y
Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00007311m |
Family | GH13 |
Protein Properties | Length: 353 Molecular Weight: 38894.3 Isoelectric Point: 9.7717 |
Chromosome | Chromosome/Scaffold: 044460 Start: 2657 End: 3967 |
Description | alpha-amylase-like |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 82 | 269 | 2e-24 |
TGHPDTGADFAAAPDIDHLNPRVQRELSEWLAWLQKGVGFDGWRLDFAKGYSPAVARAYVRSARPGFVVAEIWSSLSYDGDGKPAASQDDKRRELVSWVR EVGGPAATAFDFPTKGVLQAAVQGELWRMRDKDGRAPGMIGWLPEKAVTFVDNHDTGSTQRMWPFPADKVMQGYAYILTHPGIPCIFY |
Full Sequence |
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Protein Sequence Length: 353 Download |
MDKQLVALSA LVAAFLFLAP DVHAQTTTQI LFQAGRLVQR AQGPGGRHRR RRRHARLAAP 60 ALALDWGPGM VCRDDTSYSD GTGHPDTGAD FAAAPDIDHL NPRVQRELSE WLAWLQKGVG 120 FDGWRLDFAK GYSPAVARAY VRSARPGFVV AEIWSSLSYD GDGKPAASQD DKRRELVSWV 180 REVGGPAATA FDFPTKGVLQ AAVQGELWRM RDKDGRAPGM IGWLPEKAVT FVDNHDTGST 240 QRMWPFPADK VMQGYAYILT HPGIPCIFYD HVFDWNLKRE ITALAAVRRR NGIKAGSKLR 300 ILAAESDLYV AMVDERVVAK IGPRFDVGGV IPQGFKVAAH GDGYCVWEKS RR* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00810 | Alpha-amyl_C2 | 3.0e-29 | 289 | 349 | 61 | + Alpha-amylase C-terminal beta-sheet domain. This entry represents the beta-sheet domain that is found in several alpha-amylases, usually at the C-terminus. This domain is organised as a five-stranded anti-parallel beta-sheet. | ||
PLN02784 | PLN02784 | 2.0e-86 | 65 | 350 | 287 | + alpha-amylase | ||
PLN02361 | PLN02361 | 6.0e-102 | 76 | 349 | 279 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-105 | 85 | 299 | 216 | + 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 | 3.0e-165 | 65 | 349 | 287 | + 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:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAA33886.1 | 0 | 64 | 349 | 139 | 423 | alpha-amylase (EC 3.2.1.1) [Oryza sativa] |
GenBank | AAA33895.1 | 0 | 64 | 349 | 140 | 424 | alpha-amylase [Oryza sativa Japonica Group] |
EMBL | CAA39776.1 | 0 | 60 | 350 | 140 | 429 | alpha-amylase [Oryza sativa (japonica cultivar-group)] |
GenBank | EEC84703.1 | 0 | 60 | 350 | 140 | 429 | hypothetical protein OsI_31647 [Oryza sativa Indica Group] |
RefSeq | NP_001063367.1 | 0 | 60 | 350 | 140 | 429 | Os09g0457400 [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 | 58 | 349 | 110 | 402 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1ava_B | 0 | 58 | 349 | 110 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 58 | 349 | 110 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 58 | 349 | 110 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 64 | 350 | 117 | 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 |