Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10006762m |
Family | GH13 |
Protein Properties | Length: 879 Molecular Weight: 98429.7 Isoelectric Point: 6.1647 |
Chromosome | Chromosome/Scaffold: 5 Start: 14813468 End: 14816170 |
Description | debranching enzyme 1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 379 | 708 | 7.5e-27 |
NVAGTFSGVAEKVNHLKTLGTNAVLLEPIFSFSEQEGPYFPFHFFSPMDMYGPSNGHESAVNSMKEMVKKLHSQGIEVILEVVFTHTAESGALRGIDDSC YYYKGRANDLDSKSYLNCNYPVVQQLILESLRYWVTEFHVDGFCFINASSLLRGVHGEHLSRPPLVEAIAFDPLLAETKLIADCWDPHDSMVIPKEVRFP HWKRWAELNTRYCRNVRNFVRGRGVLSDLATRICGSGDIFTDGRGPAFSFNYISRNSGLSLVDLVSFSGPELASELSWNCGEEGATNKSAVLQRRLKQIR NFLFIQYISLGIPVLNMGDECGISTKGSPL |
Full Sequence |
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Protein Sequence Length: 879 Download |
MAAWSLSVGI GSCCLSNSIT RTWKFPSTRF FTGMNKTKPG SETLIVTGKP LLRDQLSRIC 60 ASKTSIELRD QVSTRSAQAN DLKKAVSYLF RTKAGTLVKV KVEKKREKYS ILVYVSSLEV 120 SGDDESRPVM VWGVYRSDSS CFLPLDFENS SQELQTHTTE TPFVKSSLSE LMLGLEFDGK 180 ESPFYLSFHL KLLSGKDPDG LKMLTHKDAN FCVPVGFTAG QPLPLGLSSG PGNDSWNFAF 240 FSRHSRGVVL CLYDDSTTDK PALELDLDPY VNRTGDVWHA SVEKTWDFVR YGYRCKENVH 300 SEEEEEEEGN VEAEKIVLDP YATVIGKSVS QKFLGSLFKN SSFDWGNDVS PNIPLEKLIV 360 YRLNVKGFTQ HKSCKLPSNV AGTFSGVAEK VNHLKTLGTN AVLLEPIFSF SEQEGPYFPF 420 HFFSPMDMYG PSNGHESAVN SMKEMVKKLH SQGIEVILEV VFTHTAESGA LRGIDDSCYY 480 YKGRANDLDS KSYLNCNYPV VQQLILESLR YWVTEFHVDG FCFINASSLL RGVHGEHLSR 540 PPLVEAIAFD PLLAETKLIA DCWDPHDSMV IPKEVRFPHW KRWAELNTRY CRNVRNFVRG 600 RGVLSDLATR ICGSGDIFTD GRGPAFSFNY ISRNSGLSLV DLVSFSGPEL ASELSWNCGE 660 EGATNKSAVL QRRLKQIRNF LFIQYISLGI PVLNMGDECG ISTKGSPLLK SRKPFDWKML 720 ASAFGVQITQ FISFMTSVRE RRSDVFQRRN FLKPENIVWY ANDQTTPSWE DPSSKFLALG 780 IKAESEEEET ASLVEPTEPK NNDLFIGFNA GDHPENVILP TLPDGSKWRR LVDTALPFPG 840 FFSVEGETVA AVEQTQQLVV YEMKPYSCTL FETINSTA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11346 | AmyAc_plant_IsoA | 2.0e-23 | 677 | 747 | 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. | ||
COG1523 | PulA | 1.0e-99 | 218 | 851 | 721 | + Type II secretory pathway, pullulanase PulA and related glycosidases [Carbohydrate transport and metabolism] | ||
TIGR02100 | glgX_debranch | 2.0e-102 | 219 | 839 | 706 | + 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 | 5.0e-112 | 343 | 705 | 405 | + 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 | 7.0e-129 | 354 | 618 | 278 | + 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 | |
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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 | AAM98123.1 | 0 | 1 | 878 | 1 | 882 | putative isoamylase [Arabidopsis thaliana] |
DDBJ | BAF52942.1 | 0 | 50 | 877 | 47 | 864 | isoamylase-type starch-debranching enzyme 2 [Phaseolus vulgaris] |
RefSeq | NP_171830.1 | 0 | 1 | 878 | 1 | 882 | isoamylase, putative / starch debranching enzyme, putative [Arabidopsis thaliana] |
RefSeq | XP_002271798.1 | 0 | 7 | 873 | 7 | 877 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002533079.1 | 0 | 57 | 873 | 60 | 867 | isoamylase, putative [Ricinus communis] |
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 | 220 | 706 | 15 | 553 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vuy_A | 0 | 220 | 706 | 15 | 553 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vr5_B | 0 | 220 | 706 | 15 | 553 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vr5_A | 0 | 220 | 706 | 15 | 553 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2vnc_B | 0 | 220 | 706 | 15 | 553 | A Chain A, Crystal Structure Of Glycogen Debranching Enzyme Trex From Sulfolobus Solfataricus |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES817618 | 345 | 356 | 693 | 0 |
EV528320 | 255 | 529 | 782 | 0 |
GE635058 | 275 | 448 | 722 | 0 |
DR926647 | 306 | 365 | 666 | 0 |
EV223877 | 231 | 613 | 843 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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