y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000647541 |
Family | GH13 |
Protein Properties | Length: 871 Molecular Weight: 96920.2 Isoelectric Point: 5.2645 |
Chromosome | Chromosome/Scaffold: 003619249 Start: 5450 End: 8062 |
Description | debranching enzyme 1 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 379 | 707 | 5.6e-28 |
NIAGTFSGLTEKLEHFKALGVNAVLLEPIFPFDEQKGPYFPVHFFSPMNCFGPPRGPVSAVISMKEMVKXFHADGIEVLLEVVFTHTSEGEAMQGIDISS YYHVNGVEDLEARNALNCNYPVVQQMVLDSLXYWVTEFHVDGFCFINASSLLRGSNGEYLSRPPLVEAIAFDPLLSKTKIIADCWDPRGLVPKETRFPHW KRWAEVNTKFSNDVRNFLRGEGLLSDLATRLCGNGDIXSDGRGPASSFNFISRNSGLXLVDLVSFSGVELAAELSXNCGEEGPTNKTAVLERRLKQIRNF LFILFVSLGVPVLNMGDEYGQSAGGSPAY |
Full Sequence |
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Protein Sequence Length: 871 Download |
MATLPLSIAI QASCCLNCGT TELPKLTATD RYGHRNNGVH GYVKLGTERN LVLREVVQIL 60 KERPLRDREW KVYATSRVSV EPVEQRVSTG TETEEVGKVS TYLFRTDTGD PVNVFVRKRN 120 AKYAVNIEVS LLHLSRSDRR LVLSWGMYRA DSSSFVPSNF RSSTPADRTT ALETPFTGTS 180 SGKFTLELEF EAKQIPFYLS FVLKSPADAD LSDLEIRSHR KTNFCFPVGF GRGCPAPLGV 240 SFSNDGSMNF AIFSRNAESV VLCLYAETTA EKPVLELDLD PYVNRSGDIW HASFENAWDF 300 VSYGYRFDEG NVLLDPYAKI IAKSVPHGTG SKYLGRLCEE PAFEWAGDVX PDLTLEKLVV 360 YRLNVKRFTK HKSSKLPTNI AGTFSGLTEK LEHFKALGVN AVLLEPIFPF DEQKGPYFPV 420 HFFSPMNCFG PPRGPVSAVI SMKEMVKXFH ADGIEVLLEV VFTHTSEGEA MQGIDISSYY 480 HVNGVEDLEA RNALNCNYPV VQQMVLDSLX YWVTEFHVDG FCFINASSLL RGSNGEYLSR 540 PPLVEAIAFD PLLSKTKIIA DCWDPRGLVP KETRFPHWKR WAEVNTKFSN DVRNFLRGEG 600 LLSDLATRLC GNGDIXSDGR GPASSFNFIS RNSGLXLVDL VSFSGVELAA ELSXNCGEEG 660 PTNKTAVLER RLKQIRNFLF ILFVSLGVPV LNMGDEYGQS AGGSPAYSDR KAFDWNALGT 720 GFATQTTQFI AFLSSFRIRR SDXLQKRNFL KEENIDWYGS XQSSPKWEDP SXKFLAMKLK 780 ADXEEAYESG DDSSPSWGDL FVAFSAADXS ETVILPPLPE GXGWFXLVDT ALPFPGFFST 840 DGEPVAEQPA GLFAYEMXSH SCALFEARSL * 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK03705 | PRK03705 | 1.0e-71 | 233 | 768 | 616 | + glycogen debranching enzyme; Provisional | ||
COG1523 | PulA | 5.0e-108 | 235 | 833 | 684 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02100 | glgX_debranch | 6.0e-113 | 233 | 850 | 707 | + 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 | 2.0e-120 | 343 | 737 | 435 | + 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 | 4.0e-139 | 355 | 745 | 404 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAM98123.1 | 0 | 1 | 867 | 1 | 877 | putative isoamylase [Arabidopsis thaliana] |
GenBank | AAN15318.1 | 0 | 1 | 870 | 1 | 859 | isoamylase isoform 2 [Solanum tuberosum] |
DDBJ | BAF52942.1 | 0 | 65 | 867 | 49 | 860 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
RefSeq | XP_002271798.1 | 0 | 1 | 870 | 1 | 880 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533079.1 | 0 | 1 | 867 | 1 | 867 | isoamylase, 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 | 2vuy_B | 0 | 233 | 740 | 15 | 598 | A Chain A, Pectin Methylesterase From Carrot |
PDB | 2vuy_A | 0 | 233 | 740 | 15 | 598 | A Chain A, Pectin Methylesterase From Carrot |
PDB | 2vr5_B | 0 | 233 | 740 | 15 | 598 | A Chain A, Pectin Methylesterase From Carrot |
PDB | 2vr5_A | 0 | 233 | 740 | 15 | 598 | A Chain A, Pectin Methylesterase From Carrot |
PDB | 2vnc_B | 0 | 233 | 740 | 15 | 598 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES817618 | 333 | 356 | 688 | 0 |
CN939141 | 222 | 179 | 400 | 0 |
GE635058 | 272 | 449 | 720 | 0 |
DR926647 | 299 | 365 | 657 | 0 |
FY782990 | 275 | 570 | 844 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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