y
Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr8g101490.1 |
Family | GH13 |
Protein Properties | Length: 823 Molecular Weight: 93245.8 Isoelectric Point: 6.2347 |
Chromosome | Chromosome/Scaffold: 8 Start: 29353323 End: 29363886 |
Description | isoamylase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 240 | 661 | 0 |
KAEFPGTYLGVVEKLDHLKELGVNCIELMPCHEFNELEYYSYNAIQGDYRVNFWGYSTINYFSPMIRYSSAGIQNCGRDGINEMKLLIKEAHKRGIEVIM DVVFNHTAEGNEKGPIISFRGVDNSVYYMVAPKGEFYNYSGCGNTFNCNHPVVRKFIVDCLRYWVTEMHVDGFRFDLASIMTRSSSLWNGVNVFGAPIEG DFLTTGTPLSSPPLIDMISIDPILRGVKLIAEAWDAGGLYQVGTFPHWGIWSEWNGKVSADYRDTVRQFIKGTDGFAGAFAECICGSPNLYQLNLKVVFS VAIVYSSTLFLCGGHYSIFLVQGGRKPWNSINLVCAHDGFTLADLVTYNNKHNLPNGEDNNDGENHNSSWNCGEEGEFVSASVKKMRKRQMRNFFLSLMV SQGVPMIFMGDEYGHTKGGNNN |
Full Sequence |
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Protein Sequence Length: 823 Download |
MACIPHILSP LSHSTTLANL INITNFEIHN RTSIIISPNS RPKKKKKKIF AIGNRVGVDT 60 ETAVIEIEKR QLQLSKGHPS PYGATPQEDG VNFAINSLNS LSATLCFFTL SDFKNNKVTE 120 YITLDPLVNK TGCVWHVFLK GDFKDMLYAY KFDGKFSPQQ GHYYDSSRIL IDPYAKAVIS 180 RGEFGEVGPD GNCWPQMAGM VPFDNEEFDW EGDLPLKYPQ KDLIIYEMHV RGFTKHESSK 240 AEFPGTYLGV VEKLDHLKEL GVNCIELMPC HEFNELEYYS YNAIQGDYRV NFWGYSTINY 300 FSPMIRYSSA GIQNCGRDGI NEMKLLIKEA HKRGIEVIMD VVFNHTAEGN EKGPIISFRG 360 VDNSVYYMVA PKGEFYNYSG CGNTFNCNHP VVRKFIVDCL RYWVTEMHVD GFRFDLASIM 420 TRSSSLWNGV NVFGAPIEGD FLTTGTPLSS PPLIDMISID PILRGVKLIA EAWDAGGLYQ 480 VGTFPHWGIW SEWNGKVSAD YRDTVRQFIK GTDGFAGAFA ECICGSPNLY QLNLKVVFSV 540 AIVYSSTLFL CGGHYSIFLV QGGRKPWNSI NLVCAHDGFT LADLVTYNNK HNLPNGEDNN 600 DGENHNSSWN CGEEGEFVSA SVKKMRKRQM RNFFLSLMVS QGVPMIFMGD EYGHTKGGNN 660 NTYCHDNYLN YFRWDKKEES SSDFFRFCRL LTKFRQECES LGLDDFPTSE RLQWHGHFPV 720 TPDWSESSRF VAFTLMDLVK GEVYVAFNTS HLPFTITLPE RPGYRWEPLV DTSKKAPYDF 780 LTPDLPGRDI AIQQYAQFLD ANMYPMLSYS SIILLRTPDV NA* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK14510 | PRK14510 | 6.0e-124 | 75 | 763 | 721 | + putative bifunctional 4-alpha-glucanotransferase/glycogen debranching enzyme; Provisional | ||
PRK03705 | PRK03705 | 5.0e-140 | 73 | 701 | 645 | + glycogen debranching enzyme; Provisional | ||
cd11326 | AmyAc_Glg_debranch | 0 | 208 | 697 | 495 | + 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 | 73 | 796 | 751 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02100 | glgX_debranch | 0 | 77 | 777 | 739 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAZ81835.1 | 0 | 20 | 822 | 22 | 791 | isoamylase isoform 1 [Pisum sativum] |
DDBJ | BAF52941.1 | 0 | 10 | 822 | 18 | 791 | isoamylase-type starch-debranching enzyme 1 [Phaseolus vulgaris] |
EMBL | CBI40669.1 | 0 | 49 | 822 | 63 | 809 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002308090.1 | 0 | 70 | 821 | 76 | 825 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002324659.1 | 0 | 55 | 822 | 58 | 794 | predicted protein [Populus trichocarpa] |
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 | 70 | 743 | 8 | 647 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vuy_A | 0 | 70 | 743 | 8 | 647 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vr5_B | 0 | 70 | 743 | 8 | 647 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vr5_A | 0 | 70 | 743 | 8 | 647 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vnc_B | 0 | 70 | 743 | 8 | 647 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |