| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os06g49970.2 |
| Family | GH13 |
| Protein Properties | Length: 446 Molecular Weight: 48696 Isoelectric Point: 5.2261 |
| Chromosome | Chromosome/Scaffold: 6 Start: 30262778 End: 30266915 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 37 | 347 | 3e-38 |
| SGGWYNLLMGKVDDIVAAGVTHVWLPPPSHSVSTQGYMPGRLYDLDASRYGTSMELKSLISALHGKGIQAIADVVINHRCADYKDSRGIYCIFEGGTPDG RLDWGPHMICRDDTQFSDGTGNLDTGADFAAAPDIDHLNGVVQRELTDWLLWLKSDEVGFDAWRLDFARGYSPEVAKVYIEGTTPVGLAVAELWDSMAYG GDGKPEYNQDAHRQALVDWVDRVGGTASAGMVFDFTTKGIMNTAVEGELWRLIDQQGKAPGVIGWWPAKAVTFVDNHDTGSTQQMWPFPSDKVMQGYAYI LTHPGNPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 446 Download |
| MATGRRLSMI LLLLLLGLAS GDKILFQGFN WESWRQSGGW YNLLMGKVDD IVAAGVTHVW 60 LPPPSHSVST QGYMPGRLYD LDASRYGTSM ELKSLISALH GKGIQAIADV VINHRCADYK 120 DSRGIYCIFE GGTPDGRLDW GPHMICRDDT QFSDGTGNLD TGADFAAAPD IDHLNGVVQR 180 ELTDWLLWLK SDEVGFDAWR LDFARGYSPE VAKVYIEGTT PVGLAVAELW DSMAYGGDGK 240 PEYNQDAHRQ ALVDWVDRVG GTASAGMVFD FTTKGIMNTA VEGELWRLID QQGKAPGVIG 300 WWPAKAVTFV DNHDTGSTQQ MWPFPSDKVM QGYAYILTHP GNPCIFYDHF FDWGLKEQIA 360 ALVAVRQRNG VTATSSLKIM LHDADAYVAE IDGKVVMKIG SRYDVSSLIP PGFHLAAHGN 420 GYAVWEKIAA AAAAADHRTS SSASL* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 2.0e-43 | 24 | 389 | 436 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN02784 | PLN02784 | 4.0e-145 | 20 | 427 | 409 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 2.0e-148 | 20 | 427 | 413 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-162 | 24 | 377 | 357 | + 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 | 2 | 428 | 430 | + 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 |
| Swiss-Prot | A2YGY2 | 0 | 1 | 445 | 1 | 446 | AMY2A_ORYSI RecName: Full=Alpha-amylase isozyme 2A; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; AltName: Full=Alpha-amylase isozyme C2; Flags: Precursor |
| GenBank | AAA33894.1 | 0 | 1 | 445 | 1 | 443 | alpha-amylase [Oryza sativa Japonica Group] |
| GenBank | ADC54365.1 | 0 | 23 | 432 | 2 | 409 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
| EMBL | CAA45903.1 | 0 | 1 | 427 | 1 | 425 | alpha-amylase [Oryza sativa (indica cultivar-group)] |
| RefSeq | NP_001058568.1 | 0 | 1 | 445 | 1 | 445 | Os06g0713800 [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 | 3bsg_A | 0 | 23 | 432 | 2 | 409 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 23 | 427 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1p6w_A | 0 | 23 | 427 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1ht6_A | 0 | 23 | 427 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 3bsh_A | 0 | 23 | 432 | 2 | 409 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR 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 |
