| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10000661 |
| Family | GH13 |
| Protein Properties | Length: 830 Molecular Weight: 91634.7 Isoelectric Point: 6.6899 |
| Chromosome | Chromosome/Scaffold: 554 Start: 15253 End: 17742 |
| 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 | 342 | 663 | 2.8e-29 |
| DVAGSFAGVAEKVKHFKDLGVNAVLIEPVFPFDEHKGPYFPYHFFSPSNQYGSRSSSDSVSAISSMKEMVKTLHDSGIEVFMEVVFSHTAESRALQGIDD SSYYYADNSSLNCNYPVVTRMILDSLRHWVTEFHIDGFCFMNASSLLRGFHGESLSRPPLIESIAFEPVLSKTKIIADFWDPQEMLAKKETRFPHWKRWA EMNTKFCYDVRNFLKGEGHLSCLATRLCGSGDFFSSGRGPSHGFNFIARNSGLSLVDLVSFSSDNKVAHELSWNCGEEGPTGKTLVLERRLKQIRNYLFI LFVSLGVPVLNMGDECGQSSGG | |||
| Full Sequence |
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| Protein Sequence Length: 830 Download |
| MRTLSPSLSI CGQLKSAKLN FVSHCAIAGN GSFGIRGIGV GSNVSLRKLS LGAVNAKSRP 60 SFREIVTPPP SIEVDELKKE ASSSTYLFRT EVGGGSVKVS ISKNKKKDKY VVYVEVSSLE 120 LGISDCTVTL VWGICRSDSL DESTTVENSS LLQSTIGGGF SGELEFELGQ SPFYLSFVLK 180 SSEVEIRSHR KTKFCVPVGF GRGDPSPLGI SFSADGSVNF AFFSRNAEKV VLCLYSNDKK 240 PAVEIDLDSY VNKTGNIWHA SFEDVSSFRS YGFRCDKGGT GQALLDPYAK VTGSYLGRLC 300 KEPDFDWNGD VRPNLPLEKL VVYRLNVKRF TQHGSSLLSS DDVAGSFAGV AEKVKHFKDL 360 GVNAVLIEPV FPFDEHKGPY FPYHFFSPSN QYGSRSSSDS VSAISSMKEM VKTLHDSGIE 420 VFMEVVFSHT AESRALQGID DSSYYYADNS SLNCNYPVVT RMILDSLRHW VTEFHIDGFC 480 FMNASSLLRG FHGESLSRPP LIESIAFEPV LSKTKIIADF WDPQEMLAKK ETRFPHWKRW 540 AEMNTKFCYD VRNFLKGEGH LSCLATRLCG SGDFFSSGRG PSHGFNFIAR NSGLSLVDLV 600 SFSSDNKVAH ELSWNCGEEG PTGKTLVLER RLKQIRNYLF ILFVSLGVPV LNMGDECGQS 660 SGGSISYSDR KPLDWNALST GFGSQTTEFV SFLSELRARR SDLLQKGNFL DEKNIKWYGN 720 DQSPPKWDDP STKFLAMGLK TNKPGDAKGD LFMAFNAGRK SEDVILPIAP EGMKWHRLVD 780 TALPYPGFFS ETGEIADEDM EGSVVYEMRS HSCVLFEARS SISSDLLPL* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd11346 | AmyAc_plant_IsoA | 2.0e-21 | 635 | 705 | 71 | + 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. | ||
| cd11346 | AmyAc_plant_IsoA | 7.0e-98 | 316 | 576 | 281 | + 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. | ||
| COG1523 | PulA | 3.0e-99 | 203 | 824 | 728 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02100 | glgX_debranch | 3.0e-100 | 203 | 816 | 720 | + 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]. | ||
| cd11326 | AmyAc_Glg_debranch | 6.0e-103 | 305 | 699 | 446 | + 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. | ||
| 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 | 85 | 819 | 87 | 857 | isoamylase isoform 2 [Solanum tuberosum] |
| DDBJ | BAF52942.1 | 0 | 33 | 818 | 20 | 860 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
| RefSeq | NP_171830.1 | 0 | 73 | 818 | 88 | 877 | isoamylase, putative / starch debranching enzyme, putative [Arabidopsis thaliana] |
| RefSeq | XP_002271798.1 | 0 | 1 | 820 | 1 | 879 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002533079.1 | 0 | 3 | 818 | 9 | 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 | 203 | 696 | 15 | 584 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 2vuy_A | 0 | 203 | 696 | 15 | 584 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 2vr5_B | 0 | 203 | 696 | 15 | 584 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 2vr5_A | 0 | 203 | 696 | 15 | 584 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
| PDB | 2vnc_B | 0 | 203 | 696 | 15 | 584 | 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 |
| DV132907 | 251 | 476 | 725 | 0 |
| ES817618 | 338 | 318 | 648 | 0 |
| GE635058 | 272 | 414 | 680 | 0 |
| FY782990 | 272 | 531 | 794 | 0 |
| JG277995 | 168 | 663 | 830 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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