| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT4G25000.1 |
| Family | GH13 |
| Protein Properties | Length: 424 Molecular Weight: 47377.6 Isoelectric Point: 5.8227 |
| Chromosome | Chromosome/Scaffold: 4 Start: 12851969 End: 12853845 |
| Description | alpha-amylase precursor, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 40 | 345 | 2.90069e-43 |
| EGGFYNSLHNSIDDIANAGITHLWLPPPSQSVAPEGYLPGKLYDLNSSKYGSEAELKSLIKALNQKGIKALADIVINHRTAERKDDKCGYCYFEGGTSDD RLDWDPSFVCRNDPKFPGTGNLDTGGDFDGAPDIDHLNPRVQKELSEWMNWLKTEIGFHGWRFDYVRGYASSITKLYVQNTSPDFAVGEKWDDMKYGGDG KLDYDQNEHRSGLKQWIEEAGGGVLTAFDFTTKGILQSAVKGELWRLKDSQGKPPGMIGIMPGNAVTFIDNHDTFRTWVFPSDKVLLGYVYILTHPGTPC IFYNHY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 424 Download |
| MTSLHTLLFS SLLFFIVFPT FTFSSTLLFQ SFNWESWKKE GGFYNSLHNS IDDIANAGIT 60 HLWLPPPSQS VAPEGYLPGK LYDLNSSKYG SEAELKSLIK ALNQKGIKAL ADIVINHRTA 120 ERKDDKCGYC YFEGGTSDDR LDWDPSFVCR NDPKFPGTGN LDTGGDFDGA PDIDHLNPRV 180 QKELSEWMNW LKTEIGFHGW RFDYVRGYAS SITKLYVQNT SPDFAVGEKW DDMKYGGDGK 240 LDYDQNEHRS GLKQWIEEAG GGVLTAFDFT TKGILQSAVK GELWRLKDSQ GKPPGMIGIM 300 PGNAVTFIDN HDTFRTWVFP SDKVLLGYVY ILTHPGTPCI FYNHYIEWGL KESISKLVAI 360 RNKNGIGSTS SVTIKAAEAD LYLAMIDDKV 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-43 | 40 | 370 | 406 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 4.0e-119 | 33 | 423 | 395 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 3.0e-129 | 33 | 422 | 398 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-139 | 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:0005576 | extracellular region |
| 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 | AAM64582.1 | 0 | 1 | 423 | 1 | 423 | alpha-amylase-like protein [Arabidopsis thaliana] |
| 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_002301187.1 | 0 | 26 | 423 | 4 | 404 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002327139.1 | 0 | 1 | 422 | 1 | 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 At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
| 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 |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1823 | EC-3.2.1.1 | alpha-amylase |
| starch degradation I | RXN-1825 | EC-3.2.1.1 | alpha-amylase |
