| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.005G139200.2 |
| Family | GH13 |
| Protein Properties | Length: 643 Molecular Weight: 72435.7 Isoelectric Point: 5.4117 |
| Chromosome | Chromosome/Scaffold: 05 Start: 36287705 End: 36293693 |
| 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 | 271 | 561 | 9.90001e-40 |
| KEKASEISSLGFTVIWLPPPTESVSPEGYLPKDLYNLNSRYGTIDELKDLVKSLHGVGLKVLGDVVLNHRCAHYQNQNGVWNIFGGRLNWDDRAVVGDDP HFQGRGNKSSGDNFHAAPNIDHSQDFVRKDLIEWLCWLREEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVD WINATNGTAGAFDVTTKGILHSALERREYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYILTHPGTPAVFY | |||
| Full Sequence |
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| Protein Sequence Length: 643 Download |
| MIHTKRSFGK WPEASCDSKN ENRRLEGFYE EQPIVKEVSV GNMVNVAIRK FPDAANIVLH 60 LETDIPGDVV VHWGVCRDDA KTWEISAVPY PPETTVFRNK ALRTLLQPTG NGSRALFTLD 120 EKLDGFLFVL KLDANSWVNF QGNDFYIPLS SARSVKGQSD SESEETSGKA HTDGIINEIR 180 NLVSGLNSEK SLQTKVKEAK ESILNEIEKL AAEAYSIFRS STPSYPEEDS DADDAEPTIN 240 ISSGTGSGFE ILCQGFNWES NKSGRWYMEL KEKASEISSL GFTVIWLPPP TESVSPEGYL 300 PKDLYNLNSR YGTIDELKDL VKSLHGVGLK VLGDVVLNHR CAHYQNQNGV WNIFGGRLNW 360 DDRAVVGDDP HFQGRGNKSS GDNFHAAPNI DHSQDFVRKD LIEWLCWLRE EIGYDGWRLD 420 FVRGFWGGYV KDYLDASEPY FAVGEYWDSL SYTYGEMDHN QDAHRQRIVD WINATNGTAG 480 AFDVTTKGIL HSALERREYW RLSDQKGKPP GVVGWWPSRA VTFIENHDTG STQGHWRFPG 540 GKEMQGYAYI LTHPGTPAVF YDHIVSHHRS EIGALISLRN RNKIHCRSIV EIVKAERDVY 600 AATIDDRVAM KIGPGYYEPP SGPQRWSLAL EGYDYKVWEA SS* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02784 | PLN02784 | 0.003 | 53 | 149 | 106 | + alpha-amylase | ||
| PLN00196 | PLN00196 | 1.0e-131 | 239 | 639 | 414 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-154 | 251 | 590 | 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 | 5.0e-163 | 247 | 639 | 400 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 12 | 641 | 643 | + 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 | 6 | 641 | 240 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 6 | 641 | 240 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 17 | 641 | 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 | 250 | 639 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 250 | 639 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 250 | 639 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 250 | 639 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 250 | 639 | 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 | 15 | 641 | 0 |
| HO826981 | 401 | 241 | 641 | 0 |
| HO811991 | 298 | 344 | 641 | 0 |
| ES805448 | 328 | 208 | 534 | 0 |
| EG631183 | 138 | 26 | 149 | 0.41 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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