| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os02g52710.1 |
| Family | GH13 |
| Protein Properties | Length: 435 Molecular Weight: 48456.5 Isoelectric Point: 4.9052 |
| Chromosome | Chromosome/Scaffold: 2 Start: 32248279 End: 32250180 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 46 | 353 | 8.5e-40 |
| NGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVGEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDS RLDWGPHMICRDDPYGDGTGNPDTGADFAAAPDIDHLNKRVQRELIGWLDWLKMDIGFDAWRLDFAKGYSADMAKIYIDATEPSFAVAEIWTSMANGGDG KPNYDQNAHRQELVNWVDRVGGANSNATAFDFTTKGILNVAVEGELWRLRGEDGKAPGMIGWWPAKATTFVDNHDTGSTQHLWPFPSDKVMQGYAYILTH PGNPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 435 Download |
| MQVLNTMVNK HFLSLSVLIV LLGLSSNLTA GQVLFQGFNW ESWKENGGWY NFLMGKVDDI 60 AAAGITHVWL PPPSHSVGEQ GYMPGRLYDL DASKYGNEAQ LKSLIEAFHG KGVQVIADIV 120 INHRTAEHKD GRGIYCLFEG GTPDSRLDWG PHMICRDDPY GDGTGNPDTG ADFAAAPDID 180 HLNKRVQREL IGWLDWLKMD IGFDAWRLDF AKGYSADMAK IYIDATEPSF AVAEIWTSMA 240 NGGDGKPNYD QNAHRQELVN WVDRVGGANS NATAFDFTTK GILNVAVEGE LWRLRGEDGK 300 APGMIGWWPA KATTFVDNHD TGSTQHLWPF PSDKVMQGYA YILTHPGNPC IFYDHFFDWG 360 LKEEIERLVS IRNRQGIHPA SELRIMEADS DLYLAEIDGK VITKIGPRYD VEHLIPEGFQ 420 VVAHGDGYAI WEKI* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 7.0e-42 | 31 | 374 | 418 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 9.0e-139 | 32 | 433 | 403 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 4.0e-146 | 32 | 433 | 406 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-161 | 33 | 383 | 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 | 29 | 434 | 407 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005576 | extracellular region |
| 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 | AAA33885.1 | 0 | 1 | 434 | 1 | 434 | alpha-amylase (EC 3.2.1.1) [Oryza sativa] |
| DDBJ | BAD17123.1 | 0 | 7 | 434 | 1 | 428 | putative alpha-amylase precursor [Oryza sativa Japonica Group] |
| EMBL | CAA34516.1 | 0 | 7 | 434 | 1 | 428 | alpha-amylase [Oryza sativa (japonica cultivar-group)] |
| GenBank | EAY87654.1 | 0 | 7 | 434 | 1 | 428 | hypothetical protein OsI_09066 [Oryza sativa Indica Group] |
| RefSeq | NP_001048220.1 | 0 | 1 | 434 | 1 | 434 | Os02g0765600 [Oryza sativa (japonica cultivar-group)] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1bg9_A | 0 | 32 | 434 | 1 | 403 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 1ava_B | 0 | 32 | 434 | 1 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 32 | 434 | 1 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 32 | 434 | 1 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 32 | 433 | 2 | 404 | 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 |
