Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.010G092900.7 |
Family | GH13 |
Protein Properties | Length: 600 Molecular Weight: 67815 Isoelectric Point: 6.1586 |
Chromosome | Chromosome/Scaffold: 10 Start: 11582343 End: 11590217 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 229 | 519 | 1.1e-38 |
KQKIEEISSLGFTVVWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDLVKRFHGKGVKVLGDAVLNHRCAHYKNGNGVWNIFGGRLNWDDRAVVADDP HFQGRGNKSSGDNFHAAPNIDHSQEFVRKDLKEWLLWLRKEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGELDHDQDAHRQRIVD WINATSGTAGAFDVTTKGILHTTLERCEYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPSGKEMQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 600 Download |
MHHSLLVFSI DNWNLGYLDG WYCRLIYFNV KNSYFLLLLC HLNGHPILQA KEDGNGRSGS 60 FTLDEDLVGF LFVLKLNDST WLNCMGNDFY IALPISSSIP ALSGAGQSEV APVSENTVGA 120 DQEVSHAIYT DGIINEIRSL VSDFSSEKRQ KTKTKEAQES ILQEIEKLAA EAYSIFRSSI 180 PTFLDETALE SEATEAPKIC SGTGTGHEIL LQGFNWESHK LGHWYMELKQ KIEEISSLGF 240 TVVWLPPPTE SVSPEGYMPK DLYNLNSRYG NIDELKDLVK RFHGKGVKVL GDAVLNHRCA 300 HYKNGNGVWN IFGGRLNWDD RAVVADDPHF QGRGNKSSGD NFHAAPNIDH SQEFVRKDLK 360 EWLLWLRKEI GYDGWRLDFV RGFWGGYVKD YLDASEPYFA VGEYWDSLSY TYGELDHDQD 420 AHRQRIVDWI NATSGTAGAF DVTTKGILHT TLERCEYWRL SDQKGKPPGV VGWWPSRAVT 480 FIENHDTGST QGHWRFPSGK EMQGYAYILT HPGTPAVFYD HIFSHYQSEI AALISLRNRN 540 KIHCRSTVKI TKAERDVYAA IIDEKVAVKI GPGHYEPPSG PYSWSSKIEG RNYKVWEAS* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 4.0e-48 | 205 | 539 | 416 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-144 | 208 | 597 | 403 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-165 | 209 | 548 | 343 | + 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. | ||
PLN02361 | PLN02361 | 3.0e-170 | 206 | 597 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 48 | 599 | 554 | + alpha-amylase |
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 | AAX33231.1 | 0 | 48 | 599 | 352 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 61 | 599 | 360 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 47 | 599 | 339 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 47 | 599 | 339 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 47 | 599 | 347 | 900 | alpha-amylase, putative [Ricinus communis] |
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 | 2qpu_C | 0 | 207 | 597 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 207 | 597 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 207 | 597 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 207 | 597 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 207 | 597 | 1 | 403 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 555 | 48 | 600 | 0 |
HO826981 | 405 | 196 | 600 | 0 |
HO811991 | 299 | 302 | 600 | 0 |
ES805448 | 328 | 166 | 492 | 0 |
HO826981 | 27 | 164 | 190 | 0.22 |
Sequence Alignments (This image is cropped. Click for full image.) |
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