y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29104.m000024 |
Family | GH13 |
Protein Properties | Length: 556 Molecular Weight: 61061.1 Isoelectric Point: 5.9225 |
Chromosome | Chromosome/Scaffold: 29104 Start: 10 End: 1677 |
Description | |
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 | 84 | 486 | 1.5e-35 |
GYCAYVQNFGGTLNGVAERIPYLQEMGVSYLHLLPFLRARQGENDGGFAVSDFDDVEPSLGSNADLVALTTRLREAGISLCSDFILNHVADDHAWALAAK AGDEQARAMFLFYPDREMPDRYERTLGQVFPQVAPGNFTPAMGGWVWSTFYPYQWDLNYANPAVFAAMAATLLRLANRGIEVFRLDSTAFLWKREGTNSM NQQEAHQILQALRAIVDIVAPGVLLKAEAIVPTRELPAYLGSAEARECHIAYHSSLMAAGWLALSEQGTGVLREVIGNTPALPPSATWLSYVRCHDDIGW NVLRAEASADGSDANARLARASRFFAGGEGSYAAGAAFQSTDPNAAHGSNGAAASLVGLERADSGAARALAMRRLQLLHGLALSFGALPVLYMGDELAME NDY |
Full Sequence |
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Protein Sequence Length: 556 Download |
SDRMLAVLPD ALRAQAVRRL AIHEPVLRKL LAGLYGQQAD FDAWMGKLME SLGALYAARP 60 AALRELDAQR EAQPEWFLSQ RMLGYCAYVQ NFGGTLNGVA ERIPYLQEMG VSYLHLLPFL 120 RARQGENDGG FAVSDFDDVE PSLGSNADLV ALTTRLREAG ISLCSDFILN HVADDHAWAL 180 AAKAGDEQAR AMFLFYPDRE MPDRYERTLG QVFPQVAPGN FTPAMGGWVW STFYPYQWDL 240 NYANPAVFAA MAATLLRLAN RGIEVFRLDS TAFLWKREGT NSMNQQEAHQ ILQALRAIVD 300 IVAPGVLLKA EAIVPTRELP AYLGSAEARE CHIAYHSSLM AAGWLALSEQ GTGVLREVIG 360 NTPALPPSAT WLSYVRCHDD IGWNVLRAEA SADGSDANAR LARASRFFAG GEGSYAAGAA 420 FQSTDPNAAH GSNGAAASLV GLERADSGAA RALAMRRLQL LHGLALSFGA LPVLYMGDEL 480 AMENDYSYRH RPQHAMDSRW LQRPMFDHTR WSARDDTASN AGQMYQSLIR MVRVRRQQDA 540 LAANAPRTLL DDAPDG 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11356 | AmyAc_Sucrose_phosphorylase-like_1 | 7.0e-5 | 462 | 551 | 92 | + Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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. | ||
cd11356 | AmyAc_Sucrose_phosphorylase-like_1 | 1.0e-43 | 111 | 382 | 276 | + Alpha amylase catalytic domain found in sucrose phosphorylase-like proteins (also called sucrose glucosyltransferase, disaccharide glucosyltransferase, and sucrose-phosphate alpha-D glucosyltransferase). Sucrose phosphorylase is a bacterial enzyme that catalyzes the phosphorolysis of sucrose to yield glucose-1-phosphate and fructose. These enzymes do not have the conserved calcium ion present in other alpha amylase family enzymes. 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. | ||
TIGR02456 | treS_nterm | 2.0e-45 | 94 | 381 | 290 | + trehalose synthase. Trehalose synthase interconverts maltose and alpha, alpha-trehalose by transglucosylation. This is one of at least three mechanisms for biosynthesis of trehalose, an important and widespread compatible solute. However, it is not driven by phosphate activation of sugars and its physiological role may tend toward trehalose degradation. This view is accentuated by numerous examples of fusion to a probable maltokinase domain. The sequence region described by this model is found both as the whole of a trehalose synthase and as the N-terminal region of a larger fusion protein that includes trehalose synthase activity. Several of these fused trehalose synthases have a domain homologous to proteins with maltokinase activity from Actinoplanes missouriensis and Streptomyces coelicolor (PMID:15378530) [Energy metabolism, Biosynthesis and degradation of polysaccharides]. | ||
cd11334 | AmyAc_TreS | 2.0e-48 | 85 | 381 | 315 | + Alpha amylase catalytic domain found in Trehalose synthetase. Trehalose synthetase (TreS) catalyzes the reversible interconversion of trehalose and maltose. The enzyme catalyzes the reaction in both directions, but the preferred substrate is maltose. Glucose is formed as a by-product of this reaction. It is believed that the catalytic mechanism may involve the cutting of the incoming disaccharide and transfer of a glucose to an enzyme-bound glucose. This enzyme also catalyzes production of a glucosamine disaccharide from maltose and glucosamine. 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. | ||
cd11324 | AmyAc_Amylosucrase | 0 | 13 | 541 | 535 | + Alpha amylase catalytic domain found in Amylosucrase. Amylosucrase is a glucosyltransferase that catalyzes the transfer of a D-glucopyranosyl moiety from sucrose onto an acceptor molecule. When the acceptor is another saccharide, only alpha-1,4 linkages are produced. Unlike most amylopolysaccharide synthases, it does not require any alpha-D-glucosyl nucleoside diphosphate substrate. In the presence of glycogen it catalyzes the transfer of a D-glucose moiety onto a glycogen branch, but in its absence, it hydrolyzes sucrose and synthesizes polymers, smaller maltosaccharides, and sucrose isoforms. 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_002535566.1 | 0 | 1 | 556 | 1 | 556 | alpha-amylase, putative [Ricinus communis] |
RefSeq | YP_003375236.1 | 0 | 12 | 532 | 25 | 550 | probable sucrose hydrolase protein [Xanthomonas albilineans] |
RefSeq | YP_450025.1 | 0 | 19 | 544 | 30 | 560 | amylosucrase or alpha amylase [Xanthomonas oryzae pv. oryzae MAFF 311018] |
RefSeq | ZP_06484144.1 | 0 | 14 | 544 | 25 | 560 | amylosucrase or alpha amylase [Xanthomonas campestris pv. vasculorum NCPPB702] |
RefSeq | ZP_06488861.1 | 0 | 14 | 544 | 25 | 560 | amylosucrase or alpha amylase [Xanthomonas campestris pv. musacearum NCPPB4381] |
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 | 2wpg_A | 0 | 19 | 544 | 31 | 561 | A Chain A, Sucrose Hydrolase |
PDB | 3czg_A | 0 | 17 | 544 | 28 | 560 | A Chain A, Sucrose Hydrolase |
PDB | 3cze_A | 0 | 17 | 544 | 28 | 560 | A Chain A, Crystal Structure Analysis Of Sucrose Hydrolase (Suh)- Tris Complex |
PDB | 3czl_A | 0 | 17 | 544 | 28 | 560 | A Chain A, Crystal Structure Analysis Of Sucrose Hydrolase (Suh)- Tris Complex |
PDB | 3czk_A | 0 | 17 | 544 | 28 | 560 | A Chain A, Crystal Structure Analysis Of Sucrose Hydrolase(Suh) E322q- Sucrose Complex |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX919337 | 262 | 127 | 388 | 2e-24 |
FG599800 | 149 | 233 | 381 | 1e-23 |
BE249225 | 153 | 235 | 387 | 2e-21 |
CX943088 | 154 | 229 | 382 | 0.00000000000002 |
JG858766 | 200 | 61 | 251 | 0.0000000009 |
Sequence Alignments (This image is cropped. Click for full image.) |
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