| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.007G082900.4 |
| Family | GH13 |
| Protein Properties | Length: 930 Molecular Weight: 105029 Isoelectric Point: 6.1408 |
| Chromosome | Chromosome/Scaffold: 07 Start: 5918572 End: 5928342 |
| 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 | 598 | 878 | 4.9e-34 |
| LSHSGITAVWLPPPTQSVAPQGYMPSDLYNLNSSYGSVEDLKSCIEEMHSQELLALGDIVLNHRCAHKQSPNGVWNIFGGKLAWGPEAIVCDDPNFQGRG NPSSGDIFHAAPNVDHSQHFVRKDVKEWLYWLRNDIGYDGWRLDFVRGFSGTFVKEYIEASNPAFAIGEYWDSMAYEHGNLCYNQDAHRQRIVNWINATG GTSSAFDVTTKGILHSALHDQYWRLIDPQGKPTGVMGWWPSRACTFLENHDTGSTQGHWPFPRDKLTQGYAYILTHPGTVS | |||
| Full Sequence |
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| Protein Sequence Length: 930 Download |
| MGVFVLPSSA FGVLLPHFPV VSLGTPRGQF HLVLGGSSNR KRKNLLTGNW QCRPRIVVAS 60 NRDDSKDNVT DDEDGSLLGS YEMLEMKEDE LVEARKALSE VKARQAALEK ERDQLLEDFA 120 SSEAKQKEYV ASVLHDKELA VSELESTKSL FHQKLQESVK EKFALESKLV LARQDAVELA 180 VQVEKLAEVA FRQATSHILE DAKLRVSAAE TLAAESAFQI DEQIRKSTEG TIFSIIVESK 240 DAINKALDVA ENAIDEATQA VAVFTDAVNP IDVIASAQSE NIKLQGAVSD LEAQLLVSES 300 ELDRLKLELQ QAQVQANAAE LRSSNAEKAL LEFQELSRKK ALEQEEEIRS LLEKIKKEAV 360 ERKKVLSKAF KAELESIKAA VDASKEITCS RENAYMRRCE ALQRSLRTSE SALKLWRQRA 420 EMAQSLLLKE RSEKEDDEDV IYIANGGRID LLTDDDSQKW KLLSYGPRKE IPQWMARRIR 480 SIRPKFPPRK TDISKALNSN FKSLELPKLD EVWSIAQEKL REGDMLTEHV IEKEVIEKKR 540 KALERALQRK TVKWKRIPEE TKIEPGTGTG REIVFQGFNW ESWRRQWYQE LAFKAADLSH 600 SGITAVWLPP PTQSVAPQGY MPSDLYNLNS SYGSVEDLKS CIEEMHSQEL LALGDIVLNH 660 RCAHKQSPNG VWNIFGGKLA WGPEAIVCDD PNFQGRGNPS SGDIFHAAPN VDHSQHFVRK 720 DVKEWLYWLR NDIGYDGWRL DFVRGFSGTF VKEYIEASNP AFAIGEYWDS MAYEHGNLCY 780 NQDAHRQRIV NWINATGGTS SAFDVTTKGI LHSALHDQYW RLIDPQGKPT GVMGWWPSRA 840 CTFLENHDTG STQGHWPFPR DKLTQGYAYI LTHPGTVSCH QNLYMILHMG TTRTLRNICS 900 FTVCFFSLFL QMSNNGASKD GHDLDFILL* 960 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 6.0e-42 | 572 | 879 | 388 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 2.0e-122 | 572 | 875 | 317 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-145 | 573 | 876 | 308 | + 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 | 6.0e-152 | 570 | 875 | 309 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 562 | 876 | 317 | + alpha-amylase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| 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 | CBI21221.1 | 0 | 1 | 876 | 1 | 885 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_001782830.1 | 0 | 574 | 884 | 14 | 325 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_002276872.1 | 0 | 1 | 876 | 1 | 885 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324108.1 | 0 | 575 | 876 | 10 | 311 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002526120.1 | 0 | 1 | 876 | 1 | 882 | 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 | 571 | 879 | 1 | 321 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 2qps_A | 0 | 571 | 879 | 1 | 321 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1rpk_A | 0 | 571 | 879 | 1 | 321 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1p6w_A | 0 | 571 | 879 | 1 | 321 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1ht6_A | 0 | 571 | 879 | 1 | 321 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO795567 | 548 | 329 | 876 | 0 |
| HO778903 | 507 | 88 | 594 | 0 |
| HO778903 | 106 | 593 | 698 | 0 |
| CO484505 | 301 | 504 | 804 | 0 |
| GE474085 | 256 | 621 | 876 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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