| Basic Information | |
|---|---|
| Species | Panicum virgatum |
| Cazyme ID | Pavirv00050888m |
| Family | GH13 |
| Protein Properties | Length: 353 Molecular Weight: 38619.8 Isoelectric Point: 5.806 |
| Chromosome | Chromosome/Scaffold: 073763 Start: 1633 End: 3462 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 32 | 276 | 3.6e-34 |
| SGGWYNLLTGKVDDIAGGGVTHVWLPPASHSASADGYLPGPELKSLIAAFHSKGIQAVADIVINHRTRTARATSTPAPDIDHLNARVQRELTEWLLWLRS ELGFDAWRLDFAKGYSAEVGGVYINGTAPSWVVAEIWNSMAYGGDGKPLYNQDPHRQALVDWVDNVGGGAGASPATVFDLTTKGILNAAVEGELWRLIDP QGKAVTFIDNHDTGSTQAMWPFPSDKVMQGYAYTLTHPGTPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 353 Download |
| ALCCLSTLLL LFGLASGLVL FQAFNWESCK QSGGWYNLLT GKVDDIAGGG VTHVWLPPAS 60 HSASADGYLP GPELKSLIAA FHSKGIQAVA DIVINHRTRT ARATSTPAPD IDHLNARVQR 120 ELTEWLLWLR SELGFDAWRL DFAKGYSAEV GGVYINGTAP SWVVAEIWNS MAYGGDGKPL 180 YNQDPHRQAL VDWVDNVGGG AGASPATVFD LTTKGILNAA VEGELWRLID PQGKAVTFID 240 NHDTGSTQAM WPFPSDKVMQ GYAYTLTHPG TPCIFYDHFF DWGLKDEIAA LVAVRKRNGI 300 TPASELTILK YDGDAYVSQI DDKVIMKIGS RYDVSALIPA RYQYSYFFFA RF* 360 |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| PLN00196 | PLN00196 | 4.0e-33 | 22 | 96 | 88 | + alpha-amylase; Provisional |
| PLN02784 | PLN02784 | 8.0e-95 | 22 | 332 | 371 | + alpha-amylase |
| PLN02361 | PLN02361 | 2.0e-108 | 22 | 329 | 368 | + alpha-amylase |
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-130 | 22 | 306 | 312 | + 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. |
| PLN00196 | PLN00196 | 2.0e-143 | 110 | 343 | 245 | + alpha-amylase; Provisional |
| 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 |
| GenBank | ADC54282.1 | 0 | 19 | 345 | 3 | 393 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| GenBank | ADC54308.1 | 0 | 19 | 345 | 3 | 393 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| GenBank | ADC54327.1 | 0 | 19 | 345 | 3 | 393 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| GenBank | ADC54359.1 | 0 | 19 | 345 | 3 | 393 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| RefSeq | XP_002462321.1 | 0 | 18 | 343 | 29 | 413 | hypothetical protein SORBIDRAFT_02g023790 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3bsg_A | 0 | 19 | 345 | 3 | 393 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 19 | 345 | 3 | 393 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1p6w_A | 0 | 19 | 345 | 3 | 393 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1ht6_A | 0 | 19 | 345 | 3 | 393 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 2qpu_C | 0 | 19 | 345 | 3 | 393 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation I | RXN-1823 | EC-3.2.1.1 | α-amylase |
| starch degradation I | RXN-1825 | EC-3.2.1.1 | α-amylase |
