Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_400732g0010 |
Family | GH13 |
Protein Properties | Length: 241 Molecular Weight: 26965.3 Isoelectric Point: 8.7012 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 1 | 158 | 1.1e-21 |
WMNWLKSNVGFDGWRFDFAKGYAGNLLGVYLQNTSPKFAVGEVWDDLSYSDGSLAYDQGAHRQRLVDFVHSTGDRAAAFDFTTKGILQEALKSNELWRLK DSNGKPAGLIGVLPQKAVTFIENHDTGSTQNNWPFPSDKLIQGYAYILTHPGIPTIFY |
Full Sequence |
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Protein Sequence Length: 241 Download |
WMNWLKSNVG FDGWRFDFAK GYAGNLLGVY LQNTSPKFAV GEVWDDLSYS DGSLAYDQGA 60 HRQRLVDFVH STGDRAAAFD FTTKGILQEA LKSNELWRLK DSNGKPAGLI GVLPQKAVTF 120 IENHDTGSTQ NNWPFPSDKL IQGYAYILTH PGIPTIFYDH FVDGNLKKTI QTLIALRKRN 180 NINANSTSRI ITADADLYLA AIDEKVLVKI GSRFDLRNNA PSADFRLVAS GNDYAVWEKN 240 K |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00810 | Alpha-amyl_C2 | 9.0e-24 | 178 | 239 | 62 | + 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 | 9.0e-92 | 1 | 239 | 239 | + alpha-amylase | ||
PLN02361 | PLN02361 | 8.0e-99 | 1 | 239 | 243 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-99 | 1 | 186 | 186 | + 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 | 6.0e-105 | 1 | 240 | 244 | + alpha-amylase; Provisional |
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 | ABK24287.1 | 0 | 1 | 239 | 205 | 445 | unknown [Picea sitchensis] |
GenBank | ABK24434.1 | 0 | 1 | 240 | 204 | 444 | unknown [Picea sitchensis] |
GenBank | ABR16554.1 | 0 | 1 | 239 | 205 | 445 | unknown [Picea sitchensis] |
RefSeq | XP_001754460.1 | 0 | 1 | 239 | 157 | 395 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002285213.1 | 0 | 1 | 239 | 186 | 423 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 1 | 239 | 163 | 402 | A Chain A, Solution Structure Of The C-Terminal Gal-Bind Lectin Domain From Human Galectin-4 |
PDB | 1ava_B | 0 | 1 | 239 | 163 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 1 | 239 | 163 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 1 | 239 | 163 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 1 | 240 | 164 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES665878 | 242 | 1 | 240 | 0 |
DR546349 | 242 | 1 | 240 | 0 |
CX650084 | 235 | 8 | 240 | 0 |
EX319682 | 238 | 1 | 236 | 0 |
FD741248 | 238 | 5 | 240 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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