Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00048050m |
Family | GH13 |
Protein Properties | Length: 402 Molecular Weight: 44967.8 Isoelectric Point: 6.0127 |
Chromosome | Chromosome/Scaffold: 015681 Start: 958 End: 2557 |
Description | alpha-amylase-like 2 |
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 | 78 | 312 | 1.1e-24 |
NGGWYNFLMGKVDDIAAAGITHVWLPPVSHSLAEQGYLPGHLYDLDASKYGNEAQLKSLIEAFHGKGVKVIADIVINHRTAEHQDGRGIYSMFEGGTPDS RLDWLKMDIGFNAWRLDFAKGYSADVAKIYIDNTEPSLAVVEIWTSLAYGGDGKPYYDQNAHRQELVNWVDRVGWSGPATTFDFTTKGILNVTVDGELWR LRGADGKAPDMIEWWPVKAVTFIDNHDTGSTQHMW |
Full Sequence |
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Protein Sequence Length: 402 Download |
MARTGLCVCF LAFQGLSSNL ALSQVLFQVR AARLTSSASK IHHKVFCHLS GDWTLSLCDH 60 YVPAWLHRGF NWESWKQNGG WYNFLMGKVD DIAAAGITHV WLPPVSHSLA EQGYLPGHLY 120 DLDASKYGNE AQLKSLIEAF HGKGVKVIAD IVINHRTAEH QDGRGIYSMF EGGTPDSRLD 180 WLKMDIGFNA WRLDFAKGYS ADVAKIYIDN TEPSLAVVEI WTSLAYGGDG KPYYDQNAHR 240 QELVNWVDRV GWSGPATTFD FTTKGILNVT VDGELWRLRG ADGKAPDMIE WWPVKAVTFI 300 DNHDTGSTQH MWPFPADKFY DHFFDWGLKN EIAHLVSIKD CHGIQPDSEL RIIDADADLY 360 LAEIDGKVIV KIGSRFDCGN LIPAGFQVVA HGDGYAVWEK F* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00810 | Alpha-amyl_C2 | 7.0e-27 | 341 | 400 | 60 | + 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 | 66 | 400 | 395 | + alpha-amylase | ||
PLN02361 | PLN02361 | 2.0e-103 | 66 | 400 | 397 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-112 | 69 | 350 | 315 | + 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 | 400 | 467 | + 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 | AAM09952.1 | 0 | 66 | 400 | 3 | 402 | alpha-amylase [Eleusine coracana subsp. coracana] |
DDBJ | BAD17123.1 | 0 | 66 | 401 | 28 | 428 | putative alpha-amylase precursor [Oryza sativa Japonica Group] |
RefSeq | NP_001150278.1 | 0 | 66 | 400 | 27 | 427 | alpha-amylase [Zea mays] |
RefSeq | XP_002452881.1 | 0 | 1 | 401 | 1 | 428 | hypothetical protein SORBIDRAFT_04g034150 [Sorghum bicolor] |
RefSeq | XP_002454601.1 | 0 | 10 | 400 | 11 | 427 | hypothetical protein SORBIDRAFT_04g034140 [Sorghum bicolor] |
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 | 66 | 401 | 3 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_B | 0 | 66 | 401 | 3 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 66 | 401 | 3 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 66 | 401 | 3 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1rpk_A | 0 | 66 | 400 | 4 | 404 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
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 |