y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10000912 |
Family | GH13 |
Protein Properties | Length: 900 Molecular Weight: 102924 Isoelectric Point: 5.6268 |
Chromosome | Chromosome/Scaffold: 570 Start: 22222 End: 27792 |
Description | Alpha amylase family protein |
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 | 410 | 736 | 4.3e-26 |
SDFTEKVLPHVKEAGYNAIQLIGVVEHKDYYTVGYRVTNFFAVSSRYGTPDDFKHLVDEAHGMGLLVFLEIVHSYAAADEMVGLSLFDGSNDCYFHTGKR GHHKFWGTRMFKYGDQEVLQFLLSNLNWWVEEYQIDGFQFHALSSMIYTHNGFASFTGDLEEYCNQYVDKEALQYLMFANELLHAIHPNIITIAEDATFY PGLCDPISQGGLGFDYYVNFSVPEMWLSFLQNVPAHEWSMSKIVSTLMDNKHYADKMLVYAENHNQSISGGQSFAEILIGETVDRSSDSEEVELRGCALL KMIKLITFTLSGGHAYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 900 Download |
MASVDSSTKI SLSLYPTESS PRFRSHSSFQ NISFPTKIRL AIKCSAANQP KQQHSKKRDK 60 NEEDEDKGVN PVGFLTRLGI THKQFAIFLR ERHKAYKDLK EDISKRQFMV KDLAYGHPEH 120 RMDFMDWAPG ARYGSVVGDF NDWSPTENAA REGLLGHDDY GYWFIVLEDK LREGEEPDEL 180 YFQQYNYLED YDKGDSGVSI DELFQKARDD YWEPGEDEYI KNRLKVPAKL YEQIFGPNGP 240 QTLEKLEEIP LKDAETRYKE WKEQHKDVPP SNLPPFDVID QGKEYDILNV VSDPAWLAKI 300 SSKDPPLPYW LEIRKGRKAW LKKYSPAVPH GSKYRVYYNT PDGQLERVPA WATYVQPDVN 360 GKQAYAVHWE PSPERAYKWK QTAPKVPTSL RIYECHVGIS GSEPKIASFS DFTEKVLPHV 420 KEAGYNAIQL IGVVEHKDYY TVGYRVTNFF AVSSRYGTPD DFKHLVDEAH GMGLLVFLEI 480 VHSYAAADEM VGLSLFDGSN DCYFHTGKRG HHKFWGTRMF KYGDQEVLQF LLSNLNWWVE 540 EYQIDGFQFH ALSSMIYTHN GFASFTGDLE EYCNQYVDKE ALQYLMFANE LLHAIHPNII 600 TIAEDATFYP GLCDPISQGG LGFDYYVNFS VPEMWLSFLQ NVPAHEWSMS KIVSTLMDNK 660 HYADKMLVYA ENHNQSISGG QSFAEILIGE TVDRSSDSEE VELRGCALLK MIKLITFTLS 720 GGHAYLNFMG NEFGHPKRVE FPVLSNNFSF SLANRQWDLL ENVGLHQHLF SFDKDLMRLG 780 ENQKAISRGL PNVHHVNDMA MVCSFPLLKT ANEEEGPLLF VFNFHPIDSH LTYSVGVEEA 840 GEYQIILNTD DDKYGGEGTI EAGKYVQKTI TGRVDGLRYC LQLQLPSRSG QVSRLVVVV* 900 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 2.0e-7 | 83 | 169 | 94 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 9.0e-177 | 373 | 774 | 408 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. | ||
PLN02960 | PLN02960 | 0 | 7 | 896 | 900 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 1 | 895 | 910 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 325 | 896 | 581 | + 1,4-alpha-glucan-branching enzyme |
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 |
GenBank | ABN05323.1 | 0 | 6 | 899 | 18 | 894 | putative starch branching enzyme [Populus trichocarpa] |
DDBJ | BAB02827.1 | 0 | 4 | 899 | 2 | 901 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 7 | 899 | 5 | 894 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 4 | 899 | 2 | 897 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002529457.1 | 0 | 7 | 892 | 6 | 892 | 1,4-alpha-glucan branching enzyme, 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 | 3amk_A | 0 | 326 | 860 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 326 | 860 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 326 | 860 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BF272517 | 278 | 347 | 624 | 0 |
JG636329 | 270 | 334 | 603 | 0 |
CO104525 | 273 | 374 | 646 | 0 |
DY965821 | 293 | 256 | 548 | 0 |
CA482990 | 226 | 117 | 342 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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