| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.008G182600.4 |
| Family | CBM45 |
| Protein Properties | Length: 764 Molecular Weight: 85800 Isoelectric Point: 6.2768 |
| Chromosome | Chromosome/Scaffold: 08 Start: 46044569 End: 46052878 |
| 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 |
| CBM45 | 125 | 208 | 1.2e-26 |
| LHWGVSYLGDSGSEWDQPPKGMRPPGSIPIKDYAIETPLKKLSEGDIFHEVKIDFNPISEIAAIHFVLKDEETGAWYQHRGMDF | |||
| GH13 | 524 | 727 | 1.1e-30 |
| KASEISSLGFTVIWLPPPTESVSPEGYMPKDLYNLNSRYGTIDELKELVKSLHEVGMKVLGDVVLNHRCAHFKNQNGVWNIFGGRLNWDDRAVVADDPHF QGRGNKSSGDNFHAAPNIDHSQEFVRKDLKEWLGWLREEIGYDGWRLDFVRGFWGGYVKDYLEASGPYFAVGEYWDSLSYTYGEMDHNQDSHRQRIVDWI NATN | |||
| Full Sequence |
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| Protein Sequence Length: 764 Download |
| MAAVTIDSLL QNPTLLFRPK AKVLLKPPRS LDCSRNRKLP LSRGSCLCSF NPRRTIHVVR 60 ASSSETALIG NFDISSSDDI LYKDIFPVKR IEKVEGKFFI RLDRSKDQHD WQFTVGCSLP 120 GKWILHWGVS YLGDSGSEWD QPPKGMRPPG SIPIKDYAIE TPLKKLSEGD IFHEVKIDFN 180 PISEIAAIHF VLKDEETGAW YQHRGMDFKV PLVDYLEDDG NIVGAKRGFG VWSGALQQFS 240 NVLLKSEASH ADSQNNSIES KDSKNKNRCL EGFYEEQSIV KEVSVGNLVS VAVRKSPETG 300 KVVVCLETDI PGDVVVHWGV CRDDAKIWKI PAAPYPPETT VFKNKALRTL LQPKATGNRS 360 GALFTLDEEH FGFLFVLKLD DNTWLKFKEN DFYVPLLGTS SVPGQYGQSD STSEEISSKS 420 YTDGIINEIR NLVSGLSSEK SLKTKKKEVQ ESILQEIEQL AAEAYSIFRS SITTVPDEVV 480 SETETTKPAV KISSGTGTGF EILCQGFNWE SHKSRRWYME LKEKASEISS LGFTVIWLPP 540 PTESVSPEGY MPKDLYNLNS RYGTIDELKE LVKSLHEVGM KVLGDVVLNH RCAHFKNQNG 600 VWNIFGGRLN WDDRAVVADD PHFQGRGNKS SGDNFHAAPN IDHSQEFVRK DLKEWLGWLR 660 EEIGYDGWRL DFVRGFWGGY VKDYLEASGP YFAVGEYWDS LSYTYGEMDH NQDSHRQRIV 720 DWINATNGTA GAFDVTTKGI LHSLCPQTGN HYLMFLILGS GKM* 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 6.0e-40 | 501 | 735 | 304 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 4.0e-72 | 492 | 742 | 263 | + alpha-amylase; Provisional | ||
| PLN02361 | PLN02361 | 2.0e-96 | 499 | 745 | 250 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-105 | 502 | 745 | 246 | + 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 | 0 | 1 | 743 | 752 | + 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 |
| GenBank | AAX33233.1 | 0 | 40 | 743 | 38 | 746 | plastid alpha-amylase [Actinidia chinensis] |
| EMBL | CAN69906.1 | 0 | 1 | 743 | 1 | 731 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI32016.1 | 0 | 1 | 743 | 1 | 736 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 1 | 743 | 1 | 752 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002520134.1 | 0 | 6 | 743 | 1 | 752 | 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 | 501 | 743 | 2 | 256 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 2qps_A | 0 | 501 | 743 | 2 | 256 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1rpk_A | 0 | 501 | 743 | 2 | 256 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1p6w_A | 0 | 501 | 743 | 2 | 256 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1ht6_A | 0 | 501 | 743 | 2 | 256 | 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 |
| EG631183 | 759 | 1 | 743 | 0 |
| ES805448 | 286 | 458 | 743 | 0 |
| GR441435 | 289 | 449 | 737 | 0 |
| CO132753 | 282 | 241 | 522 | 0 |
| EV551363 | 270 | 467 | 736 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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