| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_023754m |
| Family | GH13 |
| Protein Properties | Length: 425 Molecular Weight: 46962.8 Isoelectric Point: 4.5007 |
| Chromosome | Chromosome/Scaffold: 08265 Start: 1004648 End: 1006218 |
| Description | alpha-amylase-like |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 41 | 343 | 1.50001e-40 |
| WYNSLKNMIPDLANAGVTHVWLPPPSQSAAPQGYLPGRLYDLNASKYGTQDELVSLIDSFHQKGIKSLADIVINHRTAEKKDDRGIYCIFEGGTPDGTLD WGPSFICRDDTAYSDGQGNPDTGEDFKGAPDIDHLNPRVQIELSDWMNWLKTEIGFVGFRFDFVKGYAPSITKLYMEETLPEFAVGEKWDSLAYGQDGKP DPNQDGHRVALEDWIQAAGGAVTAFDFTTKGILQAAVQGELWRLKDSNGKPSGLIGLFPQNAVTFIDNHDTGSTQNLWPFPSDKVILGYAYILTHPGIPS IFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 425 Download |
| MNFLSPLCVL SFLLFVFPSF ISSQLLFQGF NWESCNKAEG WYNSLKNMIP DLANAGVTHV 60 WLPPPSQSAA PQGYLPGRLY DLNASKYGTQ DELVSLIDSF HQKGIKSLAD IVINHRTAEK 120 KDDRGIYCIF EGGTPDGTLD WGPSFICRDD TAYSDGQGNP DTGEDFKGAP DIDHLNPRVQ 180 IELSDWMNWL KTEIGFVGFR FDFVKGYAPS ITKLYMEETL PEFAVGEKWD SLAYGQDGKP 240 DPNQDGHRVA LEDWIQAAGG AVTAFDFTTK GILQAAVQGE LWRLKDSNGK PSGLIGLFPQ 300 NAVTFIDNHD TGSTQNLWPF PSDKVILGYA YILTHPGIPS IFYDHFFDWG LKEEISKLAT 360 IRNNYKIDST SSVDILAADS DLYVAAINDN IIVKIGPKND LGSLIPSNFQ VVASGKDYAV 420 WAKN* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 7.0e-52 | 24 | 365 | 411 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 3.0e-137 | 24 | 423 | 401 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 3.0e-148 | 24 | 423 | 405 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-156 | 26 | 373 | 351 | + 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 | 24 | 424 | 404 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005975 | carbohydrate metabolic process |
| GO:0043169 | cation binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PRF/SEQDB | 0 | 1 | 421 | 1 | 420 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
| DDBJ | BAC76729.1 | 0 | 1 | 421 | 1 | 420 | alpha-amylase [Vigna angularis] |
| RefSeq | XP_002301187.1 | 0 | 25 | 423 | 5 | 403 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002327139.1 | 0 | 1 | 423 | 1 | 423 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002510218.1 | 0 | 1 | 424 | 1 | 421 | 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 | 1bg9_A | 0 | 24 | 423 | 1 | 402 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
| PDB | 1ava_B | 0 | 24 | 423 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 24 | 423 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 24 | 423 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 24 | 424 | 2 | 405 | 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 |
