| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01035168001 |
| Family | GH13 |
| Protein Properties | Length: 810 Molecular Weight: 91658.6 Isoelectric Point: 5.6657 |
| Chromosome | Chromosome/Scaffold: 11 Start: 12508618 End: 12602202 |
| Description | isoamylase 1 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 254 | 647 | 0 |
| TKFPGTYHGVVEKLDHLKELGVNCIELMPCHEFNELEYFSYNSVLDDYRYTCISMVNFWGYSTVNYFSPMIRYSSAGIHNCGHDAINEVKLLIREAHKRG IEVLMDVVFNHTAEGNENGPILSFRGVDNSVYYMLAPKGEFYNYSGCGNTFNCNHPIVRQFILDCLRYWVTEMHVDGFRFDLASIMTRGSSLWDALNVYG NPAEGDSLTTGTPLSSPPLIDMISNDPILRGVKLIAEAWDAGGLYQVGMFPHWGLWSEWNGKYRDIVRQFIKGSDGFSGAFAECLCGSPNLYQEGGRKPW NSINFVCAHDGFTLADLVTYNKKHNNANGEDNNDGENHNNSWNCGQEGEFASISVKKLRKRQMRNFFLCLMVSQGVPMIYMGDEYGHTKGGNNN | |||
| Full Sequence |
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| Protein Sequence Length: 810 Download |
| MLMHEIFKSL MELTHYASCS SHYLPKLLSP HKPPQWWNPT PRGKSSNNWS AKPSNMRFSK 60 WVVAAVGSGA EAETVVVEKP KLQPFLVFEG CPAPLGATAR DGGVNFAVYS GNAVSATLCL 120 ISASDLEEDR VTEQISLDPL TNKTGDVWHV FLKGNFENIV YGYKFDGKFS PEEGHYYDSS 180 RLLLDPYAKA VISRGEFGIL GPEGNCWPLM AGMIPSSDAE FDWEGDLPLK YPQKDLIIYE 240 MHVRGFTRHE SSRTKFPGTY HGVVEKLDHL KELGVNCIEL MPCHEFNELE YFSYNSVLDD 300 YRYTCISMVN FWGYSTVNYF SPMIRYSSAG IHNCGHDAIN EVKLLIREAH KRGIEVLMDV 360 VFNHTAEGNE NGPILSFRGV DNSVYYMLAP KGEFYNYSGC GNTFNCNHPI VRQFILDCLR 420 YWVTEMHVDG FRFDLASIMT RGSSLWDALN VYGNPAEGDS LTTGTPLSSP PLIDMISNDP 480 ILRGVKLIAE AWDAGGLYQV GMFPHWGLWS EWNGKYRDIV RQFIKGSDGF SGAFAECLCG 540 SPNLYQEGGR KPWNSINFVC AHDGFTLADL VTYNKKHNNA NGEDNNDGEN HNNSWNCGQE 600 GEFASISVKK LRKRQMRNFF LCLMVSQGVP MIYMGDEYGH TKGGNNNTYC QDNYMNYFRW 660 DKKEESLSDF FRFCCLMSKF RQECESLGLN DFPTAERLQW HGRTPGMPDW SKTSRFVAFT 720 MVDSVKGEIY VAFNTSHLPI IITLPERPGY RWQPLVDTSK PAPFDFLSND VPERDTAVKQ 780 YSQFTEANLY PMLSYSSIIL LLCPVDENA* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK14510 | PRK14510 | 1.0e-133 | 81 | 749 | 706 | + putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional | ||
| PRK03705 | PRK03705 | 9.0e-149 | 90 | 670 | 600 | + glycogen debranching enzyme; Provisional | ||
| cd11326 | AmyAc_Glg_debranch | 0 | 221 | 683 | 468 | + 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 | 0 | 92 | 778 | 716 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
| TIGR02100 | glgX_debranch | 0 | 89 | 764 | 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]. | ||
| 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 |
| DDBJ | BAF52941.1 | 0 | 63 | 809 | 51 | 791 | isoamylase-type starch-debranching enzyme 1 [Phaseolus vulgaris] |
| EMBL | CBI40669.1 | 0 | 1 | 809 | 1 | 809 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002265964.1 | 0 | 56 | 809 | 1 | 742 | PREDICTED: similar to isoamylase-type starch-debranching enzyme 1 [Vitis vinifera] |
| RefSeq | XP_002308090.1 | 0 | 11 | 808 | 1 | 826 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002324659.1 | 0 | 11 | 806 | 1 | 792 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2vuy_B | 0 | 90 | 729 | 15 | 647 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 2vuy_A | 0 | 90 | 729 | 15 | 647 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 2vr5_B | 0 | 90 | 729 | 15 | 647 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 2vr5_A | 0 | 90 | 729 | 15 | 647 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 2vnc_B | 0 | 90 | 729 | 15 | 647 | 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 |
| HO800235 | 265 | 503 | 767 | 0 |
| HO800235 | 119 | 329 | 447 | 0 |
| HO800235 | 58 | 444 | 501 | 0 |
| HO431228 | 419 | 382 | 800 | 0 |
| DW065550 | 291 | 482 | 772 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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