Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a007250m |
Family | GH13 |
Protein Properties | Length: 414 Molecular Weight: 47105.9 Isoelectric Point: 7.5159 |
Chromosome | Chromosome/Scaffold: 87 Start: 243285 End: 247789 |
Description | alpha-amylase-like 2 |
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 | 47 | 333 | 3.2e-30 |
KKVPDIAKSGFTSAWLPPATQSFAPEGYLPQNLYSLNSSYGSEHLLKALLNKMKTHKVRAMADIVINHRVGTTQGHGGMYNRYDGIPLAWDERAVTVCTG GKGNKSTGDNFNGVPNIDHTQEFVRKDIIDWLRWLRNTIGFQDFRFDFARGYSAKYVREYIDGVKPIFCVGEYWDSCNYRGSYLEYNQDSHRQRIINWID GTGQLSAAFDFTTKGILQEAVKGELWRLRDSQGKPPGVMGWWPSRTVTFLDNHDTGSTQAHWPFPSSHIMEGYAYILTHPGIPSVFY |
Full Sequence |
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Protein Sequence Length: 414 Download |
MGYLSNEIDQ DNKENDPVAA IRNGKEVILQ AFNWESHKHD WWSNLEKKVP DIAKSGFTSA 60 WLPPATQSFA PEGYLPQNLY SLNSSYGSEH LLKALLNKMK THKVRAMADI VINHRVGTTQ 120 GHGGMYNRYD GIPLAWDERA VTVCTGGKGN KSTGDNFNGV PNIDHTQEFV RKDIIDWLRW 180 LRNTIGFQDF RFDFARGYSA KYVREYIDGV KPIFCVGEYW DSCNYRGSYL EYNQDSHRQR 240 IINWIDGTGQ LSAAFDFTTK GILQEAVKGE LWRLRDSQGK PPGVMGWWPS RTVTFLDNHD 300 TGSTQAHWPF PSSHIMEGYA YILTHPGIPS VFYDHFYDWG SPIHDEIVKL IDIRKLQGIH 360 SRSPINILEA QPNLYAANIG DKISMKIGDG SWSPPGKEWT LATSGHRYAV WKK* 420 |
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 | 23 | 355 | 415 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 3.0e-136 | 26 | 413 | 407 | + alpha-amylase; Provisional | ||
PLN02784 | PLN02784 | 6.0e-160 | 23 | 413 | 398 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-164 | 27 | 365 | 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 | 19 | 413 | 397 | + 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 | AAA91884.1 | 0 | 11 | 413 | 5 | 407 | alpha-amylase [Solanum tuberosum] |
GenBank | ACV30014.1 | 0 | 11 | 413 | 5 | 407 | alpha-amylase [Solanum tuberosum] |
GenBank | ACZ26470.1 | 0 | 11 | 413 | 5 | 407 | alpha-amylase [Solanum tuberosum] |
EMBL | CAH58639.1 | 0 | 2 | 413 | 3 | 413 | alpha-amylase [Plantago major] |
RefSeq | XP_002510621.1 | 0 | 19 | 413 | 4 | 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 | 26 | 413 | 1 | 402 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1ava_B | 0 | 26 | 413 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 26 | 413 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 26 | 413 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 26 | 413 | 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 | 414 | 1 | 414 | 0 |
HO798064 | 406 | 17 | 413 | 0 |
BU103706 | 396 | 21 | 414 | 0 |
DV704349 | 306 | 13 | 318 | 0 |
HO798064 | 33 | 382 | 414 | 0.00001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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