y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000185233 |
Family | GH13 |
Protein Properties | Length: 839 Molecular Weight: 95418.4 Isoelectric Point: 7.5481 |
Chromosome | Chromosome/Scaffold: 011216293 Start: 6987 End: 20111 |
Description | isoamylase 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 | 338 | 599 | 1.4e-39 |
TDFPGTYLGLVEKLDHLKELGINCLELMPCHEFNELEYFSYNSVSGDYKVNFWGYSTINCFSPMIRYSSAGIRNCGRDAINEVKFLIKEAHKRGIEVIMD VVFNHTAEGNENGPMLSFRGADNSVYYMLAPKGEFYNYSGCGNTFNCNHPVVRQFIVDCLRYWVTEMHVDGFRFDLASIMTRGSSLWDAINVYGSAIEGD FLTTGTPLATPPLVDMISNDPILHGAKLIAEAWDAGGLYQVGMFPHWGSWSEWNGKYRDTVR |
Full Sequence |
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Protein Sequence Length: 839 Download |
MTSRLQISRR RTRRTREVTK KTEKDDVREY GENTSNVPPK NKNKFQPLRN ESDTDNISSQ 60 KSIPLQTKQT GGQESLSLTD EPMAQQQQLT KCSAWSTAPN LNLPRQNTQR FAFPNARRQN 120 PNQKTKSLNW WMRGFGNHAR ALVAKASNGG AGTEVAENTV VDRPKLQPFQ VSQGHPSALG 180 ATARDGGVNF AVYSGNAVSV TLCLITLSDL EGDKVTELIP LDPLTNKTGN VWHVLLKGDF 240 KDILYGYKFD GKFSPEEGHY YDSSRIVLDP YAKAVIRRGE FRKLGPDGNC WPQMAGTVPS 300 FDDQFDWEGD LPLKYPQKDL IIYEMHVRGF TRHESSVTDF PGTYLGLVEK LDHLKELGIN 360 CLELMPCHEF NELEYFSYNS VSGDYKVNFW GYSTINCFSP MIRYSSAGIR NCGRDAINEV 420 KFLIKEAHKR GIEVIMDVVF NHTAEGNENG PMLSFRGADN SVYYMLAPKG EFYNYSGCGN 480 TFNCNHPVVR QFIVDCLRYW VTEMHVDGFR FDLASIMTRG SSLWDAINVY GSAIEGDFLT 540 TGTPLATPPL VDMISNDPIL HGAKLIAEAW DAGGLYQVGM FPHWGSWSEW NGKYRDTVRQ 600 FIKGTVAFLG LWLNAFVGAL IYIRESIFLA FRRLITLEDG KYAFYVFMGQ KLRITSVEGE 660 LTSISVKKLR KRQMRNFFVC LMVSQINYFR WDKKEESSSD FFRFCYLMTK FRQECKSLGL 720 NDFPTAERLQ WHGHAPGVPD WSDTSRFVAF TLMDAVKREL YIAFNASHLA VIISLPERPG 780 YRWEPLVDTS KPAPFDFLTS DLPERDTAIK QYAHFLDANL YPMLSYSSII LLLSPVEDP 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11326 | AmyAc_Glg_debranch | 4.0e-9 | 657 | 714 | 85 | + 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. | ||
PRK03705 | PRK03705 | 8.0e-101 | 170 | 601 | 445 | + glycogen debranching enzyme; Provisional | ||
TIGR02100 | glgX_debranch | 5.0e-137 | 174 | 795 | 712 | + 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 | 4.0e-150 | 305 | 610 | 311 | + 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 | 2.0e-157 | 168 | 809 | 727 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] |
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 | AAZ81835.1 | 0 | 150 | 835 | 60 | 787 | isoamylase isoform 1 [Pisum sativum] |
DDBJ | BAF52941.1 | 0 | 141 | 838 | 47 | 790 | isoamylase-type starch-debranching enzyme 1 [Phaseolus vulgaris] |
EMBL | CBI40669.1 | 0 | 120 | 838 | 38 | 807 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002265964.1 | 0 | 150 | 838 | 12 | 740 | PREDICTED: similar to isoamylase-type starch-debranching enzyme 1 [Vitis vinifera] |
RefSeq | XP_002324659.1 | 0 | 135 | 838 | 45 | 793 | predicted protein [Populus trichocarpa] |
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 | 162 | 760 | 9 | 647 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2vuy_A | 0 | 162 | 760 | 9 | 647 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2vr5_B | 0 | 162 | 760 | 9 | 647 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2vr5_A | 0 | 162 | 760 | 9 | 647 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2vnc_B | 0 | 162 | 760 | 9 | 647 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |