y
Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g005552m |
Family | GH13 |
Protein Properties | Length: 692 Molecular Weight: 78103.4 Isoelectric Point: 6.4674 |
Chromosome | Chromosome/Scaffold: 00050 Start: 580562 End: 590497 |
Description | isoamylase 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 274 | 530 | 1.6e-25 |
KGEFYNYSGCGNTFNCNHPVVRQFIVDCLRYWVTEMHVDGFRFDLASIMTRGSSLWDSVNVYGIPIEGDLLTTGTPLRSPPLIDLISNDPILRGVKLIAE AWDTGGLYQVGIFPHWGIWSEWNGKYRDIVRQFIKGTDGFAGAFAECLCGSPNLYQGGGRKPWNSINFVCAHDGFSLADLVSYNQKHNLANGEDNNDGET HNNSWNCGQEGEFANILVKKLRRRQMRNFFLCLMVSQGVPMISMGDEYGHTKGGNNN |
Full Sequence |
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Protein Sequence Length: 692 Download |
MELLQFTSSP LLHGSSKFIN SPEFYKSKLS NLKKPPTTTF RCCNHPNKTS HFANSKAFEN 60 VTKNLVIRAS KSAELETAVI KKPQSQRFQV SKGYPTPFGA TLRDGGVNFS IFSSNAVSAT 120 LCLITLSDLQ ENKVTEEIAL DSFANKTGDV WHVFLKGDFK DMLYGYKFDG KFSPQEGHYF 180 DPTKIVLDPY AKAVISRAQF GVLGPDENCW PQMACLVPTP EDEFDWEGDL PLKYPQRDLI 240 IYEVHVRGFT RHESSKTEHP GTYLGVVEKL DHLKGEFYNY SGCGNTFNCN HPVVRQFIVD 300 CLRYWVTEMH VDGFRFDLAS IMTRGSSLWD SVNVYGIPIE GDLLTTGTPL RSPPLIDLIS 360 NDPILRGVKL IAEAWDTGGL YQVGIFPHWG IWSEWNGKYR DIVRQFIKGT DGFAGAFAEC 420 LCGSPNLYQG GGRKPWNSIN FVCAHDGFSL ADLVSYNQKH NLANGEDNND GETHNNSWNC 480 GQEGEFANIL VKKLRRRQMR NFFLCLMVSQ GVPMISMGDE YGHTKGGNNN TYCHDNDINY 540 FRWDKKEESK SDFFRFCCLL TKFRHECESL GLSDFPTADR LQWHGHAPGL PDWSDKSRFV 600 AFTLIDSVKG EIYVAFNASH LPVIISLPKR PGYRWEPLVD TSKPEPFDFL SSDLPAKEIA 660 IKQYAPFLDA NLYPMLSYSS IILLLSPDEN A* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11326 | AmyAc_Glg_debranch | 5.0e-17 | 224 | 274 | 54 | + 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 | 1.0e-35 | 89 | 274 | 205 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02100 | glgX_debranch | 6.0e-126 | 274 | 647 | 394 | + 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 | 1.0e-134 | 275 | 668 | 402 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
cd11326 | AmyAc_Glg_debranch | 2.0e-171 | 270 | 566 | 298 | + 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 | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAF52941.1 | 0 | 57 | 274 | 42 | 260 | isoamylase-type starch-debranching enzyme 1 [Phaseolus vulgaris] |
DDBJ | BAF52941.1 | 0 | 274 | 691 | 374 | 791 | isoamylase-type starch-debranching enzyme 1 [Phaseolus vulgaris] |
EMBL | CAN70034.1 | 0 | 239 | 691 | 47 | 512 | hypothetical protein [Vitis vinifera] |
EMBL | CBI40669.1 | 0 | 62 | 274 | 59 | 271 | unnamed protein product [Vitis vinifera] |
EMBL | CBI40669.1 | 0 | 239 | 691 | 344 | 809 | unnamed protein product [Vitis vinifera] |
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 | 274 | 645 | 320 | 693 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
PDB | 2vuy_B | 1e-20 | 93 | 269 | 15 | 205 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
PDB | 2vuy_A | 0 | 274 | 645 | 320 | 693 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
PDB | 2vuy_A | 1e-20 | 93 | 269 | 15 | 205 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
PDB | 2vr5_B | 0 | 274 | 645 | 320 | 693 | 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 |
EY716964 | 287 | 352 | 638 | 0 |
HO431228 | 398 | 274 | 671 | 0 |
HO800235 | 265 | 386 | 650 | 0 |
HO800235 | 57 | 274 | 330 | 0 |
HO800235 | 58 | 327 | 384 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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