| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_001414m |
| Family | GH13 |
| Protein Properties | Length: 884 Molecular Weight: 99057.4 Isoelectric Point: 5.9496 |
| Chromosome | Chromosome/Scaffold: 11998 Start: 1355893 End: 1359220 |
| Description | debranching enzyme 1 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 390 | 716 | 1.1e-27 |
| SDIAGTFAGLTEKLNHIKNLGVNAVLLEPIFPFDEEKGPFFPRHFFSPSNIYGPSGGSISAITSMKEMVKQFHANGIEVLLEVVFTHTAEGGSLQGIDDF SYYYANRAVELESRNALNCNYPIVQRMILDSLRHWVTEYHIDGFCFINASFLQRGFHGEILSRPPLVEAIAFDPLLSKTKIIADCWDPEDVIPKDTCFPH WKRWAEMNAKFCFDVRNFLRGESLLSDLATRLCGSGDIFSSGRGPAFSFNYVARNSGLPLVDLVSFSSSELASELSWNCGEEGATNKTPVLERRLKQIRN YLFILYVSLGVPVLNMGDECGQSSNGS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 884 Download |
| MATLLPSFAI SRCCYSCGAV ESSKLTLTTR YTSGKKMELG FGRTDVEKRL LVGEVAQNVR 60 STLHWNHNSG VFAAARVPVQ ETEQILSTIT EVDELQKVSS YLFRTQIGGN VKVSVRKKNA 120 KYAVYIEVSS LELGNSDYRL VLAWGIYRSD SSCFMPLDSQ RLDPVARTME TPFVQNAFAI 180 FSLELEFEAK QTPFSLSFLL KSMFNTDSSG SEIRNHKKAN FSVPIGFSSG YPDPLGLSFS 240 TDGSMNFAFF SRNAEGVVLC LYDDSTTDKP ALELDLDPYV NRSGDVWHAS LEGACTFSSY 300 GYRCMGGILQ GETGKDYVER VLLDPYARII VNFTADHGSH SSLKYLGRLC KEPAFEWSDE 360 VYPNLDMEKL VVYRLNVKRF TEHKSSQLYS DIAGTFAGLT EKLNHIKNLG VNAVLLEPIF 420 PFDEEKGPFF PRHFFSPSNI YGPSGGSISA ITSMKEMVKQ FHANGIEVLL EVVFTHTAEG 480 GSLQGIDDFS YYYANRAVEL ESRNALNCNY PIVQRMILDS LRHWVTEYHI DGFCFINASF 540 LQRGFHGEIL SRPPLVEAIA FDPLLSKTKI IADCWDPEDV IPKDTCFPHW KRWAEMNAKF 600 CFDVRNFLRG ESLLSDLATR LCGSGDIFSS GRGPAFSFNY VARNSGLPLV DLVSFSSSEL 660 ASELSWNCGE EGATNKTPVL ERRLKQIRNY LFILYVSLGV PVLNMGDECG QSSNGSTSYG 720 DRKPFDWNAL SMGFGIQMTR FISFMSSLRR RRSDVLQKRN FMKEENIDWH GSGQSPPRWE 780 DRSCKFLAMT LKTEKTENKL SPESSNIKGD LFMAFNAYPH SESVILPPVP EGMTWHRLVD 840 TSLPFPGFFS EDGEPVFEQM AGLIAYEMKS HSCTLFEATS LGG* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd11346 | AmyAc_plant_IsoA | 2.0e-21 | 687 | 757 | 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. | ||
| cd11326 | AmyAc_Glg_debranch | 2.0e-110 | 355 | 751 | 458 | + 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. | ||
| TIGR02100 | glgX_debranch | 1.0e-112 | 229 | 846 | 701 | + 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 | 3.0e-113 | 228 | 852 | 696 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| cd11346 | AmyAc_plant_IsoA | 1.0e-124 | 366 | 629 | 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:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAN15318.1 | 0 | 1 | 882 | 1 | 860 | isoamylase isoform 2 [Solanum tuberosum] |
| DDBJ | BAF52942.1 | 0 | 66 | 878 | 51 | 860 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
| RefSeq | NP_171830.1 | 0 | 1 | 878 | 1 | 877 | isoamylase, putative / starch debranching enzyme, putative [Arabidopsis thaliana] |
| RefSeq | XP_002271798.1 | 0 | 1 | 883 | 1 | 882 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002533079.1 | 0 | 1 | 883 | 1 | 872 | 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 | 230 | 752 | 15 | 598 | A Chain A, Crystal Structure Of Galactosyltransferase Lgtc In Complex With Mn And Udp-2f-Galactose |
| PDB | 2vuy_A | 0 | 230 | 752 | 15 | 598 | A Chain A, Crystal Structure Of Galactosyltransferase Lgtc In Complex With Mn And Udp-2f-Galactose |
| PDB | 2vr5_B | 0 | 230 | 752 | 15 | 598 | A Chain A, Crystal Structure Of Galactosyltransferase Lgtc In Complex With Mn And Udp-2f-Galactose |
| PDB | 2vr5_A | 0 | 230 | 752 | 15 | 598 | A Chain A, Crystal Structure Of Galactosyltransferase Lgtc In Complex With Mn And Udp-2f-Galactose |
| PDB | 2vnc_B | 0 | 230 | 752 | 15 | 598 | 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 |
| ES817618 | 344 | 368 | 703 | 0 |
| GE635058 | 272 | 460 | 731 | 0 |
| FY782990 | 274 | 582 | 855 | 0 |
| DR926647 | 304 | 377 | 676 | 0 |
| ES817618 | 104 | 677 | 778 | 0.018 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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