Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.005G139200.1 |
Family | GH13 |
Protein Properties | Length: 732 Molecular Weight: 82565.1 Isoelectric Point: 5.2879 |
Chromosome | Chromosome/Scaffold: 05 Start: 36287009 End: 36293991 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 360 | 650 | 1.3e-39 |
KEKASEISSLGFTVIWLPPPTESVSPEGYLPKDLYNLNSRYGTIDELKDLVKSLHGVGLKVLGDVVLNHRCAHYQNQNGVWNIFGGRLNWDDRAVVGDDP HFQGRGNKSSGDNFHAAPNIDHSQDFVRKDLIEWLCWLREEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVD WINATNGTAGAFDVTTKGILHSALERREYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 732 Download |
MWPHGSIPIK DYAIETPFKK PSKDDTFHEV KIDFNPSSAI EAIHFILKDE ETGASYQHKG 60 RDFRVSLVNY LEDDGNMIHT KRSFGKWPDA VEQLPNMVLK AEASCDSKNE NRRLEGFYEE 120 QPIVKEVSVG NMVNVAIRKF PDAANIVLHL ETDIPGDVVV HWGVCRDDAK TWEISAVPYP 180 PETTVFRNKA LRTLLQPTGN GSRALFTLDE KLDGFLFVLK LDANSWVNFQ GNDFYIPLSS 240 ARSVKGQSDS ESEETSGKAH TDGIINEIRN LVSGLNSEKS LQTKVKEAKE SILNEIEKLA 300 AEAYSIFRSS TPSYPEEDSD ADDAEPTINI SSGTGSGFEI LCQGFNWESN KSGRWYMELK 360 EKASEISSLG FTVIWLPPPT ESVSPEGYLP KDLYNLNSRY GTIDELKDLV KSLHGVGLKV 420 LGDVVLNHRC AHYQNQNGVW NIFGGRLNWD DRAVVGDDPH FQGRGNKSSG DNFHAAPNID 480 HSQDFVRKDL IEWLCWLREE IGYDGWRLDF VRGFWGGYVK DYLDASEPYF AVGEYWDSLS 540 YTYGEMDHNQ DAHRQRIVDW INATNGTAGA FDVTTKGILH SALERREYWR LSDQKGKPPG 600 VVGWWPSRAV TFIENHDTGS TQGHWRFPGG KEMQGYAYIL THPGTPAVFY DHIVSHHRSE 660 IGALISLRNR NKIHCRSIVE IVKAERDVYA ATIDDRVAMK IGPGYYEPPS GPQRWSLALE 720 GYDYKVWEAS S* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02784 | PLN02784 | 0.004 | 142 | 238 | 106 | + alpha-amylase | ||
PLN00196 | PLN00196 | 9.0e-131 | 328 | 728 | 414 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-153 | 340 | 679 | 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 | 1.0e-162 | 336 | 728 | 400 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 730 | 754 | + 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 |
EMBL | CBI32016.1 | 0 | 1 | 730 | 138 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 730 | 138 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 730 | 145 | 900 | 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 | 2qpu_C | 0 | 339 | 728 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 339 | 728 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 339 | 728 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 339 | 728 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 339 | 728 | 2 | 403 | 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 |
EG631183 | 758 | 1 | 730 | 0 |
HO826981 | 401 | 330 | 730 | 0 |
HO811991 | 298 | 433 | 730 | 0 |
ES805448 | 328 | 297 | 623 | 0 |
EG631183 | 177 | 77 | 238 | 0.14 |
Sequence Alignments (This image is cropped. Click for full image.) |
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