| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT2G39930.1 |
| Family | GH13 |
| Protein Properties | Length: 784 Molecular Weight: 89481.1 Isoelectric Point: 6.1217 |
| Chromosome | Chromosome/Scaffold: 2 Start: 16666023 End: 16672494 |
| Description | Alpha amylase, catalytic domain containing protein, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 236 | 622 | 0 |
| IEFPGTYQGVAEKLDHLKELGINCIELMPCHEFNELEYYSYNTILGDHRVNFWGYSTIGFFSPMIRYASASSNNFAGRAINEFKILVKEAHKRGIEVIMD VVLNHTAEGNEKGPIFSFRGVDNSVYYMLAPKGEFYNYSGCGNTFNCNHPVVRQFILDCLRYWVTEMHVDGFRFDLGSIMSRSSSLWDAANVYGADVEGD LLTTGTPISCPPVIDMISNDPILRGVKLIAEAWDAGGLYQVGMFPHWGIWSEWNGKFRDVVRQFIKGTDGFSGAFAECLCGSPNLYQGGRKPWHSINFIC AHDGFTLADLVTYNNKNNLANGEENNDGENHNYSWNCGEEGDFASISVKRLRKRQMRNFFVSLMVSQGVPMIYMGDEYGHTKGGNNN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 784 Download |
| MDAIKCSSSF LHHTKLNTLF SNHTFPKISA PNFKPLFRPI SISAKDRRSN EAENIAVVEK 60 PLKSDRFFIS DGLPSPFGPT VRDDGVNFSV YSTNSVSATI CLISLSDLRQ NKVTEEIQLD 120 PSRNRTGHVW HVFLRGDFKD MLYGYRFDGK FSPEEGHYYD SSNILLDPYA KAIISRDEFG 180 VLGPDDNCWP QMACMVPTRE EEFDWEGDMH LKLPQKDLVI YEMHVRGFTR HESSKIEFPG 240 TYQGVAEKLD HLKELGINCI ELMPCHEFNE LEYYSYNTIL GDHRVNFWGY STIGFFSPMI 300 RYASASSNNF AGRAINEFKI LVKEAHKRGI EVIMDVVLNH TAEGNEKGPI FSFRGVDNSV 360 YYMLAPKGEF YNYSGCGNTF NCNHPVVRQF ILDCLRYWVT EMHVDGFRFD LGSIMSRSSS 420 LWDAANVYGA DVEGDLLTTG TPISCPPVID MISNDPILRG VKLIAEAWDA GGLYQVGMFP 480 HWGIWSEWNG KFRDVVRQFI KGTDGFSGAF AECLCGSPNL YQGGRKPWHS INFICAHDGF 540 TLADLVTYNN KNNLANGEEN NDGENHNYSW NCGEEGDFAS ISVKRLRKRQ MRNFFVSLMV 600 SQGVPMIYMG DEYGHTKGGN NNTYCHDNYM NYFRWDKKEE AHSDFFRFCR ILIKFRDECE 660 SLGLNDFPTA KRLQWHGLAP EIPNWSETSR FVAFSLVDSV KKEIYVAFNT SHLATLVSLP 720 NRPGYRWEPF VDTSKPSPYD CITPDLPERE TAMKQYRHFL DANVYPMLSY SSIILLLSPI 780 KDP* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK14510 | PRK14510 | 5.0e-122 | 69 | 724 | 691 | + putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional | ||
| PRK03705 | PRK03705 | 1.0e-144 | 69 | 656 | 602 | + glycogen debranching enzyme; Provisional | ||
| cd11326 | AmyAc_Glg_debranch | 0 | 203 | 656 | 460 | + Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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. | ||
| COG1523 | PulA | 0 | 69 | 749 | 711 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02100 | glgX_debranch | 0 | 71 | 738 | 708 | + glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004556 | alpha-amylase activity |
| GO:0005975 | carbohydrate metabolic process |
| GO:0009507 | chloroplast |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAZ81835.1 | 0 | 9 | 779 | 21 | 787 | isoamylase isoform 1 [Pisum sativum] |
| DDBJ | BAF52941.1 | 0 | 33 | 779 | 33 | 787 | isoamylase-type starch-debranching enzyme 1 [Phaseolus vulgaris] |
| EMBL | CBI40669.1 | 0 | 51 | 782 | 71 | 807 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_181522.1 | 0 | 1 | 783 | 1 | 783 | ISA1 (ISOAMYLASE 1); alpha-amylase/ isoamylase [Arabidopsis thaliana] |
| RefSeq | XP_002324659.1 | 0 | 41 | 782 | 51 | 793 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vuy_B | 0 | 72 | 733 | 15 | 685 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
| PDB | 2vuy_A | 0 | 72 | 733 | 15 | 685 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
| PDB | 2vr5_B | 0 | 72 | 733 | 15 | 685 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
| PDB | 2vr5_A | 0 | 72 | 733 | 15 | 685 | A Chain A, Expression, Purification, Spectroscopical And Crystallographical Studies Of Segments Of The Nucleotide Binding Domain Of The Reticulocyte Binding Protein Py235 Of Plasmodium Yoelii |
| PDB | 2vnc_B | 0 | 72 | 733 | 15 | 685 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation II | RXN-12280 | EC-3.2.1.68 | isoamylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO800235 | 263 | 479 | 740 | 0 |
| HO800235 | 119 | 305 | 423 | 0 |
| HO800235 | 51 | 427 | 477 | 0 |
| HO431228 | 411 | 358 | 767 | 0 |
| DW065550 | 291 | 458 | 747 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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