| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os08g36900.1 |
| Family | GH13 |
| Protein Properties | Length: 438 Molecular Weight: 48707.6 Isoelectric Point: 5.3655 |
| Chromosome | Chromosome/Scaffold: 8 Start: 23335165 End: 23337151 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 40 | 345 | 1.59748e-43 |
| QGGWYNFLHEKVEEIASTGATHVWLPPPSHSVSPQGYMPGRLYDLDASKYGTEAELKSLIEAFHDKNVECLADIVINHRCADYKDSRGVYCVFEGGTPDG RLDWGPDMICSDDTQYSNGRGHRDTGAGFGAAPDIDHLNPRVQRELTDWLNWLRTDLGFDGWRLDFAKGYSAPLARIYVDNTNPTFVVGEIWSSLIYNGD GKPSTNQDADRQELVNWVEGVGKPATAFDFTTKGILQAAVQGELWRLHDGNGKAPGLMGWMPDQAVTFVDNHDTGSTQSLWPFPSDKVMQGYAYILTHPG IPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 438 Download |
| MGKHHVTLCC VVFAVLCLAS SLAQAQVLFQ GFNWESWRKQ GGWYNFLHEK VEEIASTGAT 60 HVWLPPPSHS VSPQGYMPGR LYDLDASKYG TEAELKSLIE AFHDKNVECL ADIVINHRCA 120 DYKDSRGVYC VFEGGTPDGR LDWGPDMICS DDTQYSNGRG HRDTGAGFGA APDIDHLNPR 180 VQRELTDWLN WLRTDLGFDG WRLDFAKGYS APLARIYVDN TNPTFVVGEI WSSLIYNGDG 240 KPSTNQDADR QELVNWVEGV GKPATAFDFT TKGILQAAVQ GELWRLHDGN GKAPGLMGWM 300 PDQAVTFVDN HDTGSTQSLW PFPSDKVMQG YAYILTHPGI PCIFYDHVFD WNLQHEIATL 360 AEIRSRNGIH AESTLDILKA EGDIYVAMID GKVITKLGPR YDAGGIIPSD FHVVAHGNDY 420 CVWEKEGLRV PAGRKHY* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 8.0e-44 | 24 | 366 | 411 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02361 | PLN02361 | 4.0e-147 | 26 | 425 | 405 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 2.0e-148 | 26 | 425 | 401 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-160 | 27 | 375 | 352 | + 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 | 425 | 429 | + 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 |
| PIR | 0 | 1 | 437 | 1 | 437 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
| EMBL | CAA39778.1 | 0 | 1 | 436 | 1 | 437 | alpha-amylase [Oryza sativa (japonica cultivar-group)] |
| GenBank | EAZ09376.1 | 0 | 1 | 436 | 1 | 437 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
| RefSeq | NP_001062023.1 | 0 | 1 | 437 | 1 | 437 | Os08g0473600 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001063369.1 | 0 | 1 | 436 | 1 | 437 | Os09g0457800 [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 | 2qpu_C | 0 | 26 | 426 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 26 | 426 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 26 | 426 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 1bg9_A | 0 | 26 | 425 | 1 | 402 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 1ava_B | 0 | 26 | 425 | 1 | 402 | 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 |
