| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb02g023790.1 |
| Family | GH13 |
| Protein Properties | Length: 436 Molecular Weight: 47800.8 Isoelectric Point: 4.7982 |
| Chromosome | Chromosome/Scaffold: 2 Start: 57701214 End: 57703517 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 43 | 346 | 1.1e-37 |
| SGGWYNLLMGKVDDIAAAGVTHVWLPPPSHSVSTQELGAGYMPGRLYDLDASKYGTAAELKSLIAAFHGKGVQVVADIVINHRCADYKDGGTPDGRLDWG PHMICRDDTIYSDGTANLDTGADFAAAPDIDHLNDRVQRELTDWLLWLKSDLGFDAWRFDFAKGYSAEVAKVYVDGTAPSFAVAEIWNNMAYDGNNKPEY DQDPHRQALVDWVDKVGGAASPATVFDFTTKGILNAAVEGELWRLIDPQGKAPGVIGWWPAKAVTFVDNHDTGSTQAMWPFPSDKVMQGYAYILTHPGNP CIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 436 Download |
| MGNRHLCCLS LLLLLGLASG QVLFQNREFV IVQAFNWESW KQSGGWYNLL MGKVDDIAAA 60 GVTHVWLPPP SHSVSTQELG AGYMPGRLYD LDASKYGTAA ELKSLIAAFH GKGVQVVADI 120 VINHRCADYK DGGTPDGRLD WGPHMICRDD TIYSDGTANL DTGADFAAAP DIDHLNDRVQ 180 RELTDWLLWL KSDLGFDAWR FDFAKGYSAE VAKVYVDGTA PSFAVAEIWN NMAYDGNNKP 240 EYDQDPHRQA LVDWVDKVGG AASPATVFDF TTKGILNAAV EGELWRLIDP QGKAPGVIGW 300 WPAKAVTFVD NHDTGSTQAM WPFPSDKVMQ GYAYILTHPG NPCIFYDHFF DWGFKDEIAA 360 LVAVRKRNGI TPTSELTILE HDGDSYVAEI GGKVIVKIGS RYDVGHLIPA GFEVAAHGND 420 YAVWEKAGTE QVTRA* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 7.0e-45 | 30 | 367 | 416 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 2.0e-132 | 30 | 427 | 403 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 4.0e-144 | 23 | 426 | 414 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-166 | 30 | 376 | 348 | + 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 | 0 | 30 | 427 | 407 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ADC54344.1 | 0 | 30 | 428 | 3 | 406 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| GenBank | ADC54351.1 | 0 | 30 | 426 | 3 | 404 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| EMBL | CAA09323.1 | 0 | 3 | 431 | 4 | 432 | alpha amylase [Avena fatua] |
| EMBL | CAX51372.1 | 0 | 3 | 428 | 4 | 430 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
| RefSeq | XP_002462321.1 | 0 | 1 | 435 | 1 | 435 | 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 | 1rpk_A | 0 | 30 | 426 | 3 | 404 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 1p6w_A | 0 | 30 | 426 | 3 | 404 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 1ht6_A | 0 | 30 | 426 | 3 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 3bsh_A | 0 | 30 | 428 | 3 | 406 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 3bsg_A | 0 | 30 | 428 | 3 | 406 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| 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 |
