| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G103055_T01 |
| Family | GH13 |
| Protein Properties | Length: 481 Molecular Weight: 53161.8 Isoelectric Point: 6.1964 |
| Chromosome | Chromosome/Scaffold: 5 Start: 209898977 End: 209901053 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 91 | 399 | 8.80001e-41 |
| NGGWYNFLMGKVDDIAEAGITHVWLPPASHSLAEQGYLPGRLYDLDASKYGNEAQLKSLIEAFHSKGVKVIADIVINHRTAEHQDGRGIYCIFEGGTPDS RLDWGPHMICSDDRAYSDGTGNPDTGADFGGAPDIDHLNPRVQQELTGWLNWLKTDVGFDAWRLDFAKGYSADVAKVYIDGTQPCFAVAEIWTSLAYGGD GKPFYDQNAHRQELVSWLDRVGGKASPATTFDFTTKGILNVAVDGELWRLRGADGKAPGLIGWWPAKAVTFVDNHDTGSTQHMWPFPADKVMQGYAYILT HPGNPSIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 481 Download |
| MHCAKATPRG QAHPACMLDY KYPAGCTGQF HPAIDSPPVH RHSSRKRQEL KNMANRGLHL 60 ALFLVLLGLS SNLAAGQILF QGFNWESWKQ NGGWYNFLMG KVDDIAEAGI THVWLPPASH 120 SLAEQGYLPG RLYDLDASKY GNEAQLKSLI EAFHSKGVKV IADIVINHRT AEHQDGRGIY 180 CIFEGGTPDS RLDWGPHMIC SDDRAYSDGT GNPDTGADFG GAPDIDHLNP RVQQELTGWL 240 NWLKTDVGFD AWRLDFAKGY SADVAKVYID GTQPCFAVAE IWTSLAYGGD GKPFYDQNAH 300 RQELVSWLDR VGGKASPATT FDFTTKGILN VAVDGELWRL RGADGKAPGL IGWWPAKAVT 360 FVDNHDTGST QHMWPFPADK VMQGYAYILT HPGNPSIFYD HFFDWGLKNE IAHLVSIRDR 420 HGIQADSELR IIEADADLYL AEIDGKVIVK IGSRYDCGHL IPEGFQVVAH GDGYAVWEKN 480 * 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-45 | 77 | 426 | 420 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 4.0e-131 | 77 | 479 | 408 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 1.0e-149 | 77 | 479 | 408 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-159 | 78 | 429 | 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 | 77 | 480 | 404 | + 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 | 53 | 479 | 1 | 426 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
| GenBank | AAM09952.1 | 0 | 77 | 479 | 1 | 402 | alpha-amylase [Eleusine coracana subsp. coracana] |
| RefSeq | NP_001150278.1 | 0 | 53 | 480 | 1 | 428 | alpha-amylase [Zea mays] |
| RefSeq | XP_002452881.1 | 0 | 53 | 479 | 1 | 427 | hypothetical protein SORBIDRAFT_04g034150 [Sorghum bicolor] |
| RefSeq | XP_002454601.1 | 0 | 53 | 480 | 1 | 428 | 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 | 77 | 479 | 1 | 402 | A Chain A, Heme Ligand Mutant Of Recombinant Horseradish Peroxidase In Complex With Benzhydroxamic Acid |
| PDB | 1ava_B | 0 | 77 | 479 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 77 | 479 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 77 | 479 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1rpk_A | 0 | 77 | 480 | 2 | 405 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
