Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00022620m |
Family | GH13 |
Protein Properties | Length: 249 Molecular Weight: 27623 Isoelectric Point: 5.284 |
Chromosome | Chromosome/Scaffold: 002837 Start: 71 End: 1307 |
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 | 36 | 237 | 6.1e-31 |
KQGGWYNSLKAQVDDIVKAGVTHVWLPPPSHSVSPQGYMPGRLYDLDASQYGTAAELKSLIAAFHGRGIQCVADIVINHRCAEKKDARGVYCIFEGGTPD DRLDWGPAMICSDDTQYSDGTGHRDTGEGFGAAPDVDHLNARVQRELTDWLNWLKSDVGFDGWRLDFAKGYSPAIASMYVENTKPSFVVAEIWNSLSYTD GK |
Full Sequence |
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Protein Sequence Length: 249 Download |
MKHSSSLCLL FFLVALCSLV QAQVLFQGFN WESYKKQGGW YNSLKAQVDD IVKAGVTHVW 60 LPPPSHSVSP QGYMPGRLYD LDASQYGTAA ELKSLIAAFH GRGIQCVADI VINHRCAEKK 120 DARGVYCIFE GGTPDDRLDW GPAMICSDDT QYSDGTGHRD TGEGFGAAPD VDHLNARVQR 180 ELTDWLNWLK SDVGFDGWRL DFAKGYSPAI ASMYVENTKP SFVVAEIWNS LSYTDGKPSA 240 NQDQCRQEL |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 6.0e-29 | 21 | 230 | 282 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02361 | PLN02361 | 1.0e-59 | 23 | 247 | 227 | + alpha-amylase | ||
PLN02784 | PLN02784 | 2.0e-69 | 23 | 249 | 227 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 3.0e-87 | 24 | 249 | 228 | + 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 | 2.0e-144 | 2 | 249 | 250 | + alpha-amylase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
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 | ACN34260.1 | 0 | 19 | 249 | 25 | 258 | unknown [Zea mays] |
DDBJ | BAD73797.1 | 0 | 17 | 249 | 20 | 253 | putative alpha-amylase isozyme 3E precursor [Oryza sativa Japonica Group] |
GenBank | EEC83728.1 | 0 | 17 | 249 | 20 | 253 | hypothetical protein OsI_29570 [Oryza sativa Indica Group] |
RefSeq | NP_001062024.1 | 0 | 17 | 249 | 60 | 293 | Os08g0473900 [Oryza sativa (japonica cultivar-group)] |
Swiss-Prot | P27933 | 0 | 17 | 249 | 20 | 253 | AMY3D_ORYSJ RecName: Full=Alpha-amylase isozyme 3D; AltName: Full=1,4-alpha-D-glucan glucanohydrolase; 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 | 1bg9_A | 0 | 23 | 249 | 1 | 228 | B Chain B, Crystal Structure Of Plant Cell Wall Invertase In Complex With A Specific Protein Inhibitor |
PDB | 1ava_B | 0 | 23 | 249 | 1 | 228 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 23 | 249 | 1 | 228 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 23 | 249 | 1 | 228 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qps_A | 0 | 23 | 249 | 2 | 229 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
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 |