Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30170.m014309 |
Family | GH13 |
Protein Properties | Length: 398 Molecular Weight: 45616.6 Isoelectric Point: 9.23 |
Chromosome | Chromosome/Scaffold: 30170 Start: 3852906 End: 3857164 |
Description | alpha-amylase-like 2 |
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 | 31 | 318 | 1.2e-30 |
ERKVPDIAKSGFTSAWLPPPSQSLSPEGYLPQNLYSLNSVYGSEHLLKALLQKMKQYNVRAMADIVINHRIGTTKGHGGMYNRYDGIPIPWDERAVTLCT GGLGNRSTGDNFNGVPNIDHTQHFVRKDIIGWLKWLRNVVGFQDFRFDFARGYSAKYVKEYIEAAKPIFSIGEYWDSCNYSGTYLEYSQDSHRQRIVNWI DCTGQLSAAFDFTTKGILQEAVKGQLWRLRDSKGKPPGVMGWWPSRAVTFIDNHDTGSTQGHWPFPSHHIMEGYAYILTHPGIPTVFY |
Full Sequence |
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Protein Sequence Length: 398 Download |
MQGAAVRNGK EILLQAFNWE SHKHDWWRNL ERKVPDIAKS GFTSAWLPPP SQSLSPEGYL 60 PQNLYSLNSV YGSEHLLKAL LQKMKQYNVR AMADIVINHR IGTTKGHGGM YNRYDGIPIP 120 WDERAVTLCT GGLGNRSTGD NFNGVPNIDH TQHFVRKDII GWLKWLRNVV GFQDFRFDFA 180 RGYSAKYVKE YIEAAKPIFS IGEYWDSCNY SGTYLEYSQD SHRQRIVNWI DCTGQLSAAF 240 DFTTKGILQE AVKGQLWRLR DSKGKPPGVM GWWPSRAVTF IDNHDTGSTQ GHWPFPSHHI 300 MEGYAYILTH PGIPTVFYDH FYDWGNSIHE QIVKLIDIRK RQDINSRSSI RILEAQPNLY 360 SAIIGEKVCM KIGDGSWSPS GREWTLATSG HRYAVWQK |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-41 | 8 | 341 | 411 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 5.0e-136 | 11 | 398 | 407 | + alpha-amylase; Provisional | ||
PLN02784 | PLN02784 | 3.0e-162 | 4 | 398 | 402 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-165 | 12 | 350 | 343 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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. | ||
PLN02361 | PLN02361 | 0 | 1 | 398 | 400 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004556 | alpha-amylase activity |
GO:0005509 | calcium ion binding |
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 | AAX33234.1 | 0 | 3 | 398 | 19 | 414 | cytosolic alpha-amylase [Malus x domestica] |
GenBank | AAY85174.1 | 0 | 3 | 398 | 13 | 407 | alpha-amylase 2 [Manihot esculenta] |
RefSeq | NP_177740.1 | 0 | 3 | 398 | 18 | 413 | AMY2 (ALPHA-AMYLASE-LIKE 2); alpha-amylase/ calcium ion binding / catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002301935.1 | 0 | 3 | 398 | 11 | 406 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510621.1 | 0 | 1 | 398 | 1 | 398 | alpha-amylase, 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 | 1bg9_A | 0 | 11 | 398 | 1 | 402 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 1ava_B | 0 | 11 | 398 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 11 | 398 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 11 | 398 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 11 | 398 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO780661 | 395 | 4 | 398 | 0 |
HO798064 | 369 | 4 | 372 | 0 |
BU103706 | 398 | 3 | 398 | 0 |
CO073142 | 294 | 105 | 398 | 0 |
HO798064 | 33 | 366 | 398 | 0.0000001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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