccharophila] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P22963 | 1.98e-213 | 15 | 529 | 20 | 551 | Glucan 1,4-alpha-maltotetraohydrolase OS=Pelomonas saccharophila OX=304 GN=mta PE=1 SV=1 |
| P13507 | 1.67e-211 | 15 | 528 | 20 | 547 | Glucan 1,4-alpha-maltotetraohydrolase OS=Pseudomonas stutzeri OX=316 GN=amyP PE=1 SV=2 |
| Q8LFG1 | 5.70e-38 | 31 | 426 | 24 | 411 | Probable alpha-amylase 2 OS=Arabidopsis thaliana OX=3702 GN=AMY2 PE=2 SV=1 |
| A2YGY2 | 1.41e-37 | 31 | 431 | 21 | 430 | Alpha-amylase isozyme 2A OS=Oryza sativa subsp. indica OX=39946 GN=AMYC2 PE=2 SV=1 |
| Q0D9J1 | 3.60e-37 | 31 | 438 | 21 | 440 | Alpha-amylase isozyme 2A OS=Oryza sativa subsp. japonica OX=39947 GN=AMY2A PE=2 SV=1 |
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 |
|---|---|---|---|---|---|
| 0.000245 | 0.999185 | 0.000136 | 0.000154 | 0.000132 | 0.000131 |