| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra033388 |
| Family | GH13 |
| Protein Properties | Length: 849 Molecular Weight: 95311 Isoelectric Point: 6.0226 |
| Chromosome | Chromosome/Scaffold: 10 Start: 3918468 End: 3921014 |
| Description | debranching enzyme 1 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 364 | 672 | 4.9e-26 |
| NIAGTFTGVAEKVNHLKTLGTNAVLLEPIFSFSEQNGPYFPFHFFSPMDMYGPSNSMKEMVKRLHSEGIEVLLEVVFTHTADSGALHGIDESCYYLDSKS YVNCNFPVVQELVLESLRYWVTEFHVDGFCFINASSLLRGVHGEHLSRPPLVEAISFDPLLAGRKLIADCWDPHDMKMPKEVRFPHWKRWAEVNTRYCRN VRNFVRGRGVLSDLATRICGSGDVFTDGRGPAFSFNYISRNSGLSLVDLVSFSGPEVASELSWNCGEEGATNKSAVLQTRLKQIRNFLFIQYISLGVPVL NMGDECGVS | |||
| Full Sequence |
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| Protein Sequence Length: 849 Download |
| MAVWSPSVGI GSCCLLHNVI TEAWRFPSTC FSTCNNNTKR GSKTLRVTSA LQSYHRLSKI 60 CASKTSTELK EEVSTRSSQV DEPKKVTTSY SFRTKSGALV KVKVEKKREK YSIMVYVSSL 120 ELIGGDDGKS SSLVMVWGVY RSDSSCFLPL DFESSSQDSQ THTTETLFVK GSLSESKLGL 180 EFDGKESPFS LSFRLKNPNG GLEMLTHRDT NFCVPVGFTA GRPLPLGLSS GPDEDNSWNF 240 AFFSRNAKSV VLCLYDDTTT DKPALELDLD PYINRTGDVW HASVEKTWEF VRYGYRCLSE 300 EEAEDIVLDP YARVIEKFLG SLSKNPCFDW GRDVSPNIPL EKLIVYRLNV KGFTQHKSSK 360 LPTNIAGTFT GVAEKVNHLK TLGTNAVLLE PIFSFSEQNG PYFPFHFFSP MDMYGPSNSM 420 KEMVKRLHSE GIEVLLEVVF THTADSGALH GIDESCYYLD SKSYVNCNFP VVQELVLESL 480 RYWVTEFHVD GFCFINASSL LRGVHGEHLS RPPLVEAISF DPLLAGRKLI ADCWDPHDMK 540 MPKEVRFPHW KRWAEVNTRY CRNVRNFVRG RGVLSDLATR ICGSGDVFTD GRGPAFSFNY 600 ISRNSGLSLV DLVSFSGPEV ASELSWNCGE EGATNKSAVL QTRLKQIRNF LFIQYISLGV 660 PVLNMGDECG VSTRGLTSRK PFDWNMLASA FGVQITQFIS FMTSVRGRRS DVFQRRNFLK 720 PENIFWYAND QTTPKWEDPA SKFLALEIKA EREEETTASL VEPTEPKNND LFIGFNASDQ 780 PENVILPPLP KGSKWRRLVD TALPSPGFFS VEGETVVAEE EEEEMNQPVM YEMKPYSCTL 840 FETINATA* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK03705 | PRK03705 | 2.0e-59 | 219 | 675 | 547 | + glycogen debranching enzyme; Provisional | ||
| COG1523 | PulA | 1.0e-96 | 219 | 806 | 691 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02100 | glgX_debranch | 3.0e-101 | 220 | 806 | 695 | + 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-103 | 328 | 675 | 406 | + 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 | 2.0e-115 | 339 | 588 | 277 | + 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 | AAM98123.1 | 0 | 1 | 848 | 1 | 882 | putative isoamylase [Arabidopsis thaliana] |
| DDBJ | BAF52942.1 | 0 | 25 | 847 | 19 | 864 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
| RefSeq | NP_171830.1 | 0 | 1 | 848 | 1 | 882 | isoamylase, putative / starch debranching enzyme, putative [Arabidopsis thaliana] |
| RefSeq | XP_002271798.1 | 0 | 1 | 843 | 1 | 877 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002533079.1 | 0 | 58 | 843 | 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 | 221 | 725 | 15 | 606 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2vuy_A | 0 | 221 | 725 | 15 | 606 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2vr5_B | 0 | 221 | 725 | 15 | 606 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2vr5_A | 0 | 221 | 725 | 15 | 606 | A Chain A, Barley Limit Dextrinase In Complex With Beta-Cyclodextrin |
| PDB | 2vnc_B | 0 | 221 | 725 | 15 | 606 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| starch degradation II | RXN-12280 | EC-3.2.1.68 | isoamylase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EV528320 | 261 | 500 | 755 | 0 |
| EV223877 | 228 | 583 | 810 | 0 |
| DK534643 | 244 | 608 | 849 | 0 |
| ES817618 | 344 | 341 | 663 | 0 |
| DK531924 | 239 | 613 | 849 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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