| Basic Information | |
|---|---|
| Species | Brachypodium distachyon |
| Cazyme ID | Bradi1g35050.1 |
| Family | GH13 |
| Protein Properties | Length: 448 Molecular Weight: 48750.2 Isoelectric Point: 5.9802 |
| Chromosome | Chromosome/Scaffold: 1 Start: 30571109 End: 30573260 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH13 | 42 | 350 | 1e-39 |
| QGGWYNMLLGKVDDIAAAGVTHVWLPPPSHSVSNEGYMPGRLYDLDASKYGSASELKSLIGALHGKGVQAIADVVINHRCADYKDSRGIYCIFEGGTADG RLDWGPHMICRDDTAYGDGTANLDTGADFAAAPDIDHLNDRVQRELTDWLLWLKSDLGFDAWRLDFAKGYSPEMAKVYIDGTKPGLAVAEVWNDMTPGGD GKPAYDQDAHRQALVNWVDRVGGKDSAGMVFDFTTKGILNVAVEGELWRLIDPQGKAPGVVGWWPAKAVTFVDNHDTGSTQAMWPFPADKVMLGYAYILT HPGTPCIFY | |||
| Full Sequence |
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| Protein Sequence Length: 448 Download |
| MGKHGSHLCC FSLLSLLLLL AGFASGHQVL FQGFNWESWK QQGGWYNMLL GKVDDIAAAG 60 VTHVWLPPPS HSVSNEGYMP GRLYDLDASK YGSASELKSL IGALHGKGVQ AIADVVINHR 120 CADYKDSRGI YCIFEGGTAD GRLDWGPHMI CRDDTAYGDG TANLDTGADF AAAPDIDHLN 180 DRVQRELTDW LLWLKSDLGF DAWRLDFAKG YSPEMAKVYI DGTKPGLAVA EVWNDMTPGG 240 DGKPAYDQDA HRQALVNWVD RVGGKDSAGM VFDFTTKGIL NVAVEGELWR LIDPQGKAPG 300 VVGWWPAKAV TFVDNHDTGS TQAMWPFPAD KVMLGYAYIL THPGTPCIFY DHFFNWGFKE 360 EIAALVAVRK RNGITATSAL RILMHDGDAY VAEVDGKVVV KIGSRYDVAA VIPSGFVTTA 420 HGKDYAVWEK AGVAAAAGFQ RSRRSLD* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 3.0e-45 | 26 | 371 | 417 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 3.0e-138 | 26 | 430 | 406 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 3.0e-143 | 26 | 430 | 410 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 7.0e-164 | 29 | 380 | 355 | + 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 | 28 | 430 | 403 | + 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:0009250 | glucan biosynthetic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAA32927.1 | 0 | 1 | 442 | 1 | 438 | alpha-amylase 2 [Hordeum vulgare] |
| GenBank | ADC54353.1 | 0 | 27 | 442 | 1 | 414 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| EMBL | CAA72144.1 | 0 | 1 | 442 | 1 | 437 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
| EMBL | CAX51372.1 | 0 | 1 | 442 | 1 | 438 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
| Swiss-Prot | P00693 | 0 | 1 | 442 | 1 | 438 | AMY1_HORVU RecName: Full=Alpha-amylase type A isozyme; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; AltName: Full=AMY1; AltName: Full=Low pI alpha-amylase; Flags: Precursor |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3bsg_A | 0 | 27 | 442 | 1 | 414 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 3bsh_A | 0 | 27 | 442 | 1 | 414 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 1rpk_A | 0 | 27 | 430 | 1 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 1p6w_A | 0 | 27 | 430 | 1 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
| PDB | 1ht6_A | 0 | 27 | 430 | 1 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| 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 |
