| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.005G139200.3 |
| Family | GH13 |
| Protein Properties | Length: 636 Molecular Weight: 71508.7 Isoelectric Point: 5.177 |
| Chromosome | Chromosome/Scaffold: 05 Start: 36288262 End: 36293991 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 264 | 554 | 9.6e-40 |
| KEKASEISSLGFTVIWLPPPTESVSPEGYLPKDLYNLNSRYGTIDELKDLVKSLHGVGLKVLGDVVLNHRCAHYQNQNGVWNIFGGRLNWDDRAVVGDDP HFQGRGNKSSGDNFHAAPNIDHSQDFVRKDLIEWLCWLREEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVD WINATNGTAGAFDVTTKGILHSALERREYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYILTHPGTPAVFY | |||
| Full Sequence |
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| Protein Sequence Length: 636 Download |
| MVLKAEASCD SKNENRRLEG FYEEQPIVKE VSVGNMVNVA IRKFPDAANI VLHLETDIPG 60 DVVVHWGVCR DDAKTWEISA VPYPPETTVF RNKALRTLLQ PTGNGSRALF TLDEKLDGFL 120 FVLKLDANSW VNFQGNDFYI PLSSARSVKG QSDSESEETS GKAHTDGIIN EIRNLVSGLN 180 SEKSLQTKVK EAKESILNEI EKLAAEAYSI FRSSTPSYPE EDSDADDAEP TINISSGTGS 240 GFEILCQGFN WESNKSGRWY MELKEKASEI SSLGFTVIWL PPPTESVSPE GYLPKDLYNL 300 NSRYGTIDEL KDLVKSLHGV GLKVLGDVVL NHRCAHYQNQ NGVWNIFGGR LNWDDRAVVG 360 DDPHFQGRGN KSSGDNFHAA PNIDHSQDFV RKDLIEWLCW LREEIGYDGW RLDFVRGFWG 420 GYVKDYLDAS EPYFAVGEYW DSLSYTYGEM DHNQDAHRQR IVDWINATNG TAGAFDVTTK 480 GILHSALERR EYWRLSDQKG KPPGVVGWWP SRAVTFIENH DTGSTQGHWR FPGGKEMQGY 540 AYILTHPGTP AVFYDHIVSH HRSEIGALIS LRNRNKIHCR SIVEIVKAER DVYAATIDDR 600 VAMKIGPGYY EPPSGPQRWS LALEGYDYKV WEASS* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02784 | PLN02784 | 0.003 | 46 | 142 | 106 | + alpha-amylase | ||
| PLN00196 | PLN00196 | 5.0e-132 | 232 | 632 | 414 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-154 | 244 | 583 | 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 | 8.0e-164 | 240 | 632 | 400 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 4 | 634 | 644 | + 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 |
| EMBL | CBI32016.1 | 0 | 1 | 634 | 237 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 1 | 634 | 237 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 10 | 634 | 259 | 900 | 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 | 2qpu_C | 0 | 243 | 632 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 243 | 632 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 243 | 632 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 243 | 632 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 243 | 632 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631183 | 641 | 8 | 634 | 0 |
| HO826981 | 401 | 234 | 634 | 0 |
| HO811991 | 298 | 337 | 634 | 0 |
| ES805448 | 328 | 201 | 527 | 0 |
| EG631183 | 138 | 19 | 142 | 0.38 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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