y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 35877.m000015 |
Family | GH13 |
Protein Properties | Length: 371 Molecular Weight: 41820.4 Isoelectric Point: 6.2522 |
Chromosome | Chromosome/Scaffold: 35877 Start: 73 End: 1188 |
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 | 1 | 270 | 0 |
MGVDILWLMPIQPIGEKNRKGTLGSYYAVRDYTAVNPEFGTLDDLKALVKQAHGLGMHVIIDWVANHTAFDNPWTQEHSDWYLKNEKGEIYPVTYTDGAE PEYWTDVTGLDWSKPGLWKGMTDAMLYWVREADIDGFRCDVAGKVPTPFWNQARAELDRVKPVFMLAEADKPELHEHAFDMTYGWDTKDLFKAIAKGKAD ARTLADFLEHPPKAFPPGAYRMRFTSNHDENSWAGSDVELYGPAFKAMAVLAATLPGMPLIYGGQEAGLD |
Full Sequence |
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Protein Sequence Length: 371 Download |
MGVDILWLMP IQPIGEKNRK GTLGSYYAVR DYTAVNPEFG TLDDLKALVK QAHGLGMHVI 60 IDWVANHTAF DNPWTQEHSD WYLKNEKGEI YPVTYTDGAE PEYWTDVTGL DWSKPGLWKG 120 MTDAMLYWVR EADIDGFRCD VAGKVPTPFW NQARAELDRV KPVFMLAEAD KPELHEHAFD 180 MTYGWDTKDL FKAIAKGKAD ARTLADFLEH PPKAFPPGAY RMRFTSNHDE NSWAGSDVEL 240 YGPAFKAMAV LAATLPGMPL IYGGQEAGLD KRIEFFEKDP IQWKDYAYGP FYTKLLALKH 300 ANPALWNGQY GGPVQVLKTG NDKVFAFRRA LKGNSVQVTV NVSGEAQRFN LPGGKQQTLA 360 AWDYRIDARG K 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11316 | AmyAc_bac2_AmyA | 7.0e-34 | 1 | 308 | 391 | + Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Chloroflexi, Dictyoglomi, and Fusobacteria. 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. | ||
cd11338 | AmyAc_CMD | 6.0e-37 | 1 | 308 | 344 | + Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). 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. | ||
pfam00128 | Alpha-amylase | 1.0e-37 | 1 | 269 | 304 | + Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain. | ||
cd11347 | AmyAc_1 | 6.0e-42 | 1 | 310 | 371 | + Alpha amylase catalytic domain found in an uncharacterized protein family. 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. | ||
cd11313 | AmyAc_arch_bac_AmyA | 1.0e-163 | 1 | 308 | 312 | + Alpha amylase catalytic domain found in archaeal and bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes firmicutes, bacteroidetes, and proteobacteria. 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: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 |
RefSeq | XP_002538047.1 | 0 | 1 | 371 | 1 | 371 | alpha-amylase, putative [Ricinus communis] |
RefSeq | YP_001343634.1 | 0 | 1 | 351 | 52 | 400 | alpha amylase catalytic region [Actinobacillus succinogenes 130Z] |
RefSeq | YP_003007378.1 | 0 | 1 | 371 | 53 | 436 | alpha amylase, catalytic region [Aggregatibacter aphrophilus NJ8700] |
RefSeq | YP_003387358.1 | 0 | 1 | 366 | 78 | 464 | alpha amylase catalytic region [Spirosoma linguale DSM 74] |
RefSeq | ZP_01134431.1 | 0 | 1 | 369 | 78 | 463 | alpha-amylase, putative [Pseudoalteromonas tunicata D2] |
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 | 4gkl_B | 0 | 1 | 344 | 37 | 379 | A Chain A, Crystal Structure Of A Noncanonic Maltogenic Alpha-amylase Amyb From Thermotoga Neapolitana |
PDB | 4gkl_A | 0 | 1 | 344 | 37 | 379 | A Chain A, Crystal Structure Of A Noncanonic Maltogenic Alpha-amylase Amyb From Thermotoga Neapolitana |
PDB | 3dhu_D | 0 | 1 | 300 | 42 | 348 | A Chain A, Crystal Structure Of An Alpha-Amylase From Lactobacillus Plantarum |
PDB | 3dhu_C | 0 | 1 | 300 | 42 | 348 | A Chain A, Crystal Structure Of An Alpha-Amylase From Lactobacillus Plantarum |
PDB | 3dhu_B | 0 | 1 | 300 | 42 | 348 | A Chain A, Crystal Structure Of An Alpha-Amylase From Lactobacillus Plantarum |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GW470024 | 149 | 1 | 131 | 0.0000000003 |
GW478424 | 149 | 1 | 131 | 0.0000000003 |
GW478572 | 149 | 1 | 131 | 0.0000000006 |
EH759953 | 169 | 1 | 140 | 0.00000005 |
EH762334 | 169 | 1 | 140 | 0.00000005 |
Sequence Alignments (This image is cropped. Click for full image.) |
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