| Basic Information | |
|---|---|
| Species | Cucumis sativus |
| Cazyme ID | Cucsa.084930.1 |
| Family | GH13 |
| Protein Properties | Length: 886 Molecular Weight: 98147.8 Isoelectric Point: 5.7798 |
| Chromosome | Chromosome/Scaffold: 00862 Start: 598634 End: 601991 |
| 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 | 395 | 719 | 5.6e-30 |
| DIAGTFSGLTKKLLHFKNLGVNAVLLEPIFQFDEKEGPYFPFHFFSPTNNYGPSGASISAINSMKEMVKELHANGVEVILEVVYTHTSGNGALQGIDDSS YYFTNRVANLEEKSALNCNYPIVQQLLLDSLRYWVTEFHVDGFCFVNASFLLRGHHGELLSRPPFVEAIAFDPLLSKTKLVADFWDPQELESKETRFPHW KRWAEVNSKFCSDIRDFFRGEGLISSLATRLCGSGDVFSDGRGPAFSFNFIARNVGLPLVDLVSFSNSNLASELSWNCGEEGPTSNLKVLEKRLKQIRNF IFVLFVSLGVPVLNMGDECGQSSGG | |||
| Full Sequence |
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| Protein Sequence Length: 886 Download |
| MATFLSSLVI QPFCVYNCGV TESPKLAASD HLTYGQKTKY QFGKMDEARM LAHGENKVGA 60 VKSSHRNLSK TYAKSGISVG KSGQRLGIGG KSKEQRRVAT YLFRTEFGDL VNVFVGKKGS 120 TFTVNIEVPS MQLVSIDEAL LLSWGVYRSD SALVTPNFES SPPDETTGAT ETPFVKTSEG 180 KFSVELEFDA KHTPFYLSFV LKYPMGVDSG SSEIRSHKKT SFSVPVGFGR GYPSPLGLSI 240 SGDGSVNFSI FSSSAESLVL CLYNDSTSEK PLLELDLDPY INRSGNIWHA SFEGASKFVS 300 YGYQCKGSKS HENQDGLEVS RIVVDPYAKI LAPSIPKSSG QGLGLPSKFL GQISKVPTFD 360 WDGEVHPNLP MEKLFVYRLN VERFTMDKSS QLPADIAGTF SGLTKKLLHF KNLGVNAVLL 420 EPIFQFDEKE GPYFPFHFFS PTNNYGPSGA SISAINSMKE MVKELHANGV EVILEVVYTH 480 TSGNGALQGI DDSSYYFTNR VANLEEKSAL NCNYPIVQQL LLDSLRYWVT EFHVDGFCFV 540 NASFLLRGHH GELLSRPPFV EAIAFDPLLS KTKLVADFWD PQELESKETR FPHWKRWAEV 600 NSKFCSDIRD FFRGEGLISS LATRLCGSGD VFSDGRGPAF SFNFIARNVG LPLVDLVSFS 660 NSNLASELSW NCGEEGPTSN LKVLEKRLKQ IRNFIFVLFV SLGVPVLNMG DECGQSSGGS 720 VAFNDKRSFN WDLLKTDFGT QTTQFIAFLS SFRSRRFDLF QNRNFLKGEN IDWFDNNQSP 780 PQWEDASCKF LAVMLRADKE ENESITENPK TRSNIFMVFN ASDQSESVAL PEPLEGTSWF 840 RVVDTALPFP GFFSSDGELV PMTGSVTYEI QAHSCALFEA KSAND* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK03705 | PRK03705 | 8.0e-70 | 231 | 881 | 723 | + glycogen debranching enzyme; Provisional | ||
| COG1523 | PulA | 4.0e-110 | 231 | 882 | 718 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02100 | glgX_debranch | 2.0e-118 | 231 | 878 | 723 | + 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-119 | 359 | 755 | 443 | + 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 | 6.0e-132 | 370 | 761 | 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 | |
|---|---|
| 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 | 14 | 880 | 13 | 877 | putative isoamylase [Arabidopsis thaliana] |
| DDBJ | BAF52942.1 | 0 | 69 | 880 | 54 | 860 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
| RefSeq | NP_171830.1 | 0 | 14 | 880 | 13 | 877 | isoamylase, putative / starch debranching enzyme, putative [Arabidopsis thaliana] |
| RefSeq | XP_002271798.1 | 0 | 1 | 884 | 1 | 881 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002533079.1 | 0 | 1 | 880 | 1 | 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 | 231 | 757 | 15 | 599 | A Chain A, The Structure Of A Protein In Glycosyl Transferase Family 8 From Anaerococcus Prevotii. |
| PDB | 2vuy_A | 0 | 231 | 757 | 15 | 599 | A Chain A, The Structure Of A Protein In Glycosyl Transferase Family 8 From Anaerococcus Prevotii. |
| PDB | 2vr5_B | 0 | 231 | 757 | 15 | 599 | A Chain A, The Structure Of A Protein In Glycosyl Transferase Family 8 From Anaerococcus Prevotii. |
| PDB | 2vr5_A | 0 | 231 | 757 | 15 | 599 | A Chain A, The Structure Of A Protein In Glycosyl Transferase Family 8 From Anaerococcus Prevotii. |
| PDB | 2vnc_B | 0 | 231 | 757 | 15 | 599 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| ES817618 | 333 | 372 | 704 | 0 |
| DR926647 | 297 | 381 | 673 | 0 |
| GE635058 | 273 | 464 | 736 | 0 |
| FY782990 | 271 | 588 | 858 | 0 |
| ES831926 | 289 | 361 | 648 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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