| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_025145m |
| Family | GH13 |
| Protein Properties | Length: 332 Molecular Weight: 37844.2 Isoelectric Point: 6.601 |
| Chromosome | Chromosome/Scaffold: 11495 Start: 462504 End: 466377 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 1 | 251 | 1.1e-30 |
| YGSIDELKDLVKSLHEVGLKVLGDAVLNHRCAHFQNQNGVWNIFGGRLNWDDQAVVADDPHFQGRGNKSSGDNFHAAPNIDHSQDFVRKDLKEWLCWLRD EIGYDGWRLDFVKGFWGGYVKDYMDTTEPYFAVGEYWDSLSYTYGETDHSQDAHRQRIIDWINATNGTAGAFDVTTKGILHAALGKCEYWRLSDHKGKPP GVMGWWPSRAVTFIENHDTGSTQGHWRFPSGKEMQGYAYILTHPGTPTVFY | |||
| Full Sequence |
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| Protein Sequence Length: 332 Download |
| YGSIDELKDL VKSLHEVGLK VLGDAVLNHR CAHFQNQNGV WNIFGGRLNW DDQAVVADDP 60 HFQGRGNKSS GDNFHAAPNI DHSQDFVRKD LKEWLCWLRD EIGYDGWRLD FVKGFWGGYV 120 KDYMDTTEPY FAVGEYWDSL SYTYGETDHS QDAHRQRIID WINATNGTAG AFDVTTKGIL 180 HAALGKCEYW RLSDHKGKPP GVMGWWPSRA VTFIENHDTG STQGHWRFPS GKEMQGYAYI 240 LTHPGTPTVF YDHIFSHYHF EIASLIALRN RKKIHCRSTV KITEAERDVY AAIIDEKVAM 300 KIGPGHYEPQ SGSRRWSLAI EGNDYKVWEA S* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-34 | 1 | 272 | 342 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 9.0e-111 | 1 | 329 | 340 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-125 | 1 | 280 | 281 | + 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 | 3.0e-138 | 1 | 329 | 335 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 1 | 331 | 331 | + alpha-amylase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAG52558.1 | 0 | 1 | 331 | 496 | 826 | AC010675_6 putative alpha-amylase; 60344-64829 [Arabidopsis thaliana] |
| GenBank | AAX33231.1 | 0 | 1 | 331 | 571 | 901 | plastid alpha-amylase [Malus x domestica] |
| EMBL | CBI32016.1 | 0 | 1 | 331 | 555 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 1 | 331 | 571 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 1 | 331 | 571 | 900 | alpha-amylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2qpu_C | 0 | 1 | 329 | 65 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 1 | 329 | 65 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 1 | 329 | 65 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 1 | 329 | 65 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 1 | 329 | 65 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1823 | EC-3.2.1.1 | α-amylase |
| starch degradation I | RXN-1825 | EC-3.2.1.1 | α-amylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO826981 | 332 | 1 | 332 | 0 |
| EG631183 | 332 | 1 | 332 | 0 |
| HO811991 | 299 | 34 | 332 | 0 |
| GO885960 | 284 | 26 | 309 | 0 |
| EE647363 | 267 | 43 | 309 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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