| Basic Information | |
|---|---|
| Species | Setaria italica |
| Cazyme ID | Si017283m |
| Family | GH13 |
| Protein Properties | Length: 428 Molecular Weight: 47500.3 Isoelectric Point: 4.9572 |
| Chromosome | Chromosome/Scaffold: 1 Start: 39019319 End: 39021025 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH13 | 39 | 346 | 8.1976e-43 |
| NGGWYNFLMGKVDDIAEAGITHVWLPPASHSLAEQGYLPGRLYDLDASRYGNEAQLKSLIEAFHDKGVKVIADIVINHRTAEHQDGRGIYCMFEGGTPDS RLDWGPHMICSDDRAYSDGTGNPDTGADFGGAPDIDHLNPRVQRELIGWLNWLKTDIGFDAWRLDFAKGYSADVAKVYIDNTEPCFAVAEIWTSLAYGGD GKPYYDQNAHRQELVNWVDRVGRSGPATTFDFTTKGILNVAVDGELWRLRGADGKAPGLIGWWPAKAVTFIDNHDTGSTQHMWPFPADKVMQGYAYILTH PGSPMIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 428 Download |
| MASKGMLLAL FIALLGLSSN SAAGQVLFQG FNWESWKQNG GWYNFLMGKV DDIAEAGITH 60 VWLPPASHSL AEQGYLPGRL YDLDASRYGN EAQLKSLIEA FHDKGVKVIA DIVINHRTAE 120 HQDGRGIYCM FEGGTPDSRL DWGPHMICSD DRAYSDGTGN PDTGADFGGA PDIDHLNPRV 180 QRELIGWLNW LKTDIGFDAW RLDFAKGYSA DVAKVYIDNT EPCFAVAEIW TSLAYGGDGK 240 PYYDQNAHRQ ELVNWVDRVG RSGPATTFDF TTKGILNVAV DGELWRLRGA DGKAPGLIGW 300 WPAKAVTFID NHDTGSTQHM WPFPADKVMQ GYAYILTHPG SPMIFYDHFF DWGLKNEIAH 360 LVSIRDRHGI QPDSELHIIE ADADLYLAEI DGKVIVKIGS RFDCEHLIPE GFHVTAHGDG 420 YAVWEKI* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 5.0e-44 | 24 | 386 | 433 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 7.0e-130 | 25 | 426 | 403 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 4.0e-148 | 25 | 426 | 407 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 9.0e-159 | 26 | 376 | 354 | + 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 | 1 | 427 | 428 | + 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 | AAA98615.1 | 0 | 1 | 427 | 1 | 427 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
| GenBank | AAM09952.1 | 0 | 25 | 427 | 1 | 403 | alpha-amylase [Eleusine coracana subsp. coracana] |
| RefSeq | NP_001150278.1 | 0 | 1 | 426 | 1 | 427 | alpha-amylase [Zea mays] |
| RefSeq | XP_002452881.1 | 0 | 1 | 427 | 1 | 428 | hypothetical protein SORBIDRAFT_04g034150 [Sorghum bicolor] |
| RefSeq | XP_002454601.1 | 0 | 1 | 426 | 1 | 427 | hypothetical protein SORBIDRAFT_04g034140 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 25 | 427 | 1 | 403 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
| PDB | 1ava_B | 0 | 25 | 427 | 1 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 25 | 427 | 1 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 25 | 427 | 1 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1rpk_A | 0 | 25 | 426 | 2 | 404 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| 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 |
