| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 492338 |
| Family | GH13 |
| Protein Properties | Length: 424 Molecular Weight: 47325.3 Isoelectric Point: 5.819 |
| Chromosome | Chromosome/Scaffold: 7 Start: 7340561 End: 7342554 |
| 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 | 40 | 345 | 2.00386e-43 |
| DGGFYNSLHNSIDDIANAGVTHLWLPPPSQSVAPEGYLPGKLYDLNSSKYGSEAELKSLIKALNQKGIKSLADIVINHRTAERKDDKCGYCYFEGGTSDD RLDWDPSFVCRNDPKFPGTGNLDTGGDFDGAPDIDHLNPRVQKELSEWMNWLKSEIGFHGWRFDYVRGYASSVTKLYVQNTSPDFAVGENWNDMKYGGDG KLDYDQNEHRSGLKQWIEEAGGGVLTAFDFTTKGILQSAVKGELWRLKDSQGKPPGLIGINPGNAVTFIDNHDTFRTWTFPSDKVLLGYVYILTHPGIPC IFYNHY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 424 Download |
| MTSLHTLLFT SLLFFIVFPA FTFSSTLLFQ SFNWESWKKD GGFYNSLHNS IDDIANAGVT 60 HLWLPPPSQS VAPEGYLPGK LYDLNSSKYG SEAELKSLIK ALNQKGIKSL ADIVINHRTA 120 ERKDDKCGYC YFEGGTSDDR LDWDPSFVCR NDPKFPGTGN LDTGGDFDGA PDIDHLNPRV 180 QKELSEWMNW LKSEIGFHGW RFDYVRGYAS SVTKLYVQNT SPDFAVGENW NDMKYGGDGK 240 LDYDQNEHRS GLKQWIEEAG GGVLTAFDFT TKGILQSAVK GELWRLKDSQ GKPPGLIGIN 300 PGNAVTFIDN HDTFRTWTFP SDKVLLGYVY ILTHPGIPCI FYNHYIEWGL KESISKLVAI 360 RNKNGIGNTS SVTIKVAESD LYVANIDDKV IMKIGPKQDV GTLVPSNFAL AYSGLDFAVW 420 EKK* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 1.0e-45 | 40 | 363 | 399 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 7.0e-122 | 33 | 423 | 395 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 3.0e-134 | 33 | 422 | 398 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-146 | 33 | 372 | 346 | + 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 | 33 | 422 | 396 | + 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 |
| GenBank | AAM64582.1 | 0 | 1 | 423 | 1 | 423 | alpha-amylase-like protein [Arabidopsis thaliana] |
| DDBJ | BAC02435.1 | 0 | 3 | 423 | 2 | 423 | alpha-amylase [Ipomoea nil] |
| EMBL | CAB36742.1 | 0 | 1 | 423 | 1 | 428 | alpha-amylase-like protein [Arabidopsis thaliana] |
| RefSeq | NP_567714.1 | 0 | 1 | 423 | 1 | 423 | AMY1 (ALPHA-AMYLASE-LIKE); alpha-amylase [Arabidopsis thaliana] |
| RefSeq | XP_002327139.1 | 0 | 3 | 422 | 2 | 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 | 27 | 422 | 2 | 402 | A Chain A, Crystal Structure Of Recombinant Ascorbate Peroxidase |
| PDB | 1ava_B | 0 | 27 | 422 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 27 | 422 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 27 | 422 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 27 | 422 | 3 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
