| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01031746001 |
| Family | GH13 |
| Protein Properties | Length: 426 Molecular Weight: 47779.5 Isoelectric Point: 6.7955 |
| Chromosome | Chromosome/Scaffold: 3 Start: 4012517 End: 4015118 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 38 | 343 | 3.40516e-43 |
| EGGWYNFLINSIPELAASGITHVWLPPPSQSVSPEGYMPGRLYDLNASKYGTQDELKTLIKVFHSKGVQCIADIVINHRTAEKQDARGIWAIFEGGTPDD RLDWTPSFICKDDTPYSDGTGNPDSGDDYSAAPDIDHINPRVQQELIDWMNWLKIEIGFDGWRFDFARGFSPAFTKFYMAKTRPKFAVGEIWKSLSYRSD GKPSYNQDSHRRELVEWVRGAGGAVNAFDFTTKGILQAAVEGELWRMKDLNGKPPGMIGLMPGNAVTFIDNHDTGSTLQHWPFPSDKVMQGYAYILTHPG IPSIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 426 Download |
| MDIATSLSCL LFFITILPAL TASPILFQGF NWESSKKEGG WYNFLINSIP ELAASGITHV 60 WLPPPSQSVS PEGYMPGRLY DLNASKYGTQ DELKTLIKVF HSKGVQCIAD IVINHRTAEK 120 QDARGIWAIF EGGTPDDRLD WTPSFICKDD TPYSDGTGNP DSGDDYSAAP DIDHINPRVQ 180 QELIDWMNWL KIEIGFDGWR FDFARGFSPA FTKFYMAKTR PKFAVGEIWK SLSYRSDGKP 240 SYNQDSHRRE LVEWVRGAGG AVNAFDFTTK GILQAAVEGE LWRMKDLNGK PPGMIGLMPG 300 NAVTFIDNHD TGSTLQHWPF PSDKVMQGYA YILTHPGIPS IFYDHFFEWG LKEEIMKLII 360 IRSRNRIKPN SAVRILASDS DLYVAAIDGK IIVKIGPRFD VGNLVPKSFK KIATSGKDYC 420 VWEKK* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-51 | 24 | 364 | 412 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 3.0e-149 | 25 | 425 | 405 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 2.0e-150 | 25 | 424 | 404 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 7.0e-159 | 25 | 373 | 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 | 6 | 424 | 422 | + 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 |
| EMBL | CAN74301.1 | 0 | 1 | 399 | 1 | 399 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN74301.1 | 3e-37 | 342 | 425 | 414 | 497 | hypothetical protein [Vitis vinifera] |
| EMBL | CAN77038.1 | 0 | 1 | 425 | 1 | 442 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002282184.1 | 0 | 1 | 425 | 1 | 425 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002285213.1 | 0 | 1 | 425 | 1 | 424 | PREDICTED: hypothetical protein [Vitis vinifera] |
| 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 | 2 | 402 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 1ava_B | 0 | 25 | 424 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 25 | 424 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 25 | 424 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 25 | 425 | 3 | 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 |
