| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_008126m |
| Family | GH13 |
| Protein Properties | Length: 430 Molecular Weight: 48230.1 Isoelectric Point: 4.9425 |
| Chromosome | Chromosome/Scaffold: 11195 Start: 15937 End: 19475 |
| Description | alpha-amylase-like |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 39 | 344 | 4.4e-38 |
| EGGWYNFLRNSIPELASSGITHVWLPPSSHSVSAEGYLPGRLYDLNASQYGNQDDLKALIRAFHNVGIQCIADIVINHRCAEKQDDRGIWSIFEGGTPDD RLDWGPSFICSDDTLYSDGKGNPDTGADFNAAPDIDHINLRVQRELSDWMNWLKNEIGFDGWRFDFARGYSPSFTKIYVANTKPSFAVGEIWKDLAYGND GKPEYNQDAHRLDIVEWIRVAGEDVTAFDFTTKGILQAAIEGELWRLNDSNGGPPGVIGLLPGSSVTFIDNHDTGSTQNHWPFPSDKIMQGYAYILTHPG IPSIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 430 Download |
| MGVIGASLSF LILTLSFWTN MSSSQILFQG FNWESWKKEG GWYNFLRNSI PELASSGITH 60 VWLPPSSHSV SAEGYLPGRL YDLNASQYGN QDDLKALIRA FHNVGIQCIA DIVINHRCAE 120 KQDDRGIWSI FEGGTPDDRL DWGPSFICSD DTLYSDGKGN PDTGADFNAA PDIDHINLRV 180 QRELSDWMNW LKNEIGFDGW RFDFARGYSP SFTKIYVANT KPSFAVGEIW KDLAYGNDGK 240 PEYNQDAHRL DIVEWIRVAG EDVTAFDFTT KGILQAAIEG ELWRLNDSNG GPPGVIGLLP 300 GSSVTFIDNH DTGSTQNHWP FPSDKIMQGY AYILTHPGIP SIFYDHFFDW GLKEEISKLI 360 AIRTRNHIRP KSVLRILVSD ADLYVAVVDE KIIAQIGPRS DIGNLVPPTF QLTASGQDYT 420 VWEKKNIRR* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 4.0e-43 | 25 | 363 | 410 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 6.0e-138 | 22 | 425 | 409 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 8.0e-141 | 25 | 424 | 405 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-150 | 26 | 374 | 352 | + 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. | ||
| PLN00196 | PLN00196 | 0 | 7 | 424 | 421 | + alpha-amylase; Provisional | ||
| 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 | AAX33232.1 | 0 | 29 | 425 | 7 | 393 | secreted alpha-amylase [Malus x domestica] |
| EMBL | CAN77038.1 | 0 | 4 | 425 | 3 | 442 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002282184.1 | 0 | 4 | 425 | 3 | 425 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002285213.1 | 0 | 4 | 425 | 3 | 424 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002327139.1 | 0 | 7 | 424 | 5 | 423 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 25 | 424 | 1 | 402 | A Chain A, The Crystal Structure Of Rice (Oryza Sativa L.) Os4bglu12 |
| PDB | 1ava_B | 0 | 25 | 424 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 25 | 424 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 25 | 424 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 25 | 424 | 2 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| 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 |
