y
Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os09g28400.1 |
Family | GH13 |
Protein Properties | Length: 441 Molecular Weight: 48867.5 Isoelectric Point: 7.311 |
Chromosome | Chromosome/Scaffold: 9 Start: 17288993 End: 17291295 |
Description | alpha-amylase-like |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 43 | 348 | 2.8026e-45 |
QGGWYNMLKDQVGDIASAGVTHVWLPPPTHSVSPQGYMPGRLYDLNASKYGTKAELKSLIAAFHAKGIKCVADIVVNHRCADDKDGRGVYCIFKGGGPRG CLDWGPSMICCDDTQYSDGTGHRDTGADFAAAPDIDHLNPLVQRELSDWLRWLRRDVGFDGWRLDFAKGYSAAVARTYVQNARPSFVVAEIWNSLSYDGD GKPAANQDGQRQELVNWVKQVGGPATAFDFTTKGILQSAVQGELWRMRDKDGKAPGMIGWYPEKAVTFVDNHDTGSTQRMWPFPSDKVILGYAYILTHPG VPCIFY |
Full Sequence |
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Protein Sequence Length: 441 Download |
MGKQMAALCG FLLVALLWLT PDVAHAQTQI LFQGFNWDSW KKQGGWYNML KDQVGDIASA 60 GVTHVWLPPP THSVSPQGYM PGRLYDLNAS KYGTKAELKS LIAAFHAKGI KCVADIVVNH 120 RCADDKDGRG VYCIFKGGGP RGCLDWGPSM ICCDDTQYSD GTGHRDTGAD FAAAPDIDHL 180 NPLVQRELSD WLRWLRRDVG FDGWRLDFAK GYSAAVARTY VQNARPSFVV AEIWNSLSYD 240 GDGKPAANQD GQRQELVNWV KQVGGPATAF DFTTKGILQS AVQGELWRMR DKDGKAPGMI 300 GWYPEKAVTF VDNHDTGSTQ RMWPFPSDKV ILGYAYILTH PGVPCIFYDH VFDWNLKQEI 360 NALAATRKRN GINAGSKLRV LAAESDMYVA MVDERVITKI GPRIDVGNII PSDFHIVAHG 420 NDYCVWEKSG LRVPEPEGRR * 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-51 | 29 | 369 | 415 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 2.0e-141 | 29 | 429 | 402 | + alpha-amylase | ||
PLN02361 | PLN02361 | 2.0e-141 | 29 | 428 | 405 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-162 | 30 | 378 | 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 | 8 | 428 | 424 | + alpha-amylase; Provisional |
Gene Ontology | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CAA39776.1 | 0 | 1 | 440 | 1 | 440 | alpha-amylase [Oryza sativa (japonica cultivar-group)] |
GenBank | EAZ09376.1 | 0 | 26 | 440 | 24 | 436 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
GenBank | EEC84703.1 | 0 | 1 | 440 | 1 | 440 | hypothetical protein OsI_31647 [Oryza sativa Indica Group] |
RefSeq | NP_001063367.1 | 0 | 1 | 440 | 1 | 440 | Os09g0457400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001063369.1 | 0 | 26 | 440 | 24 | 436 | Os09g0457800 [Oryza sativa (japonica cultivar-group)] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1bg9_A | 0 | 29 | 428 | 1 | 402 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
PDB | 1ava_B | 0 | 29 | 428 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 29 | 428 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 29 | 428 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 29 | 429 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
Metabolic Pathways | |||
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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 |