| Basic Information | |
|---|---|
| Species | Cucumis sativus |
| Cazyme ID | Cucsa.271900.2 |
| Family | GH13 |
| Protein Properties | Length: 411 Molecular Weight: 46814.6 Isoelectric Point: 6.6944 |
| Chromosome | Chromosome/Scaffold: 02500 Start: 657783 End: 662842 |
| Description | alpha-amylase-like 2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 46 | 333 | 2.3e-30 |
| ESKVHDIAKSGFTSAWLPPPTHSIAPQGYLPQNLYSLNSSYGSEDMLKTLLLKMKQCKVRAIADIVINHRVGTVVGHGGMHNRFDGILLPWNEYAVTSCS GGLGNRSTGDNFHGVPNIDHTQPFVRRDIIAWLKWLRSSVGFQDFRFDFARGFSAKFVKEYIEAGKPMLSIGEYWDSCNYNGHDLDYNQDGHRQRIINWI DGTGQLSAAFDFTTKGVLQEAVRRQLWRLRDCQGKPPGVMGWWPSRAVTFLDNHDTGSTQAHWPFPANHIMEGYAYILTHPGIPTVFY | |||
| Full Sequence |
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| Protein Sequence Length: 411 Download |
| MGDHDNVFDE SYEKTDTGAV IRNGREILFQ AFSWESHKYD WWENLESKVH DIAKSGFTSA 60 WLPPPTHSIA PQGYLPQNLY SLNSSYGSED MLKTLLLKMK QCKVRAIADI VINHRVGTVV 120 GHGGMHNRFD GILLPWNEYA VTSCSGGLGN RSTGDNFHGV PNIDHTQPFV RRDIIAWLKW 180 LRSSVGFQDF RFDFARGFSA KFVKEYIEAG KPMLSIGEYW DSCNYNGHDL DYNQDGHRQR 240 IINWIDGTGQ LSAAFDFTTK GVLQEAVRRQ LWRLRDCQGK PPGVMGWWPS RAVTFLDNHD 300 TGSTQAHWPF PANHIMEGYA YILTHPGIPT VFYDHLYEWG DSVHDEIIDI RKHQDINSRS 360 SVKILEARSD LYSAIIGEKL CMKIGDGSWC PSGTEWTLAT SGWRYAVWQK * 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 1.0e-36 | 23 | 353 | 419 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 1.0e-130 | 26 | 410 | 407 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-153 | 27 | 362 | 343 | + 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. | ||
| PLN02784 | PLN02784 | 1.0e-156 | 23 | 410 | 398 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 0 | 15 | 410 | 401 | + alpha-amylase | ||
| 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 | AAF63239.1 | 0 | 1 | 410 | 1 | 413 | AF153828_1 alpha-amylase [Malus x domestica] |
| GenBank | AAX33234.1 | 0 | 10 | 410 | 11 | 414 | cytosolic alpha-amylase [Malus x domestica] |
| RefSeq | NP_177740.1 | 0 | 1 | 410 | 1 | 413 | AMY2 (ALPHA-AMYLASE-LIKE 2); alpha-amylase/ calcium ion binding / catalytic/ cation binding [Arabidopsis thaliana] |
| RefSeq | XP_002301935.1 | 0 | 13 | 410 | 6 | 406 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002510621.1 | 0 | 18 | 410 | 3 | 398 | 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 | 3bsg_A | 0 | 26 | 410 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 26 | 410 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1p6w_A | 0 | 26 | 410 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1ht6_A | 0 | 26 | 410 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 2qps_A | 0 | 26 | 410 | 2 | 404 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO780661 | 406 | 9 | 411 | 0 |
| BU103706 | 412 | 5 | 411 | 0 |
| HO798064 | 369 | 19 | 384 | 0 |
| DV704349 | 306 | 13 | 318 | 0 |
| HO798064 | 34 | 378 | 411 | 0.000004 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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