| Basic Information | |
|---|---|
| Species | Phaseolus vulgaris |
| Cazyme ID | Phvul.001G148700.1 |
| Family | GH13 |
| Protein Properties | Length: 866 Molecular Weight: 96280.6 Isoelectric Point: 5.7882 |
| Chromosome | Chromosome/Scaffold: 01 Start: 40199619 End: 40202216 |
| Description | debranching enzyme 1 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 378 | 701 | 2.6e-28 |
| AGTFTGLAEKVQHFKDLGVNAVLLEPVFTSDEKKGPYFPCHFFSLMHIYGPSGGPVSTMASMKEMVKTMHANGIEVLVEVVFSNTAEIGALQGIDDSSYY LANGVGDLKIQSALNCNYPIVQNLILDSLRYWVTEFHIDGFSFINASHLLRGFHGEYLSRPPLVEAIAFDPVLSKTKIIADCWDPHDTVAKEIHFPHWMR WAEMNAKFCNDVRNFFRGENLLSDLATRLCGSGDMFSGGRGPAFSFNYIVRNFGFSLVDLVSFSSDDELSWNCGEEGPTNNTSVLERRLKQIRNFLFILF VSLGVPVLNMGDECAHSSGGFPAY | |||
| Full Sequence |
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| Protein Sequence Length: 866 Download |
| MASVVSAFSF SLIPFNQHKF GAKCVGFHKP LIQRKQRQLG LQNHFFPFFR NPSSKLCATS 60 RLSIEETEQQ VEPFTRPEDL KGALAYLFRT ETGGGLVKVY VTKKKDRYFV YIEISSLDVN 120 HCGDSETLVL CWGVYRGDSS CFVDMDSTGL SGNAAKRMNV SPLVQTSVCK FGVELEFDAK 180 YVPLYLSFFL MSSLDAGLEI ISHRRTNFCV PVGLLPGYPG PLGLSYSPDG SVNFAIFSRH 240 AESVVLCLYD EKGVEKPALE VDLDPYVNRS GDIWHVSFES VKSFVSYGYR CRGGVHKQNN 300 GDSSAELVVL DPYAKIVGHS YPSGLELVQN LGWLGKEPAF DWGGDFLPDL SMEELVVYRL 360 NVKRFTQHNS SQLPSGSAGT FTGLAEKVQH FKDLGVNAVL LEPVFTSDEK KGPYFPCHFF 420 SLMHIYGPSG GPVSTMASMK EMVKTMHANG IEVLVEVVFS NTAEIGALQG IDDSSYYLAN 480 GVGDLKIQSA LNCNYPIVQN LILDSLRYWV TEFHIDGFSF INASHLLRGF HGEYLSRPPL 540 VEAIAFDPVL SKTKIIADCW DPHDTVAKEI HFPHWMRWAE MNAKFCNDVR NFFRGENLLS 600 DLATRLCGSG DMFSGGRGPA FSFNYIVRNF GFSLVDLVSF SSDDELSWNC GEEGPTNNTS 660 VLERRLKQIR NFLFILFVSL GVPVLNMGDE CAHSSGGFPA YDDIKPMTWS ALTTGFGKQI 720 SQFIFFMSSL RRRRSDLLQR RSFLKEENIE WYGSDGAPPR WEDPSCKFLA MTLKSEVAVL 780 SESSVSSDIS GDIFIALNVA DEPESTVLPL PPEGMSWYRL VDTSLPFPGF FSSSGEIVPE 840 MKAGLSTYKM KSHSCALFEA CNPTI* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK03705 | PRK03705 | 1.0e-63 | 229 | 709 | 538 | + glycogen debranching enzyme; Provisional | ||
| TIGR02100 | glgX_debranch | 6.0e-92 | 229 | 824 | 674 | + 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]. | ||
| COG1523 | PulA | 2.0e-94 | 232 | 824 | 667 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| cd11326 | AmyAc_Glg_debranch | 3.0e-105 | 340 | 697 | 412 | + 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. | ||
| cd11346 | AmyAc_plant_IsoA | 1.0e-132 | 351 | 722 | 385 | + Alpha amylase catalytic domain family found in plant isoamylases. Two types of debranching enzymes exist in plants: isoamylase-type (EC 3.2.1.68) and a pullulanase-type (EC 3.2.1.41, also known as limit-dextrinase). These efficiently hydrolyze alpha-(1,6)-linkages in amylopectin and pullulan. This group does not contain the conserved catalytic triad present in other alpha-amylase-like proteins. 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. | ||
| 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 | AAN15318.1 | 0 | 50 | 860 | 64 | 856 | isoamylase isoform 2 [Solanum tuberosum] |
| GenBank | AAZ81836.1 | 0 | 1 | 860 | 1 | 852 | isoamylase isoform 2 [Pisum sativum] |
| DDBJ | BAF52942.1 | 0 | 1 | 865 | 1 | 865 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
| RefSeq | XP_002271798.1 | 0 | 26 | 860 | 40 | 877 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002533079.1 | 0 | 54 | 860 | 60 | 867 | 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 | 214 | 734 | 12 | 598 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vuy_A | 0 | 214 | 734 | 12 | 598 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vr5_B | 0 | 214 | 734 | 12 | 598 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vr5_A | 0 | 214 | 734 | 12 | 598 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2vnc_B | 0 | 214 | 734 | 12 | 598 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| ES817618 | 333 | 353 | 682 | 0 |
| DR926647 | 297 | 362 | 651 | 0 |
| GE635058 | 272 | 446 | 714 | 0 |
| ES831926 | 290 | 342 | 630 | 0 |
| ES759806 | 246 | 274 | 519 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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