y
Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10018631m |
Family | GH13 |
Protein Properties | Length: 414 Molecular Weight: 47091.9 Isoelectric Point: 8.3527 |
Chromosome | Chromosome/Scaffold: 9 Start: 1982705 End: 1985960 |
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 | 48 | 333 | 1.9e-30 |
KVPDIAKSGFTSAWLPPPSQSLAPEGYLPQDLYSLNSAYGSEHLLKSLLRKMKQYKVRAMADIVINHRVGTTRGHGGMYNRYDGISLPWDEHAVTSCTGG LGRRSTGDNFNGVPNVDHTQHFVRKDLIGWLRWLRNTVGFQDFRFDFARGYSAQYVKEYIGAAKPLFSVGEFWDSCKYNGHGLDYNQDSHRQRIINWIDA TGQLSAAFDFTTKGILQEAVKGQFWRLSDPQGKPPGVMGWWPSRAVTFLDNHDTGSTQAHWPFPSHHVMEGYAYILTHPGIPCVFY |
Full Sequence |
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Protein Sequence Length: 414 Download |
MGYYNNVFDG CNDQTDIGGV IRDGREVILQ AYNWESHKHD WWKNLDGKVP DIAKSGFTSA 60 WLPPPSQSLA PEGYLPQDLY SLNSAYGSEH LLKSLLRKMK QYKVRAMADI VINHRVGTTR 120 GHGGMYNRYD GISLPWDEHA VTSCTGGLGR RSTGDNFNGV PNVDHTQHFV RKDLIGWLRW 180 LRNTVGFQDF RFDFARGYSA QYVKEYIGAA KPLFSVGEFW DSCKYNGHGL DYNQDSHRQR 240 IINWIDATGQ LSAAFDFTTK GILQEAVKGQ FWRLSDPQGK PPGVMGWWPS RAVTFLDNHD 300 TGSTQAHWPF PSHHVMEGYA YILTHPGIPC VFYDHFYDWG SSIHDQIVKL IDIRRRQDIH 360 SRSTVRVLEA RANLYAAVVG EKLCMKLGDA SWCPSGRDWT LATSGHRYAV WHK* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 9.0e-40 | 26 | 356 | 410 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 9.0e-137 | 26 | 413 | 407 | + alpha-amylase; Provisional | ||
PLN02784 | PLN02784 | 3.0e-158 | 24 | 413 | 397 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 9.0e-166 | 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 | 15 | 413 | 401 | + 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 | AAF17626.1 | 0 | 1 | 413 | 1 | 412 | AC009978_2 T23E18.6 [Arabidopsis thaliana] |
GenBank | AAX33234.1 | 0 | 14 | 413 | 15 | 414 | cytosolic alpha-amylase [Malus x domestica] |
RefSeq | NP_177740.1 | 0 | 1 | 413 | 1 | 413 | AMY2 (ALPHA-AMYLASE-LIKE 2); alpha-amylase/ calcium ion binding / catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002301935.1 | 0 | 8 | 413 | 1 | 406 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510621.1 | 0 | 18 | 413 | 3 | 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, Solution Structure Of The C-Terminal Domain Ole E 9 |
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 | 404 | 11 | 414 | 0 |
HO798064 | 377 | 20 | 396 | 0 |
BU103706 | 399 | 18 | 414 | 0 |
CJ999444 | 279 | 103 | 381 | 0 |
HO798064 | 34 | 381 | 414 | 0.00000007 |
Sequence Alignments (This image is cropped. Click for full image.) |
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