| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma14g39930.1 |
| Family | GH13 |
| Protein Properties | Length: 414 Molecular Weight: 47365.2 Isoelectric Point: 9.1054 |
| Chromosome | Chromosome/Scaffold: 14 Start: 48995304 End: 49001386 |
| Description | alpha-amylase-like 2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 43 | 333 | 1.8e-33 |
| NNLEGKVSDIAKAGFTSVWLPPPTHSFSPEGYTPQNLYSLNSKYGSERQLKALLQKMKQYKVRAMADIVINHRTGTTQGRGGMYNRFDGIPLGWDERAVT SDSGGLGNRSTGAIFQGFPNIDHTQDFVRKDIIGWLRWLRHEVGFQDFRFDFVKGFSPKYVKEYIEGAKPLFCVGEYWDSCNYKGSTLDYNQDSHRQRII NWIDGTGQLSTAFDFTTKGILQEAVKGNFWRLRDPQGKPPGVIGWWPSRSVTFVDNHDTGSTQAHWPFPKDHIMEGYAYILTHPGIPTVFY | |||
| Full Sequence |
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| Protein Sequence Length: 414 Download |
| MGNWSSERHQ TTQQSDLGAV LRDGKEVLLQ AFNWESNKYN WWNNLEGKVS DIAKAGFTSV 60 WLPPPTHSFS PEGYTPQNLY SLNSKYGSER QLKALLQKMK QYKVRAMADI VINHRTGTTQ 120 GRGGMYNRFD GIPLGWDERA VTSDSGGLGN RSTGAIFQGF PNIDHTQDFV RKDIIGWLRW 180 LRHEVGFQDF RFDFVKGFSP KYVKEYIEGA KPLFCVGEYW DSCNYKGSTL DYNQDSHRQR 240 IINWIDGTGQ LSTAFDFTTK GILQEAVKGN FWRLRDPQGK PPGVIGWWPS RSVTFVDNHD 300 TGSTQAHWPF PKDHIMEGYA YILTHPGIPT VFYDHFYDWG DSIREQIVKL IDVRKRQGIQ 360 SRSSVRILEA KHDLYSAVIG EKVCMKIGNG SWCPTGREWT LSTSGHNYAV WHK* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-49 | 24 | 356 | 413 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 1.0e-149 | 26 | 413 | 407 | + alpha-amylase; Provisional | ||
| PLN02784 | PLN02784 | 1.0e-161 | 24 | 413 | 397 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-166 | 27 | 365 | 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. | ||
| PLN02361 | PLN02361 | 0 | 15 | 413 | 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 | 413 | 1 | 413 | AF153828_1 alpha-amylase [Malus x domestica] |
| GenBank | AAX33234.1 | 0 | 5 | 413 | 6 | 414 | cytosolic alpha-amylase [Malus x domestica] |
| GenBank | ACU19681.1 | 0 | 1 | 413 | 1 | 413 | unknown [Glycine max] |
| RefSeq | XP_002301935.1 | 0 | 13 | 413 | 6 | 406 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002510621.1 | 0 | 18 | 413 | 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 | 413 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 2qps_A | 0 | 26 | 413 | 2 | 404 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1rpk_A | 0 | 26 | 413 | 2 | 404 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1p6w_A | 0 | 26 | 413 | 2 | 404 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1ht6_A | 0 | 26 | 413 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO780661 | 407 | 8 | 414 | 0 |
| HO798064 | 384 | 18 | 392 | 0 |
| BU103706 | 416 | 1 | 414 | 0 |
| DV704349 | 307 | 12 | 318 | 0 |
| HO798064 | 34 | 381 | 414 | 0.0000000009 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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