| Basic Information | |
|---|---|
| Species | Aquilegia coerulea |
| Cazyme ID | Aquca_002_00499.4 |
| Family | CBM45 |
| Protein Properties | Length: 649 Molecular Weight: 72816 Isoelectric Point: 7.3323 |
| Chromosome | Chromosome/Scaffold: 2 Start: 4139772 End: 4147190 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM45 | 322 | 398 | 6.7e-24 |
| VHWGVCRDNDKHWEIPATPHPPKTKIFKKNALQTLLKMKEDGRGSWGSFSLDKELKGLLFVLKLGDNTWANNMGSDF | |||
| CBM45 | 126 | 212 | 2.3e-26 |
| LHWGVNYVDDIRSEWDQPPTEMRPPGSIAIKDYAIETPLTEIPSSGDGKKLHEIQIEFQRDCPITAINFVLKDEETGIWCQHRGRDF | |||
| Full Sequence |
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| Protein Sequence Length: 649 Download |
| MSTTTTLGIV ELPLLHHHSH KQNPRFHLLQ FKNKIKHNRL NYSSSNKFIF NGGSFCNYKP 60 FKVQTVKATS TDTALVEADT VLFEETFPLK RIQKVEGKIS VKLDQVKNTD KCKLTVACDL 120 PGKWILHWGV NYVDDIRSEW DQPPTEMRPP GSIAIKDYAI ETPLTEIPSS GDGKKLHEIQ 180 IEFQRDCPIT AINFVLKDEE TGIWCQHRGR DFKVPLMDYV HDDTNIVGAK KGFSIWPGAF 240 GQLSSALVKS EGPGPKGQES TGKSEEPKKN TKRLEGFYED CPILKEVPVQ NVLKVSVRKA 300 QQKDKQFVDV HLETDIPGDV VVHWGVCRDN DKHWEIPATP HPPKTKIFKK NALQTLLKMK 360 EDGRGSWGSF SLDKELKGLL FVLKLGDNTW ANNMGSDFYI PLSIENSTDV KESESSITST 420 SAEKEAAKEA VAYTDGIIND IKNLVTGIAS EKNRKTKSKG AHALILQEIE KLAAEAYSIF 480 RSSSVITVEE DVPDATLEPP LPTSGTGSGF EVLCQGFNWE SHKSGRWYME LNEKAKELSS 540 LGFTVIWLPP PTESISPEGY MPKDLYNLNS RYGSMEELKV VVKKFHEVGM KVLGDVVLNH 600 RCAHYQNQNG IWNIYGGKLN WDDRAVVADD PHFQRLTLII HKSLCGKI* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00642 | Aamy | 2.0e-21 | 511 | 616 | 118 | + Alpha-amylase domain. | ||
| PLN00196 | PLN00196 | 5.0e-31 | 511 | 633 | 130 | + alpha-amylase; Provisional | ||
| PLN02361 | PLN02361 | 3.0e-37 | 508 | 629 | 123 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-41 | 512 | 604 | 95 | + 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 | 10 | 634 | 634 | + 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 | AAX33231.1 | 0 | 13 | 634 | 8 | 633 | plastid alpha-amylase [Malus x domestica] |
| GenBank | AAX33233.1 | 0 | 30 | 634 | 12 | 627 | plastid alpha-amylase [Actinidia chinensis] |
| EMBL | CAN69906.1 | 0 | 15 | 634 | 9 | 612 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI32016.1 | 0 | 15 | 634 | 9 | 617 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270049.1 | 0 | 15 | 634 | 9 | 633 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3bsg_A | 2e-27 | 511 | 637 | 2 | 135 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 2qps_A | 2e-27 | 511 | 637 | 2 | 135 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1rp9_A | 2e-27 | 511 | 637 | 2 | 135 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| PDB | 1rp8_A | 2e-27 | 511 | 637 | 2 | 135 | A Chain A, Crystal Structure Of Barley Alpha-Amylase Isozyme 1 (Amy1) Inactive Mutant D180a In Complex With Maltoheptaose |
| PDB | 2qpu_C | 3e-27 | 511 | 637 | 2 | 135 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631183 | 631 | 13 | 634 | 0 |
| DR942234 | 291 | 339 | 629 | 0 |
| DT730376 | 265 | 7 | 271 | 0 |
| DR923500 | 252 | 382 | 633 | 0 |
| DT730376 | 136 | 277 | 402 | 0.009 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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