Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00029041m |
Family | GH13 |
Protein Properties | Length: 437 Molecular Weight: 47471.5 Isoelectric Point: 4.8413 |
Chromosome | Chromosome/Scaffold: 007970 Start: 9060 End: 13199 |
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 | 44 | 347 | 3.3e-37 |
NHLMGKVDDIAAGGVTHVWLPPPSHSVSGQGYMPGRLYDLDASKYGTAAELRSLIAAFHGKGVQAVADIVINHRCADYKDSRGIYCIFEGGTPDGRLDWG PHMICRDDAQYSDGTGNLDTGAGFAAAPDIDHLNIRVRRELTEWLLWLKSDLGFDAWRLDFARGYSAAVAAAYINGTAPSLAVAEIWGDMAYGRDGRPEY DQDAHRQALVDWVDAVGGAASAAAVFDFTTKGILNAAVEGELWRLIDPRGKAPGVIGWWPAKAVTFVDNHDTGSTQAMWPFPADKVMQGYAYILTHPGNP CIFY |
Full Sequence |
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Protein Sequence Length: 437 Download |
MGSRHLCCLS TLLQLLLLLG LASGQVLFQA FNWESWKQSG GWYNHLMGKV DDIAAGGVTH 60 VWLPPPSHSV SGQGYMPGRL YDLDASKYGT AAELRSLIAA FHGKGVQAVA DIVINHRCAD 120 YKDSRGIYCI FEGGTPDGRL DWGPHMICRD DAQYSDGTGN LDTGAGFAAA PDIDHLNIRV 180 RRELTEWLLW LKSDLGFDAW RLDFARGYSA AVAAAYINGT APSLAVAEIW GDMAYGRDGR 240 PEYDQDAHRQ ALVDWVDAVG GAASAAAVFD FTTKGILNAA VEGELWRLID PRGKAPGVIG 300 WWPAKAVTFV DNHDTGSTQA MWPFPADKVM QGYAYILTHP GNPCIFYDHF FDWGFKDEIA 360 ALVAVRKRNG ITPASELTIL EYDGDAYLAE IDGKVIVKIG SRYDVSALIP AGYQVVADGN 420 DYAVWEKGAG EQVSQA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00810 | Alpha-amyl_C2 | 1.0e-26 | 367 | 427 | 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 | 4.0e-132 | 29 | 427 | 400 | + alpha-amylase | ||
PLN02361 | PLN02361 | 8.0e-134 | 28 | 427 | 405 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-147 | 28 | 377 | 353 | + 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 | 28 | 427 | 400 | + 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 | ADC54359.1 | 0 | 25 | 435 | 2 | 412 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
GenBank | ADC54365.1 | 0 | 25 | 435 | 2 | 412 | alpha amylase [Hordeum vulgare subsp. spontaneum] |
EMBL | CAA09323.1 | 0 | 3 | 434 | 4 | 434 | alpha amylase [Avena fatua] |
EMBL | CAX51372.1 | 0 | 6 | 435 | 7 | 436 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
Swiss-Prot | P00693 | 0 | 6 | 435 | 7 | 436 | AMY1_HORVU RecName: Full=Alpha-amylase type A isozyme; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; AltName: Full=AMY1; AltName: Full=Low pI alpha-amylase; Flags: Precursor |
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 | 1rpk_A | 0 | 25 | 427 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1p6w_A | 0 | 25 | 427 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1ht6_A | 0 | 25 | 427 | 2 | 404 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 3bsg_A | 0 | 25 | 435 | 2 | 412 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rp9_A | 0 | 25 | 427 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
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 |