| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma06g10540.2 |
| Family | GH13 |
| Protein Properties | Length: 773 Molecular Weight: 87062.5 Isoelectric Point: 6.05 |
| Chromosome | Chromosome/Scaffold: 06 Start: 7971755 End: 7985816 |
| Description | isoamylase 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 265 | 629 | 0 |
| NIRGSYLGMIEKIPHLLELGINAVELLPVFEFDELEFQRRPNPRDHMINTWGYSTINFFAPMSRYASAGGGSVNASREFKQMVKSLHSAGIEVILDVVYN HTNEADDAFPYTTSFRGIDNKVYYMLDNNGQLLNFSGCGNTLNCNHPVVMELILDSLRHWVTEYHVDGFRFDLASVLCRGIDGSPLNAPPLIRAIAKDAV LSRCKIIAEPWDCGGLYLVGSFPNWDRWAEWNGKYRDDVRKFIKGDSGVKGSFATRVAGSSDLYSVNNRRPYHGINFVIAHDGFTLRDLVSYNFKHNEAN GEGGNDGSNDNFSWNCGLEGETDDASVRALRSRQMKNFHLALMISQGTPMMLMGDEYGHTRNGNN | |||
| Full Sequence |
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| Protein Sequence Length: 773 Download |
| MLHQFTLFAP IFSGGNNAGR CSFAGNSSVR DVRSLRFMKQ ASGRQSNNEH GVFSETMDRA 60 KHRATTAYGG RAQEGVLEEE SSKVIESRPS WKAFPGQSFP LGVSEVDSGI NFAIFSQNAT 120 AVTLCLVLPE RGSIDALDGG MIEMVLDPDL NKTGDIWHIC IEDLPRSNVL YGYRIDGPRD 180 WGKGHRFDSS IVLVDPYAKL VEGRRYFGDI SMKLSKFLGT YDFDSLPFDW GENYKLPNIS 240 EKDLVIYEMN VRAFTSDESS GLDSNIRGSY LGMIEKIPHL LELGINAVEL LPVFEFDELE 300 FQRRPNPRDH MINTWGYSTI NFFAPMSRYA SAGGGSVNAS REFKQMVKSL HSAGIEVILD 360 VVYNHTNEAD DAFPYTTSFR GIDNKVYYML DNNGQLLNFS GCGNTLNCNH PVVMELILDS 420 LRHWVTEYHV DGFRFDLASV LCRGIDGSPL NAPPLIRAIA KDAVLSRCKI IAEPWDCGGL 480 YLVGSFPNWD RWAEWNGKYR DDVRKFIKGD SGVKGSFATR VAGSSDLYSV NNRRPYHGIN 540 FVIAHDGFTL RDLVSYNFKH NEANGEGGND GSNDNFSWNC GLEGETDDAS VRALRSRQMK 600 NFHLALMISQ GTPMMLMGDE YGHTRNGNNN SYGHDTAINN FLWDQLDARK SDHFRFFSNM 660 IKYRHAHEVF NHESFLSKND ITWHEDNWDN HDSKFLAFTL HDKSGGDIYL AFNAHDYFVK 720 VLLPAPPKKR NWFRVVDTNL KSPDDFVLDG VPNVGNTYNI APYSSILLEA KF* 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK14510 | PRK14510 | 1.0e-134 | 95 | 727 | 670 | + putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional | ||
| PRK03705 | PRK03705 | 4.0e-150 | 95 | 664 | 591 | + glycogen debranching enzyme; Provisional | ||
| cd11326 | AmyAc_Glg_debranch | 0 | 228 | 667 | 444 | + 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 | 95 | 746 | 691 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02100 | glgX_debranch | 0 | 95 | 768 | 719 | + 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:0005975 | carbohydrate metabolic process |
| GO:0043169 | cation binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAZ81837.1 | 0 | 40 | 772 | 2 | 736 | isoamylase isoform 3 [Pisum sativum] |
| DDBJ | BAF52943.1 | 0 | 4 | 772 | 15 | 783 | isoamylase-type starch-debranching enzyme 3 [Phaseolus vulgaris] |
| EMBL | CBI19205.1 | 0 | 10 | 772 | 14 | 775 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002284042.1 | 0 | 10 | 772 | 26 | 787 | PREDICTED: similar to isoamylase-type starch-debranching enzyme 3 [Vitis vinifera] |
| RefSeq | XP_002513977.1 | 0 | 59 | 772 | 66 | 782 | isoamylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vuy_B | 0 | 95 | 750 | 14 | 699 | A Chain A, Apo Histidine-Tagged Saccharopine Dehydrogenase (L-Glu Forming) From Saccharomyces Cerevisiae |
| PDB | 2vuy_A | 0 | 95 | 750 | 14 | 699 | A Chain A, Apo Histidine-Tagged Saccharopine Dehydrogenase (L-Glu Forming) From Saccharomyces Cerevisiae |
| PDB | 2vr5_B | 0 | 95 | 750 | 14 | 699 | A Chain A, Apo Histidine-Tagged Saccharopine Dehydrogenase (L-Glu Forming) From Saccharomyces Cerevisiae |
| PDB | 2vr5_A | 0 | 95 | 750 | 14 | 699 | A Chain A, Apo Histidine-Tagged Saccharopine Dehydrogenase (L-Glu Forming) From Saccharomyces Cerevisiae |
| PDB | 2vnc_B | 0 | 95 | 750 | 14 | 699 | 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 |
| HO798725 | 453 | 189 | 641 | 0 |
| HO779625 | 244 | 530 | 773 | 0 |
| HO779625 | 181 | 347 | 527 | 0 |
| HO430858 | 266 | 508 | 771 | 0 |
| HO798725 | 50 | 641 | 690 | 0.00000001 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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